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Sample records for serum albumin scintigraphy

  1. [Protein losing enteropathy (PLE) detected by Tc99m-labelled human serum albumin abdominal scintigraphy--case report].

    Science.gov (United States)

    Hubalewska-Hoła, Alicja; Sowa-Staszczak, Anna; Szczerbiński, Tomasz; Lis, Grzegorz; Huszno, Bohdan; Szybiński, Zbigniew

    2003-01-01

    Protein losing enteropathy (PLE) is a gastrointestinal disorder that is associated with excessive loss of plasma protein into the gut resulting from abnormal mucosal permeability. The disease is usually caused by inflammation. The loss of protein in PLE is a nonselective process affecting albumin, globulin and transferrin. Abdominal scintigraphy with human serum albumin marked by Tc99m seems to be an easy and sensitive method for diagnosing PLE. An 4-year-old girl was presented to an outside Pediatric Department due to hypoproteinemia and recurrent pneumonia which had caused several prior hospitalizations. The laboratory tests revealed hypoproteinemia, hypoalbuminemia, low level of IgG, sideropenia, and a decreased level of T lymphocytes. The loss of protein into the gut was confirmed by fecal clearance of alfa-1 antitrypsin. Only nonspecific inflammation was detected by biopsy of the small intestine. These clinical and laboratory findings, quickly decreasing IgG and albumin levels in spite of i.v. supplementation and the lack of proteinuria permitted PLE diagnosis. The abdominal scintigraphy was planned to assess and localise protein losing through GIT and for strategy of possible surgical treatment. Abdominal dynamic scintigraphy was performed immediately after the injection of 300 MBq Tc99m human albumin. 90 images were taken within 180 minutes. Delayed abdominal images were obtained 6 and 24 hours after the tracer injection. Anterior abdominal scintigraphy showed pathological activity of Tc99m-albumin in small bowel in the upper left segment of the abdomen in the 40th minute after injection. Extensive accumulation of albumin was seen in the 160th minute. Delayed images, after 3 and 6 hours, revealed translocation of the tracer into the lower right abdominal segment. The further passage and tracer concentration was detected in ascendant and transverse colon. Based on the laboratory tests and scintigraphic images the girl was suspected to have segmental

  2. Imaging diagnosis of protein-losing enteropathy by 99mTc-labeled serum albumin

    International Nuclear Information System (INIS)

    Kashiwagi, Toru; Fukui, Hiroyuki; Jyokou, Takeshi

    1990-01-01

    Abdominal scintigraphy with intravenous injection of 99m Tc-labeled serum albumin was performed in 6 patients with protein-losing enteropathy (PLE) and 3 patients with nongastrointestinal tract disorders. In 3 out of 6 patients with PLE, abnormal radioactivity was observed in the ileum region 3 hours after injection, and thereafter clear colon image was obtained. In the remaining 3 patients, the colon was visualized 24 hours after injection. On the other hand, in all patients with nongastrointestinal tract disorders, no abnormal radioactivity was observed in the abdomen until 24 hours after injection. These results indicate that gastrointestinal protein loss could be demonstrated by scintigraphy with intravenously administered 99m Tc-labeled serum albumin. In one healthy subject, 99m Tc-labeled serum albumin was administered orally and abdominal scintigraphy was performed. Gastrointestinal tract image was only observed and no other image was demonstrated until 24 hours after oral administration. This result suggests that 99m Tc excreted into the gastrointestinal tract is not reabsorbed. Therefore, abdominal scintigraphy with 99m Tc-labeled serum albumin appears to be a simple and useful method for diagnosis of PLE. (author)

  3. Thallium-201 myocardial scintigraphy and cardiac pool scintigraphy with technetium-99m labelled human serum albumin of complicated anomalous heart

    International Nuclear Information System (INIS)

    Tanaka, Minoru; Watanabe, Takashi; Murase, Mitsuya; Shimizu, Ken; Abe, Toshio

    1979-01-01

    Nuclear cardiology has been used in the diagnosis of congenital heart disease, but these studies have not shown the dramatic increase that has occurred in their use in coronary heart disease. In this report, thallium-201 myocardial scintigraphy and cardiac pool scintigraphy with technetium-99m labelled human serum albumin of 13 patients with complicated congenital heart disease were compared with contrast angiography. The application of these scanning methods to visualization of the size and shape of ventricle and interventricular septum was very useful. At times these methods give us the more accurate information about cardiac shape, especially of complicated anomalous heart, than contrast angiography. Of course these methods will never replace cardiac catheterization and contrast angiography. But these studies are non-invasive. So it was concluded that these scanning methods had better be applied in patients with complicated cardiac anomaly before invasive contrast angiography. (author)

  4. Preoperative assessment of congestive liver dysfunction using technetium-99m galactosyl human Serum albumin liver scintigraphy in patients with severe valvular heart disease

    International Nuclear Information System (INIS)

    Nishi, Hiroyuki; Matsumiya, Goro; Takano, Hiroshi; Ichikawa, Hajime; Miyagawa, Shigeru; Sawa, Yoshiki; Takahashi, Toshiki

    2007-01-01

    Severe valvular heart disease is often complicated by congestive liver dysfunction, which greatly compromises the operative results. We evaluated congestive liver dysfunction by a novel approach using technetium-99m galactosyl human serum albumin ( 99m Tc-GSA) with liver scintigraphy. Between 1998 and 2004, we performed scintigraphy accompanied by 99m Tc-GSA in 28 patients who had valvular heart disease with moderate-to-severe tricuspid regurgitation and who showed symptoms of right heart failure. Based on the results, we calculated a receptor index (LHL15) and an index of blood clearance (HH15) and assessed the correlation between these factors and postoperative liver dysfunction, defined as the maximum serum total bilirubin level (max T-bil) as >2.0 mg/dl. Nineteen patients, including four who died in hospital, had postoperative liver dysfunction. The level of HH15 was significantly higher and the level of cholinesterase was significantly lower (P 99m Tc-GSA is a clinically useful predictor of postoperative liver dysfunction in patients with severe valvular disease. (author)

  5. First results of functional RES scintigraphy using sup(99m)-Tc-labeled human serum albumin millimicrospheres in progressive scleroderma: Possibility of early diagnosis of lung involvement

    International Nuclear Information System (INIS)

    Munz, D.L.; Altmeyer, P.; Ehrenheim, C.; Tuengerthal, S.; Holzmann, H.; Hoer, G.; Frankfurt Univ.

    1984-01-01

    Functional RES scintigraphy with sup(99m)Tc-labeled human serum albumin millimicrospheres (sup(99m)Tc-HSA-MM) was conducted in 11 female patients suffering from progressive scleroderma. The RES scan revealed abnormalities in the bone marrow in eight patients as well as pathological changes of the liver in 2 cases. 7 patients showed diffusely enhanced concentrations of sup(99m)Tc-HSA-MM in the lung, whereas X-ray picture and pulmonary function test revealed pathological findings in only 4 patients, respectively. Humoral inflammatory and immunologic parameters, too, indicated abnormalities less frequently than the lung scan. Thus functional RES scintigraphy seems to be a very sensitive approach to the assessment and possibly to the early diagnosis of lung involvement in progressive scleroderma. (orig.) [de

  6. First results of functional RES scintigraphy using sup(99m)-Tc-labeled human serum albumin millimicrospheres in progressive scleroderma: Possibility of early diagnosis of lung involvement

    Energy Technology Data Exchange (ETDEWEB)

    Munz, D.L.; Altmeyer, P.; Ehrenheim, C.; Tuengerthal, S.; Holzmann, H.; Hoer, G.

    1984-01-01

    Functional RES scintigraphy with sup(99m)Tc-labeled human serum albumin millimicrospheres (sup(99m)Tc-HSA-MM) was conducted in 11 female patients suffering from progressive scleroderma. The RES scan revealed abnormalities in the bone marrow in eight patients as well as pathological changes of the liver in 2 cases. 7 patients showed diffusely enhanced concentrations of sup(99m)Tc-HSA-MM in the lung, whereas X-ray picture and pulmonary function test revealed pathological findings in only 4 patients, respectively. Humoral inflammatory and immunologic parameters, too, indicated abnormalities less frequently than the lung scan. Thus functional RES scintigraphy seems to be a very sensitive approach to the assessment and possibly to the early diagnosis of lung involvement in progressive scleroderma.

  7. Diagnosis of Protein Losing Enteropathy in connective Tissue Diseases with 99mTc-human Serum Albumin(Hsa)

    International Nuclear Information System (INIS)

    Won, Kyoung Sook; Oh, Yeong Seok; Bang, Shin Ho; Park, Won

    1993-01-01

    Anterior abdominal scintigraphy after intravenous injection of 99m Tc-human serum albumin ( 99m Tc-HSA 20 mCi) was done in 16 patients with connective tissue diseases and 15 healthy control patients. Patients with proteinuria or hepatopathy were excluded. 1) 7(44%) patients among 16 connective tissue disease patients without the apparent evidence of external protein loss showed abnormal intestinal accumulation of albumin. 6 patients with positive albumin scintigraphy showed hypoalbuminaemia. 2) There was no false positive scintigraphic finding in control group. 3) The serum albumin level in connective tissue disease patients (3.1 ± 0.6 g/dl, n=16) was lower than control patients(3.9 ± 0.3 g/dl, n=15) (p 99m Tc-HSA scan(2.8 ± 0.6 g/dl, n=7) than the connective tissue disease patients with negative scan(3.3 ± 0.3 g/dl, n=9) (p 99m Tc-HSA scan also must be validated by more extended study and comparison with the quantitative study such as stool α -1 antitrypsin measurement. There must be a reevaluation of PLE in various diseases especially in connective tissue diseases with easy, fast, economical, and noninvasive method.

  8. DETERMINATION OF SERUM ALBUMIN WITH ...

    African Journals Online (AJOL)

    The reaction of tribromoarsenazo(TB-ASA) with serum albumin in the presence of emulgent OP was studied by spectrophotometry. In a Britton-Robinson buffer solution at pH 2.9, tribromoarsenazo and bovine serum albumin can immediately form a red compound in the presence of emulgent OP with a maximum absorption ...

  9. Serum albumin: accuracy and clinical use.

    Science.gov (United States)

    Infusino, Ilenia; Panteghini, Mauro

    2013-04-18

    Albumin is the major plasma protein and its determination is used for the prognostic assessment of several diseases. Clinical guidelines call for monitoring of serum albumin with specific target cut-offs that are independent of the assay used. This requires accurate and equivalent results among different commercially available methods (i.e., result standardization) through a consistent definition and application of a reference measurement system. This should be associated with the definition of measurement uncertainty goals based on medical relevance of serum albumin to make results reliable for patient management. In this paper, we show that, in the current situation, if one applies analytical goals for serum albumin measurement derived from its biologic variation, the uncertainty budget derived from each step of the albumin traceability chain is probably too high to fulfil established quality levels for albumin measurement and to guarantee the accuracy needed for clinical usefulness of the test. The situation is further worsened if non-specific colorimetric methods are used for albumin measurement as they represent an additional random source of uncertainty. Copyright © 2013 Elsevier B.V. All rights reserved.

  10. Immunologic relationships of human serum albumin, macroaggregated albumin, and albumin microspheres

    International Nuclear Information System (INIS)

    Stang, P.C.; Roelands, J.F.; Cohen, P.

    1975-01-01

    Antigenic relationships of NSA (normal serum albumin), MAA (macroaggregated albumin), and HAM (human albumin microspheres) were determined in vivo in guinea pigs and in vitro in gel diffusion plates. Results showed that HAM could sensitize but seldom elicit anaphylaxis when used to challenge guinea pigs. In contrast, NSA and MAA were strong sensitizing antigens and inducers of anaphylaxis. The relative inability of HAM to induce anaphylaxis suggests that during production of the microspheres from soluble albumin, antigenic determinants of albumin may be altered or masked. Consequently, these determinants may be less available to react with antibody at the tissue sites

  11. Serum albumin--a non-saturable carrier

    DEFF Research Database (Denmark)

    Brodersen, R; Honoré, B; Larsen, F G

    1984-01-01

    The shape of binding isotherms for sixteen ligands to human serum albumin showed no signs of approaching saturation at high ligand concentrations. It is suggested that ligand binding to serum albumin is essentially different from saturable binding of substrates to enzymes, of oxygen to haemoglobi...

  12. 2.6. Sorption of serum albumin by ethynyl-piperidol hydrogels

    International Nuclear Information System (INIS)

    Khalikov, D.Kh.

    2012-01-01

    The sorption of serum albumin by ethynyl-piperidol hydrogels was studied in this article. Albumins adsorption on the surface of solids was considered. The capacity of cross-linked ethynyl piperidol polymers to the serum albumin was considered as well. The kinetic curves of sorption of human serum albumin by triple copolymer of isopropenyl trimethyl ethynyl piperidol were constructed. Sorption activity of ethynyl-piperidol polymers depending on ph of solution of human serum albumin were defined. Influence of solution ionic strength on sorption of human serum albumin was defined as well. The desorption of human serum albumin from the complexes with hydrogels was examined.

  13. Quantitative determination of albumin in microlitre amounts of rat serum: With a short note on serum albumin levels in ageing rats

    NARCIS (Netherlands)

    Leeuw-Israel, F.R. de; Arp-Neefjes, J.M.; Hollander, C.F.

    1967-01-01

    A simple dye binding method for determining rat serum albumin, which employs the anionic dye 2-(4′-hydroxybenzneeazo) benzoic acid (HBABA) is described. Albumin in 5μ1 of serum is determined colorimetrically. Purified rat albumin is used as a primary standard and rat serum as a reference sample.

  14. Interaction of amphiphilic drugs with human and bovine serum albumins.

    Science.gov (United States)

    Khan, Abbul Bashar; Khan, Javed Masood; Ali, Mohd Sajid; Khan, Rizwan Hasan; Kabir-Ud-Din

    2012-11-01

    To know the interaction of amphiphilic drugs nortriptyline hydrochloride (NOT) and promazine hydrochloride (PMZ) with serum albumins (i.e., human serum albumin (HSA) and bovine serum albumin (BSA)), techniques of UV-visible, fluorescence, and circular dichroism (CD) spectroscopies are used. The binding affinity is more in case of PMZ with both the serum albumins. The quenching rate constant (k(q)) values suggest a static quenching process for all the drug-serum albumin interactions. The UV-visible results show that the change in protein conformation of PMZ-serum albumin interactions are more prominent as compared to NOT-serum albumin interactions. The CD results also explain the conformational changes in the serum albumins on binding with the drugs. The increment in %α-helical structure is slightly more for drug-BSA complexes as compared to drug-HSA complexes. Copyright © 2012 Elsevier B.V. All rights reserved.

  15. Structural studies on metal-serum albumin. 4

    International Nuclear Information System (INIS)

    Zhou Yongquia; Hu Xuying; Dou Chao; Liu Hong; Wang Sheyi; Shen Panwen

    1992-01-01

    There have been no detailed and reliable studies on the environment and configuration of Zn(II), Cd(II) and Hg(II) in the metal centers of human serum albumin and bovine serum albumin to date. In this paper the authentic evidence for the involvement of the cystinyl sulfur atoms in the ligation to the zinc group ions has been obtained from the X-ray photoelectron spectra. To belief that each of the zinc group ions possesses several binding sites in human- and bovine serum albumin and is bound to the deprotonated thiol group (-RS - ) of the cysteinyl residues to form tetrahedral and linear metal centers has been further confirmed by the treatment of ligand to metal charge transfer data with Jorgensen's method. According to these results, it was inferred that these binding sites may be located at the 17 disulfide bridges, most likely at the 7 pairs of adjacent disulfide bridges between positions 75 and 567, in the serum albumin. (author). 42 refs.; 5 figs

  16. Sucrose/bovine serum albumin mediated biomimetic crystallization

    Indian Academy of Sciences (India)

    To understand the role of the sucrose/bovine serum albumin system in the biomineralization process, we have tested the influence of different concentration of the sucrose/bovine serum albumin (BSA) on calcium carbonate (CaCO3) precipitation. The CaCO3 crystals were characterized by scanning electron microscope ...

  17. Production of biological nanoparticles from bovine serum albumin ...

    African Journals Online (AJOL)

    Production of biological nanoparticles from bovine serum albumin for drug delivery. ... Bovine serum albumin (BSA) was used for generation of nanoparticles in a drug delivery system. ... The impact of protein concentration and additional rate of organic solvent (i.e. ethanol) upon the particle ... AJOL African Journals Online.

  18. Determination of serum albumin with tribromoarsenazo by spectrophotometry

    Directory of Open Access Journals (Sweden)

    Qing-Zhou Zhai

    2007-08-01

    Full Text Available The reaction of tribromoarsenazo(TB-ASA with serum albumin in the presence of emulgent OP was studied by spectrophotometry. In a Britton-Robinson buffer solution at pH 2.9, tribromoarsenazo and bovine serum albumin can immediately form a red compound in the presence of emulgent OP with a maximum absorption wavelength at 354 nm. The presence of emulgent OP can increase the reaction sensitivity and the compound stability. The molar absorptivity of the compound is ε354 nm = 6.13 x 105 M-1•cm-1. Beer's law is obeyed over the range of 5.0-75.0 mg•L-1 for bovine serum albumin. The present method was applied to the determination of the total proteins in human serums with satisfactory results.

  19. Photochemistry of modified proteins benzophenone-containing bovine serum albumin

    International Nuclear Information System (INIS)

    Mariano, P.S.; Glover, G.I.; Wilkinson, T.J.

    1976-01-01

    The results of exploratory and mechanistic studies of the photochemistry of poly-p-benzoyl-acetimido-bovine serum albumin, a modified protein containing photoreactive and photosensitizing groups, are reported. Specifically described are recent findings concerning (1) the synthesis and characterization of a modified bovine serum albumin that contains benzophenone-like moieties, (2) the photochemistry of this modified protein which appeared to involve photoreductive coupling of the benzophenone chromophores to the protein backbone, and (3) triplet energy transfer from modified bovine serum albumin to small molecule acceptors resulting in quenching of the photoreaction. (author)

  20. Gamma-scintigraphy

    International Nuclear Information System (INIS)

    Desgrez, H.A.

    1960-06-01

    Gamma-scintigraphy is a medical technique making it possible to fix the image of certain organs after the concentration in these of emitting radioactive products. It is already widely used in the case of the thyroid gland with iodine-132 by applying the isotope iodine 131. The study of the liver and gall bladder is carried out using colloidal gold 198 and Bengal pink marked with iodine 131. Serum albumin marked with iodine 131 makes it possible to study rachidian blockages. Other applications can already be foreseen in this direction. (author) [fr

  1. Fluorescent investigation of the interactions between N-(p-chlorophenyl)-N'-(1-naphthyl) thiourea and serum albumin: Synchronous fluorescence determination of serum albumin

    International Nuclear Information System (INIS)

    Cui Fengling; Wang Junli; Cui Yanrui; Li Jianping

    2006-01-01

    The interactions between N-(p-chlorophenyl)-N'-(1-naphthyl) thiourea and serum albumin were investigated by fluorescence spectroscopy and UV absorption spectrum under physiological conditions. The results of spectroscopic measurements suggested that N-(p-chlorophenyl)-N'-(1-naphthyl) thiourea should have a strong ability to quench the intrinsic fluorescence of both bovine serum albumin and human serum albumin through static quenching procedure, and the hydrophobic interaction was the predominant intermolecular force stabilizing the complex. Thermodynamic parameter enthalpy changes (ΔH) and entropy changes (ΔS) were calculated according to the Vant'Hoff equation. The binding distances between N-(p-chlorophenyl)-N'-(1-naphthyl) thiourea and the proteins were evaluated on the basis of the theory of Foester energy transfer. In addition, the effects of other ions on the binding constants of complexes were also discussed. Synchronous fluorescence technology was successfully applied to the determination of serum albumins added to the CPNT solution

  2. Molecular Structure-Affinity Relationship of Flavonoids in Lotus Leaf (Nelumbo nucifera Gaertn.) on Binding to Human Serum Albumin and Bovine Serum Albumin by Spectroscopic Method.

    Science.gov (United States)

    Tang, Xiaosheng; Tang, Ping; Liu, Liangliang

    2017-06-23

    Lotus leaf has gained growing popularity as an ingredient in herbal formulations due to its various activities. As main functional components of lotus leaf, the difference in structure of flavonoids affected their binding properties and activities. In this paper, the existence of 11 flavonoids in lotus leaf extract was confirmed by High Performance Liquid Chromatography (HPLC) analysis and 11 flavonoids showed various contents in lotus leaf. The interactions between lotus leaf extract and two kinds of serum albumins (human serum albumin (HSA) and bovine serum albumin (BSA)) were investigated by spectroscopic methods. Based on the fluorescence quenching, the interactions between these flavonoids and serum albumins were further checked in detail. The relationship between the molecular properties of flavonoids and their affinities for serum albumins were analyzed and compared. The hydroxylation on 3 and 3' position increased the affinities for serum albumins. Moreover, both of the methylation on 3' position of quercetin and the C₂=C₃ double bond of apigenin and quercetin decreased the affinities for HSA and BSA. The glycosylation lowered the affinities for HSA and BSA depending on the type of sugar moiety. It revealed that the hydrogen bond force played an important role in binding flavonoids to HSA and BSA.

  3. Serum Albumin Predicts Long-Term Neurological Outcomes After Acute Spinal Cord Injury.

    Science.gov (United States)

    Tong, Bobo; Jutzeler, Catherine R; Cragg, Jacquelyn J; Grassner, Lukas; Schwab, Jan M; Casha, Steve; Geisler, Fred; Kramer, John L K

    2018-01-01

    There is a need to identify reliable biomarkers of spinal cord injury recovery for clinical practice and clinical trials. Our objective was to correlate serum albumin levels with spinal cord injury neurological outcomes. We performed a secondary analysis of patients with traumatic spinal cord injury (n = 591) participating in the Sygen clinical trial. Serum albumin concentrations were obtained as part of routine blood chemistry analysis, at trial entry (24-72 hours), 1, 2, and 4 weeks after injury. The primary outcomes were "marked recovery" and lower extremity motor scores, derived from the International Standards for the Neurological Classification of Spinal Cord Injury. Data were analyzed with multivariable logistic and linear regression to adjust for potential confounders. Serum albumin was significantly associated with spinal cord injury neurological outcomes. Higher serum albumin concentrations at 1, 2, and 4 weeks were associated with higher 52-week lower extremity motor score. Similarly, the odds of achieving "marked neurological recovery" was greater for individuals with higher serum albumin concentrations. The association between serum albumin concentrations and neurological outcomes was independent of initial injury severity, treatment with GM-1, and polytrauma. In spinal cord injury, serum albumin is an independent marker of long-term neurological outcomes. Serum albumin could serve as a feasible biomarker for prognosis at the time of injury and stratification in clinical trials.

  4. Fluorescent investigation of the interactions between N-(p-chlorophenyl)-N'-(1-naphthyl) thiourea and serum albumin: Synchronous fluorescence determination of serum albumin

    Energy Technology Data Exchange (ETDEWEB)

    Cui Fengling [School of Chemistry and Environmental Science, Key Laboratory for Environmental Pollution Control Technology of Henan Province, Henan Normal University, Xinxiang, Hennan 453007 (China)]. E-mail: fenglingcui@hotmail.com; Wang Junli [School of Chemistry and Environmental Science, Key Laboratory for Environmental Pollution Control Technology of Henan Province, Henan Normal University, Xinxiang, Hennan 453007 (China); Cui Yanrui [School of Chemistry and Environmental Science, Key Laboratory for Environmental Pollution Control Technology of Henan Province, Henan Normal University, Xinxiang, Hennan 453007 (China); Li Jianping [School of Chemistry and Environmental Science, Key Laboratory for Environmental Pollution Control Technology of Henan Province, Henan Normal University, Xinxiang, Hennan 453007 (China)

    2006-07-07

    The interactions between N-(p-chlorophenyl)-N'-(1-naphthyl) thiourea and serum albumin were investigated by fluorescence spectroscopy and UV absorption spectrum under physiological conditions. The results of spectroscopic measurements suggested that N-(p-chlorophenyl)-N'-(1-naphthyl) thiourea should have a strong ability to quench the intrinsic fluorescence of both bovine serum albumin and human serum albumin through static quenching procedure, and the hydrophobic interaction was the predominant intermolecular force stabilizing the complex. Thermodynamic parameter enthalpy changes ({delta}H) and entropy changes ({delta}S) were calculated according to the Vant'Hoff equation. The binding distances between N-(p-chlorophenyl)-N'-(1-naphthyl) thiourea and the proteins were evaluated on the basis of the theory of Foester energy transfer. In addition, the effects of other ions on the binding constants of complexes were also discussed. Synchronous fluorescence technology was successfully applied to the determination of serum albumins added to the CPNT solution.

  5. Structural changes during the unfolding of Bovine serum albumin

    Indian Academy of Sciences (India)

    The native form of serum albumin is the most important soluble protein in the body plasma. In order to investigate the structural changes of Bovine serum albumin (BSA) during its unfolding in the presence of urea, a small-angle neutron scattering (SANS) study was performed. The scattering curves of dilute solutions of BSA ...

  6. Serum Albumin Is Independently Associated with Persistent Organ Failure in Acute Pancreatitis

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    Wandong Hong

    2017-01-01

    Full Text Available Background and Aims. To investigate the association between serum albumin levels within 24 hrs of patient admission and the development of persistent organ failure in acute pancreatitis. Methods. A total of 700 patients with acute pancreatitis were enrolled. Multivariate logistic regression and subgroup analysis determined whether decreased albumin was independently associated with persistent organ failure and mortality. The diagnostic performance of serum albumin was evaluated by the area under Receiver Operating Characteristic (ROC curves. Results. As levels of serum albumin decrease, the risk of persistent organ failure significantly increases (Ptrend<0.001. The incidence of organ failure was 3.5%, 10.6%, and 41.6% in patients with normal albumin and mild and severe hypoalbuminaemia, respectively. Decreased albumin levels were also proportionally associated with prolonged hospital stay (Ptrend<0.001 and the risk of death (Ptrend<0.001. Multivariate analysis suggested that biliary etiology, chronic concomitant diseases, hematocrit, blood urea nitrogen, and the serum albumin level were independently associated with persistent organ failure. Blood urea nitrogen and the serum albumin level were also independently associated with mortality. The area under ROC curves of albumin for predicting organ failure and mortality were 0.78 and 0.87, respectively. Conclusion. A low serum albumin is independently associated with an increased risk of developing of persistent organ failure and death in acute pancreatitis. It may also be useful for the prediction of the severity of acute pancreatitis.

  7. Serum Albumin Levels and Economic Status in Japanese Older Adults.

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    Asami Ota

    Full Text Available Low serum albumin levels are associated with aging and medical conditions such as cancer, liver dysfunction, inflammation, and malnutrition and might be an independent predictor of long-term mortality in healthy older populations. We tested the hypothesis that economic status is associated with serum albumin levels and explained by nutritional and health status in Japanese older adults.We performed a cross-sectional analysis using data from the Japan Gerontological Evaluation study (JAGES. The study participants were 6528 functionally independent residents (3189 men and 3339 women aged ≥65 years living in four municipalities in Aichi prefecture. We used household income as an indicator of economic status. Multiple linear regression was used to compare serum albumin levels in relation to household income, which was classified as low, middle, and high. Additionally, mediation by nutritional and health-related factors was analyzed in multivariable models.With the middle-income group as reference, participants with low incomes had a significantly lower serum albumin level, even after adjustment for sex, age, residential area, education, marital status, and household structure. The estimated mean difference was -0.17 g/L (95% confidence interval, -0.33 to -0.01 g/L. The relation between serum albumin level and low income became statistically insignificant when "body mass index", "consumption of meat or fish", "self-rated health", "presence of medical conditions", "hyperlipidemia", or "respiratory disease "was included in the model.Serum albumin levels were lower in Japanese older adults with low economic status. The decrease in albumin levels appears to be mediated by nutrition and health-related factors with low household incomes. Future studies are needed to reveal the existence of other pathways.

  8. Potential Role of Amino Acid/Protein Nutrition and Exercise in Serum Albumin Redox State

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    Yasuaki Wada

    2017-12-01

    Full Text Available Albumin is the major protein in the serum of mammals. It is synthesized exclusively in the liver, before being secreted into the circulation. Similar to skeletal muscle protein, albumin synthesis is stimulated by dietary amino acids and proteins as well as exercise. Albumin has three isoforms based on the redox states of the free cysteine residue at position 34. The redox state of serum albumin has long been extensively investigated in terms of oxidative stress-related chronic diseases, with the redox state of serum albumin having been regarded as a marker of systemic oxidative stress. However, according to recent animal studies, the redox state of serum albumin is modulated by albumin turnover and may also reflect amino acid/protein nutritional status. Furthermore, as the redox state of serum albumin is modulated by exercise training, measuring the pre- and post-exercise redox states of serum albumin in athletes may be useful in assessing amino acid/protein nutritional status and exercise-induced oxidative stress, which are closely associated with skeletal muscle adaptive responses. This article extensively reviews serum albumin and the redox state of albumin in the context of amino acid/protein nutritional status and exercise training.

  9. Interaction between toxic azo dye C.I. Acid Red 88 and serum albumins

    International Nuclear Information System (INIS)

    Naveenraj, Selvaraj; Solomon, Rajadurai Vijay; Venuvanalingam, Ponnambalam; Asiri, Abdullah M.; Anandan, Sambandam

    2013-01-01

    Serum albumin-toxic dye interaction studies will be of paramount importance in the field of toxicology due to its relation towards the distribution and transportation of dye in blood. In this regard, the binding between C.I. Acid Red 88 (AR88) and serum albumins (HSA and BSA) was investigated by using combination of spectroscopic and molecular modeling methods. The fluorescence results revealed that AR88 interact with serum albumins through the combination of static and dynamic quenching mechanism. The distance “r” between serum albumin and AR88 was obtained according to the Forster resonance energy transfer (FRET) theory. Synchronous fluorescence and CD spectral results showed alterations in the microenvironment and conformation of serum albumins. The molecular docking method is also employed to understand the interaction of AR88 with serum albumins. All these studies confirm that BSA has more affinity towards AR88 than that of HSA which suggests that AR88 is more easily transported in the body of bovid than human and so it is more hazardous to bovids. -- Highlights: • AR88 interacts with serum albumin through the combination of both static and dynamic quenching mechanism. • The binding site of AR88 in serum albumins is nearer to tryptophan moiety. • Circular Dichroism spectra showed that AR88 alters α-helicity of serum albumin. • This interaction study could be greatly imperative for further investigations in toxicology

  10. Technetium-99m-Labeled Autologous Serum Albumin: A Personal-Exclusive Source of Serum Component

    OpenAIRE

    Wang, Yuh-Feng; Chen, Yi-Chun; Li, Dian-Kun; Chuang, Mei-Hua

    2011-01-01

    Technetium-99m human serum albumin (99mTc-HSA) is an important radiopharmaceutical required in nuclear medicine studies. However, the risk of transfusion-transmitted infection remains a major safety concern. Autopreparation of serum component acquired from patient provides a “personal-exclusive” source for radiolabeling. This paper is to evaluate the practicality of on-site elusion and subsequent radiolabeling efficacy for serum albumin. Results showed that the autologous elute contained more...

  11. Interaction of Citrinin with Human Serum Albumin

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    Miklós Poór

    2015-12-01

    Full Text Available Citrinin (CIT is a mycotoxin produced by several Aspergillus, Penicillium, and Monascus species. CIT occurs worldwide in different foods and drinks and causes health problems for humans and animals. Human serum albumin (HSA is the most abundant plasma protein in human circulation. Albumin forms stable complexes with many drugs and xenobiotics; therefore, HSA commonly plays important role in the pharmacokinetics or toxicokinetics of numerous compounds. However, the interaction of CIT with HSA is poorly characterized yet. In this study, the complex formation of CIT with HSA was investigated using fluorescence spectroscopy and ultrafiltration techniques. For the deeper understanding of the interaction, thermodynamic, and molecular modeling studies were performed as well. Our results suggest that CIT forms stable complex with HSA (logK ~ 5.3 and its primary binding site is located in subdomain IIA (Sudlow’s Site I. In vitro cell experiments also recommend that CIT-HSA interaction may have biological relevance. Finally, the complex formations of CIT with bovine, porcine, and rat serum albumin were investigated, in order to test the potential species differences of CIT-albumin interactions.

  12. Species dependence of [64Cu]Cu-Bis(thiosemicarbazone) radiopharmaceutical binding to serum albumins

    International Nuclear Information System (INIS)

    Basken, Nathan E.; Mathias, Carla J.; Lipka, Alexander E.; Green, Mark A.

    2008-01-01

    Introduction: Interactions of three copper(II) bis(thiosemicarbazone) positron emission tomography radiopharmaceuticals with human serum albumin, and the serum albumins of four additional mammalian species, were evaluated. Methods: 64 Cu-labeled diacetyl bis(N 4 -methylthiosemicarbazonato)copper(II) (Cu-ATSM), pyruvaldehyde bis(N 4 -methylthiosemicarbazonato)copper(II) (Cu-PTSM) and ethylglyoxal bis(thiosemicarbazonato)copper(II) (Cu-ETS) were synthesized and their binding to human, canine, rat, baboon and porcine serum albumins quantified by ultrafiltration. Protein binding was also measured for each tracer in human, porcine, rat and mouse serum. Results: The interaction of these neutral, lipophilic copper chelates with serum albumin is highly compound- and species-dependent. Cu-PTSM and Cu-ATSM exhibit particularly high affinity for human serum albumin (HSA), while the albumin binding of Cu-ETS is relatively insensitive to species. At HSA concentrations of 40 mg/ml, '% free' (non-albumin-bound) levels of radiopharmaceutical were 4.0±0.1%, 5.3±0.2% and 38.6±0.8% for Cu-PTSM, Cu-ATSM and Cu-ETS, respectively. Conclusions: Species-dependent variations in radiopharmaceutical binding to serum albumin may need to be considered when using animal models to predict the distribution and kinetics of these compounds in humans

  13. Interactions of serum albumins with antitumor agent benzo [a] phenazine-a spectroscopic study

    International Nuclear Information System (INIS)

    Sivakumar, Radhakrishnan; Naveenraj, Selvaraj; Anandan, Sambandam

    2011-01-01

    We present an investigation on the site specific interaction of antitumor agent benzo [a] phenazine (BAP) with serum albumins (HSA and BSA) and related photo-physical properties using absorption, emission and lifetime measurements. The absorption and emission measurements reveal that the binding of biomolecule benzo [a] phenazine took place near tryptophan moiety present in sub-domain IIA in serum albumins (HSA and BSA). In the selective excitation of benzo [a] phenazine at 365 nm, it was observed that the ground state of serum albumin quenches the excited benzo [a] phenazine through charge transfer exciplexation. The fluorescence decay analysis of serum albumins in the presence of benzo [a] phenazine shows decrease in lifetime, which confirms that photo-induced electron transfer takes place from serum albumins (HSA and BSA) to BAP. Also a suitable mechanism was proposed for the observed photo-induced electron transfer processes. Binding average distance (r) between the donor (serum albumins) and acceptor (benzo [a] phenazine) calculated using FRET theory confirmed their high probability of binding interaction. - Graphical Abstract: Highlights: → Benzo [a] phenazine (BAP) specifically bounds with tryptophan present in HSA and BSA. → Ground state of serum albumin quenches the excited BAP at 365 nm. → Lifetime of serum albumins decreases in the presence of BAP. → Photo-induced electron transfer from HSA and BSA to BAP takes place.

  14. Investigation of interactions between dendrimer-coated magnetite nanoparticles and bovine serum albumin

    International Nuclear Information System (INIS)

    Pan Bifeng; Gao Feng; Ao Limei

    2005-01-01

    We investigated the interactions between dendrimer-coated magnetite nanoparticles (MNPs) and the protein serum albumin. The investigation was based on the fluorescence quenching of tryptophan residue of serum albumin after binding with the dendrimer-coated magnetite nanoparticles. The extent of the interactions between bovine serum albumin and dendrimer-coated MNPs strongly depends on their surface groups and pH value

  15. Is serum albumin an independent predictor of post chemotherapy febrile neutropenia?

    International Nuclear Information System (INIS)

    Saleem, L.; Zahid, N.A.

    2017-01-01

    Objective: To evaluate the association between serum albumin and risk of post chemotherapy febrile neutropenia. Study Design: Cross sectional study. Place and Duration of Study: Department of oncology, Liaquat National Hospital, from 1st Jan 2015 to 31st Dec 2016. Material and Method: One hundred and sixty-six biopsy proven cancer patients with Eastern cooperative oncology group (ECOG) performance status <2 and without significant co-morbidities received first cycle of chemotherapy during two years study period. Different chemotherapies with moderate to severe risk of FN were used. Patient's pre-treatment serum albumin was measured and patients followed for occurrence of FN. Association between serum albumin and post chemotherapy FN was analyzed. Results: Data of 166 patients was available for final analysis. Post chemotherapy FN was observed in 19.9% (33/166) patients. Pre-chemotherapy serum albumin level was <3.5 mg/dl in (35/166) 21.1% of patients, out of which (15/35) 42.9% developed FN. Serum albumin (p=0.0005) was highly significantly associated with a risk of FN. On analysis of other factors age, gender, body surface area (BSA) and pre-chemotherapy hemoglobin level were not significantly associated with a risk of FN while body mass index (p=0.0005) was found to be associated with risk of FN. Conclusion: Pre-chemotherapy serum albumin levels were found to be statistically significant predictor of postchemotherapy febrile neutropenia.

  16. Spectroscopic analysis of the riboflavin-serum albumins interaction on silver nanoparticles

    Energy Technology Data Exchange (ETDEWEB)

    Voicescu, Mariana, E-mail: voicescu@icf.ro; Angelescu, Daniel G. [Institute of Physical Chemistry ' Ilie Murgulescu' , Romanian Academy (Romania); Ionescu, Sorana [University of Bucharest, Department of Physical Chemistry (Romania); Teodorescu, Valentin S. [Institute of Atomic Physics, National Institute of Materials Physics (Romania)

    2013-04-15

    Spectrophotometric behavior of riboflavin (RF) adsorbed on silver nanoparticles as well as its interaction with two serum albumins, BSA and HSA, respectively, has been evidenced. The time evolution of the plasmonic features of the complexes formed by RF/BSA/HSA and Ag(0) nanoparticles having an average diameter of 10.0 {+-} 2.0 nm have been investigated by UV-Vis absorption spectroscopy. Using steady-state and time-resolved fluorescence spectroscopy, the structure, stability, and dynamics of the serum albumins have been studied. The efficiency of energy transfer process between RF and serum albumins on silver nanoparticles has been estimated. A reaction mechanism of RF with silver nanoparticles is also proposed and the results are discussed with relevance to the involvement of the silver nanoparticles to the redox process of RF and to the RF-serum albumins interaction into a silver nanoparticles complex.

  17. Spectroscopic analysis of the riboflavin—serum albumins interaction on silver nanoparticles

    Science.gov (United States)

    Voicescu, Mariana; Angelescu, Daniel G.; Ionescu, Sorana; Teodorescu, Valentin S.

    2013-04-01

    Spectrophotometric behavior of riboflavin (RF) adsorbed on silver nanoparticles as well as its interaction with two serum albumins, BSA and HSA, respectively, has been evidenced. The time evolution of the plasmonic features of the complexes formed by RF/BSA/HSA and Ag(0) nanoparticles having an average diameter of 10.0 ± 2.0 nm have been investigated by UV-Vis absorption spectroscopy. Using steady-state and time-resolved fluorescence spectroscopy, the structure, stability, and dynamics of the serum albumins have been studied. The efficiency of energy transfer process between RF and serum albumins on silver nanoparticles has been estimated. A reaction mechanism of RF with silver nanoparticles is also proposed and the results are discussed with relevance to the involvement of the silver nanoparticles to the redox process of RF and to the RF-serum albumins interaction into a silver nanoparticles complex.

  18. Comparative scintigraphy in oleic acid pulmonary microvascular injury

    International Nuclear Information System (INIS)

    Sugerman, H.J.; Hirsch, J.I.; Tatum, J.L.; Strash, A.M.; Sharp, D.E.; Greenfield, L.J.

    1982-01-01

    Computerized gamma scintigraphy revealed a significant (p less than 0.001) rising lung:heart radioactivity ratio, which has been called ''slope of injury'' or ''slope index'', with both 99mTechnetium-tagged human serum albumin (99mTc-HSA) and 99mTechnetium-tagged red blood cells (99Tc-RBC) after 0.05 or 0.2 ml/kg iv oleic acid administration to dogs. This slope index was significantly greater with 99mTc-HSA than 99mTc-RBC (p less than 0.001). These findings verify that the scintigraphic 99mTc-HSA slope of injury is a result of a pulmonary capillary protein leak and not oleic acid induced changes in pulmonary blood or air volume. The leak of red blood cells noted with scintigraphy was confirmed by light microscopy and examination of the tracheal edema fluid. The leak of albumin, however, was much greater than the leak of red blood cells by microscopy and tracheal fluid examination, confirming the scintigraphic data. This study provides further evidence that computerized gamma scintigraphy will be of value for the diagnosis of permeability pulmonary edema and its response to treatment

  19. The relative role of serum albumin and urinary creatinine as ...

    African Journals Online (AJOL)

    Their weight, Body mass index, serum albumin and 24-hour urinary creatinine were determined before treatment, at the end of the 1st, 2nd, 4th and 6th month of treatment. Using ANOVA, the mean values of the weight, BIM and serum albumin were analysed with further analysis paired student T- test of the pre-treatment ...

  20. Design of compounds having enhanced tumour uptake, using serum albumin as a carrier. Pt. 2

    International Nuclear Information System (INIS)

    Schilling, U.; Friedrich, E.A.; Sinn, H.; Schrenk, H.H.; Clorius, J.H.; Maier-Borst, W.

    1992-01-01

    In the present in vivo study the uptake kinetics of radioiodinated albumin were determined in normal organs, and tumours of rats using sequential scintigraphy. Results indicate that cellular uptake of the marker takes place. Fluorescence was not observed in muscle tissue. This appears to suggest that the albumin uptake is greater in tumours than in normal tissue, and that it is metabolized in the tumour cells. (Author)

  1. Species dependence of [{sup 64}Cu]Cu-Bis(thiosemicarbazone) radiopharmaceutical binding to serum albumins

    Energy Technology Data Exchange (ETDEWEB)

    Basken, Nathan E. [Division of Nuclear Pharmacy, Department of Industrial and Physical Pharmacy, Purdue University, West Lafayette, IN 47907 (United States)], E-mail: nbasken@purdue.edu; Mathias, Carla J. [Division of Nuclear Pharmacy, Department of Industrial and Physical Pharmacy, Purdue University, West Lafayette, IN 47907 (United States); Lipka, Alexander E. [Department of Statistics, Purdue University, West Lafayette, IN 47907 (United States); Green, Mark A. [Division of Nuclear Pharmacy, Department of Industrial and Physical Pharmacy, Purdue University, West Lafayette, IN 47907 (United States)], E-mail: magreen@purdue.edu

    2008-04-15

    Introduction: Interactions of three copper(II) bis(thiosemicarbazone) positron emission tomography radiopharmaceuticals with human serum albumin, and the serum albumins of four additional mammalian species, were evaluated. Methods: {sup 64}Cu-labeled diacetyl bis(N{sup 4}-methylthiosemicarbazonato)copper(II) (Cu-ATSM), pyruvaldehyde bis(N{sup 4}-methylthiosemicarbazonato)copper(II) (Cu-PTSM) and ethylglyoxal bis(thiosemicarbazonato)copper(II) (Cu-ETS) were synthesized and their binding to human, canine, rat, baboon and porcine serum albumins quantified by ultrafiltration. Protein binding was also measured for each tracer in human, porcine, rat and mouse serum. Results: The interaction of these neutral, lipophilic copper chelates with serum albumin is highly compound- and species-dependent. Cu-PTSM and Cu-ATSM exhibit particularly high affinity for human serum albumin (HSA), while the albumin binding of Cu-ETS is relatively insensitive to species. At HSA concentrations of 40 mg/ml, '% free' (non-albumin-bound) levels of radiopharmaceutical were 4.0{+-}0.1%, 5.3{+-}0.2% and 38.6{+-}0.8% for Cu-PTSM, Cu-ATSM and Cu-ETS, respectively. Conclusions: Species-dependent variations in radiopharmaceutical binding to serum albumin may need to be considered when using animal models to predict the distribution and kinetics of these compounds in humans.

  2. The role of albumin conformation in the binding of diazepam to human serum albumin

    NARCIS (Netherlands)

    Wilting, J.; Hart, B.J. 't; Gier, J.J. de

    2006-01-01

    The effect of hydrogen, chloride and calcium ions on the binding of diazepare to human serum albumin has been studied by circular dichroism and equilibrium dialysis. In all cases the molar ellipticity of the diazepam-albumin complex increases with pH over the pH range 5 to 9. Under these

  3. Quantification of carbamylated albumin in serum based on capillary electrophoresis.

    Science.gov (United States)

    Delanghe, Sigurd; Moerman, Alena; Pletinck, Anneleen; Schepers, Eva; Glorieux, Griet; Van Biesen, Wim; Delanghe, Joris R; Speeckaert, Marijn M

    2017-09-01

    Protein carbamylation, a nonenzymatic posttranslational modification promoted during uremia, is linked to a poor prognosis. In the present study, carbamylation of serum albumin was assayed using the symmetry factor on a capillary electrophoresis instrument (Helena V8). The symmetry factor has been defined as the distance from the center line of the peak to the back slope, divided by the distance from the center line of the peak to the front slope, with all measurements made at 10% of the maximum peak height. Serum albumin, creatinine, and urea concentrations were assayed using routine methods, whereas uremic toxins were determined using HPLC. In vitro carbamylation induced a marked albumin peak asymmetry. Reference values for the albumin symmetry factor were 0.69-0.92. In kidney patients, albumin peak asymmetry corresponded to the chronic kidney disease stage (p < 0.0001). The symmetry factor correlated well with serum urea (r = -0.5595, p < 0.0001) and creatinine (r = -0.5986, p < 0.0001) concentrations. Several protein-bound uremic toxins showed a significant negative correlation with the symmetry factor. Morphology of the albumin fraction was not affected by presence of glycated albumin and protein-bound antibiotics. In conclusion, the presented method provides a simple, practical way for monitoring protein carbamylation. © 2017 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

  4. Nanoparticles of Conjugated Methotrexate-Human Serum Albumin: Preparation and Cytotoxicity Evaluations

    Directory of Open Access Journals (Sweden)

    Azade Taheri

    2011-01-01

    Full Text Available Methotrexate-human serum albumin conjugates were developed by a simple carbodiimide reaction. Methotrexate-human serum albumin conjugates were then crosslinked with 1-ethyl-3-(3-dimethylaminopropyl carbodiimide HCl (EDC to form nanoparticles. The size of nanoparticles determined by laser light scattering and TEM was between 90–150 nm. Nanoparticles were very stable at physiologic conditions (PBS pH 7.4, 37∘C and after incubation with serum. The effect of amount of EDC used for crosslinking on the particle size and free amino groups of nanoparticles was examined. The amount of crosslinker showed no significant effect on the size of nanoparticles but free amino groups of nanoparticles were decreased by increasing the crosslinker. The physicochemical interactions between methotrexate and human serum albumin were investigated by differential scanning calorimetry (DSC. Nanoparticles were more cytotoxic on T47D cells compared to free methotrexate. Moreover, methotrexate-human serum albumin nanoparticles decreased the IC50 value of methotrexate on T47D cells in comparison with free methotrexate.

  5. Nanoparticles of Conjugated Methotrexate-Human Serum Albumin: Preparation and Cytotoxicity Evaluations

    International Nuclear Information System (INIS)

    Taheri, A.; Atyabi, F.; Nouri, F.S.; Ahadi, F.; Derakhshan, M.A.; Dinarvand, R.; Atyabi, F.; Ghahremani, M.H.; Ostad, S.N.; Dinarvand, R.; Amini, M.; Ghahremani, M.H.; Ostad, S.N.; Mansoori, P.

    2011-01-01

    Methotrexate-human serum albumin conjugates were developed by a simple carbodiimide reaction. Methotrexate-human serum albumin conjugates were then crosslinked with 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide HCl (EDC) to form nanoparticles. The size of nanoparticles determined by laser light scattering and TEM was between 90 150 nm. Nanoparticles were very stable at physiologic conditions (PBS pH 7.4, 37 degree C) and after incubation with serum. The effect of amount of EDC used for crosslinking on the particle size and free amino groups of nanoparticles was examined. The amount of cross linker showed no significant effect on the size of nanoparticles but free amino groups of nanoparticles were decreased by increasing the cross linker. The physicochemical interactions between methotrexate and human serum albumin were investigated by differential scanning calorimetry (DSC). Nanoparticles were more cytotoxic on T 47 D cells compared to free methotrexate. Moreover, methotrexate-human serum albumin nanoparticles decreased the C50 value of methotrexate on T 47 D cells in comparison with free methotrexate.

  6. SPECTROPHOTOMETRIC ANALYSIS OF BOVINE SERUM ALBUMIN IN PRESENCE OF SOME BISCHALCONES

    OpenAIRE

    Shweta Garg; Mamta Singh; N. Raghav

    2013-01-01

    We have synthesized a series of bischalcones by the Claisen-Schmidt condensation and their effect was observed on bovine serum albumin. We have found that the synthesized bischalcones interacted with bovine serum albumin irrespective of the nature and position of the substituent with a little difference.

  7. Age and sex variation in serum albumin concentration: an observational study.

    Science.gov (United States)

    Weaving, Gary; Batstone, Gifford F; Jones, Richard G

    2016-01-01

    In the UK, a common reference interval for serum albumin is widely used irrespective of age or sex. Implicit in this is that laboratories produce analytically similar results. This paper challenges the validity of this approach. A three-week collection of results sent to all primary care centres in England has been analysed by age, sex and laboratory. In all, 1,079,193 serum albumin reports were included in this analysis. The mean population serum albumin concentration increases to peak at around age 20 years and then decreases with increasing age. Values in females decrease more rapidly but become close to male values at 60 years. The variation between laboratories was large and potentially clinically significant. Reference intervals for serum albumin should be stratified by age and sex. Until there is greater methodological standardization, laboratories should determine their own reference intervals and not accept a single consensus reference interval. © The Author(s) 2015.

  8. Correlation between serum albumin, prealbumin and ventilator dependence in patients with COPD

    Directory of Open Access Journals (Sweden)

    Shu-Miao Wu

    2016-04-01

    Full Text Available Objective: To investigate the correlation between the serum albumin, prealbumin and ventilator dependence in patients with COPD. Methods: Serum albumin and prealbumin of 44 COPD patients using breathing machine>48 h were tested at admission, 1 week, 2 weeks treatment. According to the existence of ventilator dependence, divided the patients into the ventilator dependence group and the ventilator independence group, compare the albumin, prealbumin average of two groups, evaluate the correlation between the serum albumin, prealbumin and ventilator dependence in patients with COPD. Results: Albumin levels reduced in both groups after 1 week treatment, but there was no statistically significant difference. Albumin levels reduced in both groups after 2 weeks treatment, but more significantly in the ventilator dependence group, the difference had statistical significance. Prealbumin levels in the ventilator independence group after 1 week treatment didn’t reduced, but reduced in the ventilator dependence group, the difference was statistically significant. Prealbumin levels reduced in both groups after 2 weeks treatment, but more significant in the ventilator dependence group, the difference had statistical significance. Conclusion: Serum albumin and prealbumin levels were correlation with the ventilator dependence in patients with COPD. But prealbumin can more sensitively and more early predict the ventilator dependence in patients with COPD suffered from malnutrition.

  9. Relationship Between Serum Adiponectin and Urinary Albumin Excretion Rate in Patients with Diabetes Nephropathy

    International Nuclear Information System (INIS)

    Duan Yongqiang; Yu Hui; Wang Zuobing

    2010-01-01

    To explore the relationship between the levels of serum adiponectin and urinary albumin excretion rate in patients with type 2 diabetes nephropathy, the serum levels of adiponectin and the levels of urinary albumin excretion rate in diabetes patients before and after treatment with pioglitazone were tested by ELISA and automatic biochemical analyzer respectively. The results showed that the serum levels of adiponectin in DM and DN group were lower than that of normal controls(P<0.01), but they gradually increased with progression (P<0.01). The serum adiponectin level was positively correlated with urinary albumin excretion rate (r= 0.284, P<0.05). The urinary albumin level decreased (P<0.01) and the serum levels of adiponectin increased after treatment with pioglitazone in DN group. The serum levels of adiponectin and urinary albumin excretion rate may play important role in the indication of treatment of diabetes. (authors)

  10. Serum albumin coating of demineralized bone matrix results in stronger new bone formation.

    Science.gov (United States)

    Horváthy, Dénes B; Vácz, Gabriella; Szabó, Tamás; Szigyártó, Imola C; Toró, Ildikó; Vámos, Boglárka; Hornyák, István; Renner, Károly; Klára, Tamás; Szabó, Bence T; Dobó-Nagy, Csaba; Doros, Attila; Lacza, Zsombor

    2016-01-01

    Blood serum fractions are hotly debated adjuvants in bone replacement therapies. In the present experiment, we coated demineralized bone matrices (DBM) with serum albumin and investigated stem cell attachment in vitro and bone formation in a rat calvaria defect model. In the in vitro experiments, we observed that significantly more cells adhere to the serum albumin coated DBMs at every time point. In vivo bone formation with albumin coated and uncoated DBM was monitored biweekly by computed tomography until 11 weeks postoperatively while empty defects served as controls. By the seventh week, the bone defect in the albumin group was almost completely closed (remaining defect 3.0 ± 2.3%), while uncoated DBM and unfilled control groups still had significant defects (uncoated: 40.2 ± 9.1%, control: 52.4 ± 8.9%). Higher density values were also observed in the albumin coated DBM group. In addition, the serum albumin enhanced group showed significantly higher volume of newly formed bone in the microCT analysis and produced significantly higher breaking force and stiffness compared to the uncoated grafts (peak breaking force: uncoated: 15.7 ± 4 N, albumin 46.1 ± 11 N). In conclusion, this investigation shows that implanting serum albumin coated DBM significantly reduces healing period in nonhealing defects and results in mechanically stronger bone. These results also support the idea that serum albumin coating provides a convenient milieu for stem cell function, and a much improved bone grafting success can be achieved without the use of exogenous stem cells. © 2015 Wiley Periodicals, Inc.

  11. Early Identification of the Patient with Endotheliopathy of Trauma by Arrival Serum Albumin

    DEFF Research Database (Denmark)

    Rodriguez, Erika Gonzalez; Cardenas, Jessica C; Lopez, Ernesto

    2017-01-01

    OBJECTIVE: Traumatic endotheliopathy (EoT) is associated with glycocalyx breakdown and capillary leak resulting in the extravasation of proteins. We hypothesized that lower serum albumin levels are associated with EoT, poor outcomes, and can be used for early EoT screening in trauma patients. MET...... with leakage of albumin from the intravascular compartment, which reemphasizes that arrival albumin may be a novel and timely approach to the identification of patients needing endothelial rescue therapy.......OBJECTIVE: Traumatic endotheliopathy (EoT) is associated with glycocalyx breakdown and capillary leak resulting in the extravasation of proteins. We hypothesized that lower serum albumin levels are associated with EoT, poor outcomes, and can be used for early EoT screening in trauma patients....... METHODS: We enrolled severely injured trauma patients with serum albumin levels available on admission. Syndecan-1 and soluble thrombomodulin were quantified from plasma by ELISA. Demographic and clinical data were obtained. We evaluated the association of serum albumin and EoT+ (syndecan-1 level ≥40 ng...

  12. Effects of non-enzymatic glycation in human serum albumin. Spectroscopic analysis

    Science.gov (United States)

    Szkudlarek, A.; Sułkowska, A.; Maciążek-Jurczyk, M.; Chudzik, M.; Równicka-Zubik, J.

    2016-01-01

    Human serum albumin (HSA), transporting protein, is exposed during its life to numerous factors that cause its functions become impaired. One of the basic factors - glycation of HSA - occurs in diabetes and may affect HSA-drug binding. Accumulation of advanced glycation end-products (AGEs) leads to diseases e.g. diabetic and non-diabetic cardiovascular diseases, Alzheimer disease, renal disfunction and in normal aging. The aim of the present work was to estimate how non-enzymatic glycation of human serum albumin altered its tertiary structure using fluorescence technique. We compared glycated human serum albumin by glucose (gHSAGLC) with HSA glycated by fructose (gHSAFRC). We focused on presenting the differences between gHSAFRC and nonglycated (HSA) albumin used acrylamide (Ac), potassium iodide (KI) and 2-(p-toluidino)naphthalene-6-sulfonic acid (TNS). Changes of the microenvironment around the tryptophan residue (Trp-214) of non-glycated and glycated proteins was investigated by the red-edge excitation shift method. Effect of glycation on ligand binding was examined by the binding of phenylbutazone (PHB) and ketoprofen (KP), which a primary high affinity binding site in serum albumin is subdomain IIA and IIIA, respectively. At an excitation and an emission wavelength of λex 335 nm and λem 420 nm, respectively the increase of fluorescence intensity and the blue-shift of maximum fluorescence was observed. It indicates that the glycation products decreases the polarity microenvironment around the fluorophores. Analysis of red-edge excitation shift method showed that the red-shift for gHSAFRC is higher than for HSA. Non-enzymatic glycation also caused, that the Trp residue of gHSAFRC becomes less accessible for the negatively charged quencher (I-), KSV value is smaller for gHSAFRC than for HSA. TNS fluorescent measurement demonstrated the decrease of hydrophobicity in the glycated albumin. KSV constants for gHSA-PHB systems are higher than for the unmodified serum

  13. Polymerized soluble venom--human serum albumin

    International Nuclear Information System (INIS)

    Patterson, R.; Suszko, I.M.; Grammer, L.C.

    1985-01-01

    Extensive previous studies have demonstrated that attempts to produce polymers of Hymenoptera venoms for human immunotherapy resulted in insoluble precipitates that could be injected with safety but with very limited immunogenicity in allergic patients. We now report soluble polymers prepared by conjugating bee venom with human serum albumin with glutaraldehyde. The bee venom-albumin polymer (BVAP) preparation was fractionated on Sephacryl S-300 to have a molecular weight range higher than catalase. 125 I-labeled bee venom phospholipase A was almost completely incorporated into BVAP. Rabbit antibody responses to bee venom and bee venom phospholipase A were induced by BVAP. Human antisera against bee venom were absorbed by BVAP. No new antigenic determinants on BVAP were present as evidenced by absorption of antisera against BVAP by bee venom and albumin. BVAP has potential immunotherapeutic value in patients with anaphylactic sensitivity to bee venom

  14. Study on the interaction of bovine serum albumin and fleroxacin by fluorescence method

    International Nuclear Information System (INIS)

    Nie Lihua; Zhao Huichun; Wang Xuebin; Wang Xu

    2001-01-01

    A fluorescence method is used to study the fluorescence quenching of bovine serum albumin by its interaction with fleroxacin. The interaction association constants of bovine serum albumin and fleroxacin are determined from a double reciprocal Lineweaver-Burk plot. According to the Foester dipole-dipole energy transfer, the distance to be measured between the fleroxacin and tryptophane is 4.37 nm. From thermodynamical coordination it can be judged that the binding power between fleroxacin and bovine serum albumin is static electric power

  15. Crystals of Serum Albumin for Use in Genetic Engineering and Rational Drug Design

    Science.gov (United States)

    Carter, Daniel C. (Inventor)

    1996-01-01

    Serum albumin crystal forms have been produced which exhibit superior x-ray diffraction quality. The crystals are produced from both recombinant and wild-type human serum albumin, canine, and baboon serum albumin and allow the performance of drug-binding studies as well as genetic engineering studies. The crystals are grown from solutions of polyethylene glycol or ammonium sulphate within prescribed limits during growth times from one to several weeks and include the following space groups: P2(sub 1), C2, P1.

  16. Superior serum half life of albumin tagged TNF ligands

    International Nuclear Information System (INIS)

    Mueller, Nicole; Schneider, Britta; Pfizenmaier, Klaus; Wajant, Harald

    2010-01-01

    Due to their immune stimulating and apoptosis inducing properties, ligands of the TNF family attract increasing interest as therapeutic proteins. A general limitation of in vivo applications of recombinant soluble TNF ligands is their notoriously rapid clearance from circulation. To improve the serum half life of the TNF family members TNF, TWEAK and TRAIL, we genetically fused soluble variants of these molecules to human serum albumin (HSA). The serum albumin-TNF ligand fusion proteins were found to be of similar bioactivity as the corresponding HSA-less counterparts. Upon intravenous injection (i.v.), serum half life of HSA-TNF ligand fusion proteins, as determined by ELISA, was around 15 h as compared to approximately 1 h for all of the recombinant control TNF ligands without HSA domain. Moreover, serum samples collected 6 or 24 h after i.v. injection still contained high TNF ligand bioactivity, demonstrating that there is only limited degradation/inactivation of circulating HSA-TNF ligand fusion proteins in vivo. In a xenotransplantation model, significantly less of the HSA-TRAIL fusion protein compared to the respective control TRAIL protein was required to achieve inhibition of tumor growth indicating that the increased half life of HSA-TNF ligand fusion proteins translates into better therapeutic action in vivo. In conclusion, our data suggest that genetic fusion to serum albumin is a powerful and generally applicable mean to improve bioavailability and in vivo activity of TNF ligands.

  17. Is low serum albumin associated with postoperative complications in patients undergoing oesophagectomy for oesophageal malignancies?

    Science.gov (United States)

    Goh, Sean L; De Silva, Ramesh P; Dhital, Kumud; Gett, Rohan M

    2015-01-01

    A best evidence topic was written according to a structured protocol. The question addressed was: in patients undergoing oesophagectomy for oesophageal malignancy, is low serum albumin associated with postoperative complications? Altogether, 87 papers were found using the reported search, of which 16 demonstrated the best evidence to answer the clinical question. The authors, journal, date and country of publication, patient group studied, study type, relevant outcomes and results of these papers are tabulated. This paper includes 2 level 2 papers, 12 level 3 papers and 2 level 4 papers. All the papers compared either all or some of the following postoperative complications: mortality, morbidity, anastomotic leak, respiratory and non-respiratory complications, and length of hospital stay. Eleven of the 16 papers found an association between low serum albumin and postoperative complications. Of these, one study showed that low serum albumin combined with low fibrinogen levels (FA score) was predictive of postoperative recurrence of oesophageal cancer. Another study showed that when combined with white cell count and C-reactive protein (CRP, NUn score), serum albumin had a high diagnostic accuracy for major complications after postoperative day 3. The largest study compared the in-hospital mortality in 7227 patients who underwent oesophageal surgery for malignancy. The percentage of in-hospital mortality was associated with low serum albumin (35.0 g/l, 21.0 vs 11.3%, P papers found no significant association between low serum albumin and postoperative complications. Of these papers, one showed that low serum albumin was not an independent risk factor, while four others found no association between low serum albumin with respiratory complications, anastomotic leak and postoperative mortality. Instead, these studies found other factors responsible for postoperative complications such as: CRP, smoking, disease duration, malnutrition and low T-cell levels. Taken together

  18. A DSC study of zinc binding to bovine serum albumin (BSA

    Directory of Open Access Journals (Sweden)

    SANJA OSTOJIC

    2007-04-01

    Full Text Available The thermal denaturation of bovine serum albumin (BSA is a kinetically and thermodynamically controlled process. The effects of zinc binding to bovine serum albumin (BSA, followed by differential scanning calorimetry (DSC, were investigated in this work, with the purpose of obtaining a better understanding of the albumin/zinc interaction. From the DSC curves, the thermodynamic parameters of protein denaturation were obtained, i.e., the temperature of thermal transition maximum (Tm, calorimetric enthalpy (DHcal, van't Hoff enthalpy (DHvH, the number of binding sites (I, II, the binding constants for each binding site (KbI, KbII and the average number of ligands bound per mole of native protein XN. The thermodynamic data of protein unfolding showed that zinc binding to bovine serum albumin increases the stability of the protein (higher values of DHcal and the different ratio DHcal/DHvH indicates the perturbation of the protein during thermal denaturation.

  19. Molecular basis of indomethacin-human serum albumin interaction

    DEFF Research Database (Denmark)

    Trivedi, V D; Vorum, H; Honoré, B

    1999-01-01

    Studies on the strength and extent of binding of the non-steroidal anti-inflammatory drug indomethacin to human serum albumin (HSA) have provided conflicting results. In the present work, the serum-binding of indomethacin was studied in 55 mM sodium phosphate buffer (pH 7.0) at 28 degrees C, by u...

  20. A comparative study of some physico-chemical properties of human serum albumin samples from different sources--I : Some physico-chemical properties of isoionic human serum albumin solutions

    NARCIS (Netherlands)

    Dröge, J.H.M.; Janssen, L.H.M.; Wilting, J.

    1982-01-01

    Human serum albumin samples from different sources were investigated. The fatty acid content of the albumin before and after deionization on a mixed bed ion-exchange column varied from sample to sample. When an albumin sample from one source was deionized under standard conditions the amount of

  1. Polymerized soluble venom--human serum albumin

    Energy Technology Data Exchange (ETDEWEB)

    Patterson, R.; Suszko, I.M.; Grammer, L.C.

    1985-03-01

    Extensive previous studies have demonstrated that attempts to produce polymers of Hymenoptera venoms for human immunotherapy resulted in insoluble precipitates that could be injected with safety but with very limited immunogenicity in allergic patients. We now report soluble polymers prepared by conjugating bee venom with human serum albumin with glutaraldehyde. The bee venom-albumin polymer (BVAP) preparation was fractionated on Sephacryl S-300 to have a molecular weight range higher than catalase. /sup 125/I-labeled bee venom phospholipase A was almost completely incorporated into BVAP. Rabbit antibody responses to bee venom and bee venom phospholipase A were induced by BVAP. Human antisera against bee venom were absorbed by BVAP. No new antigenic determinants on BVAP were present as evidenced by absorption of antisera against BVAP by bee venom and albumin. BVAP has potential immunotherapeutic value in patients with anaphylactic sensitivity to bee venom.

  2. Interaction of carbon nanoparticles to serum albumin: elucidation of the extent of perturbation of serum albumin conformations and thermodynamical parameters

    Energy Technology Data Exchange (ETDEWEB)

    Mandal, Samir [Molecular and Human Genetics Division, CSIR-Indian Institute of Chemical Biology, Kolkata 700032 (India); Hossain, Maidul [Biophysical Chemistry Laboratory, CSIR-Indian Institute of Chemical Biology, Kolkata 700032 (India); Devi, P. Sujatha [Nano-Structured Materials Division, CSIR-Central Glass and Ceramic Research Institute, Kolkata 700032 (India); Kumar, Gopinatha Suresh [Biophysical Chemistry Laboratory, CSIR-Indian Institute of Chemical Biology, Kolkata 700032 (India); Chaudhuri, Keya, E-mail: keya.chaudhuri@gmail.com [Molecular and Human Genetics Division, CSIR-Indian Institute of Chemical Biology, Kolkata 700032 (India)

    2013-03-15

    Highlights: ► Strong interaction of serum albumins to CNPs and potential toxicity. ► Partial unfolding and alteration of BSA and HSA secondary structure by CNP. ► Significant insight into design of nanoparticles in biomedical applications. -- Abstract: Carbon nanoparticles continuously generated from industries and vehicles due to incomplete combustion of fuels is one of the potent causes of air pollution. The exposure of this polluted air with carbon nanoparticles, introduced into the bloodstream of animals in the course of respiration, motivated us to study their interaction with plasma proteins, bovine serum albumin and human serum albumin. Carbon nanoparticles with very small size and high purity were synthesized by dehydration of D-glucose using concentrated sulphuric acid as dehydrating agent. These were characterized by transmission electron microscopy, atomic force microscopy, X-ray diffraction, Raman spectroscopy, FTIR spectroscopy and UV–visible spectroscopy. Carbon nanoparticles-protein interactions were studied by fluorescence spectroscopy, circular dichroism spectroscopy and isothermal titration calorimetry. The fluorescence quenching constants and thermodynamic parameters such as enthalpy change (ΔH°), entropy change (ΔS°) and free energy change (ΔG°) were calculated, which indicated a strong static quenching and primary electrostatic interaction between the carbon nanoparticles and blood proteins. Circular dichroism spectra provided the information about the secondary structure alteration of the proteins in presence of carbon nanoparticles. These findings have shed light towards an understanding of the interactions between carbon nanoparticles and serum proteins which may clarify the potential risks and undesirable health effects of carbon nanoparticles, as well as the related cellular trafficking and systemic translocation.

  3. Worse Neurological State During Acute Ischemic Stroke is Associated with a Decrease in Serum Albumin Levels.

    Science.gov (United States)

    Bielewicz, Joanna; Kurzepa, Jacek; Czekajska-Chehab, Elżbieta; Kamieniak, Piotr; Daniluk, Beata; Bartosik-Psujek, Halina; Rejdak, Konrad

    2016-04-01

    High serum albumin levels during ischemic stroke (IS) decrease the risk of a poor outcome. This study aimed to determine whether serum albumin levels within the first days after IS correlate with radiological and biochemical markers of brain tissue damage. Fifty-six IS patients were enrolled into the study. Neurological examinations were based on the National Institute of Health Stroke Scale. Serum albumin levels and S100BB were evaluated using commercially available ELISA kits. The albumin decrease index (ADI) was calculated as the difference between serum albumin levels measured on days 1 and 10 of IS. All parameters were estimated on the 1st, 3rd, 5th, and 10th days of IS, and the volume of ischemic focus was measured on the 10th day. Mean serum albumin levels were decreased during acute IS. There were correlations between the ADI and mean S100BB serum levels (r = 0.36, p albumin levels during the acute phase of IS corresponds to a worse neurological state as a result of a large ischemic focus with intense catabolic processes.

  4. Assessment of hepatic functional reserve for hepatic resection using 99mTc-PMT scintigraphy in comparison with 99mTc-GSA scintigraphy

    International Nuclear Information System (INIS)

    Sakuma, Atsushi

    2000-01-01

    99m Tc-diethylenetriamine-pentaacetic acid-galactosyl human serum albumin( 99m Tc-GSA) scintigraphy has been reported as a useful study of hepatic functional reserve recently. We have performed 99m Tc-N-pyridoxyl-5-methyl-tryptophan( 99m Tc-PMT) and 99m Tc-GSA preoperatively for evaluation of hepatic functional reserve and compared the usefulness of those scintigraphy study. Twenty-four patients who were the candidates of hepatic resection underwent 99m Tc-PMT scintigraphy preoperatively. Hepatic blood flow coefficient (K value), the amount of hepatic blood flow (HBF), and the ratio of portal blood flow (PVR) were computed. 99m Tc-GSA scintigraphy was also performed within two weeks of the 99m Tc-PMT scintigraphy, and the ratio of disappearance (HH 15 ) and the hepatic uptake ratio (LHL 15 ) were computed. The relationship between K value, HBF, PVR, HH 15 and LHL 15 was analyzed. Their correlation with other liver function tests was also examined. K value and HBF did not show statistically significant correlations with HH 15 and LHL 15 , PVR correlated statistically significantly HH 15 and LHL 15 . K value correlated with the preoperative values of cholinesterase, Fischer ratio, γ-globulin, ICGR 15 , albumin, and platelet count. There was a statistically significant correlation between LHL 15 and the value of cholinesterase, γ-globulin, platelet count, and Fischer ratio. When the liver resection of subsegmentectomy or more was indicated in 10 patients, nine patients had LHL 15 value less than 0.9 which delineated possibility of poor prognosis. However, judging from K value and HBF, liver resection was considered feasible and it was all successfully performed, resulting in good prognosis. From this study, it is suspected that 99m Tc-GSA scintigraphy reflect the severity of liver fibrosis and the amount of portal blood flows, and 99m Tc-PMT scintigraphy reflect the hepatic blood flow and ability of protein synthesis. It was proved that 99m Tc-PMT scintigraphy is

  5. Aggregation and fibrillation of bovine serum albumin

    DEFF Research Database (Denmark)

    Holm, NK; Jespersen, SK; Thomassen, LV

    2007-01-01

    The all-alpha helix multi-domain protein bovine serum albumin (BSA) aggregates at elevated temperatures. Here we show that these thermal aggregates have amyloid properties. They bind the fibril-specific dyes Thioflavin T and Congo Red, show elongated although somewhat worm-like morphology...

  6. Interaction of Water-Soluble CdTe Quantum Dots with Bovine Serum Albumin

    Science.gov (United States)

    2011-01-01

    Semiconductor nanoparticles (quantum dots) are promising fluorescent markers, but it is very little known about interaction of quantum dots with biological molecules. In this study, interaction of CdTe quantum dots coated with thioglycolic acid (TGA) with bovine serum albumin was investigated. Steady state spectroscopy, atomic force microscopy, electron microscopy and dynamic light scattering methods were used. It was explored how bovine serum albumin affects stability and spectral properties of quantum dots in aqueous media. CdTe–TGA quantum dots in aqueous solution appeared to be not stable and precipitated. Interaction with bovine serum albumin significantly enhanced stability and photoluminescence quantum yield of quantum dots and prevented quantum dots from aggregating. PMID:27502633

  7. Changes in serum albumin conformation under the effect of UV-radiation

    Energy Technology Data Exchange (ETDEWEB)

    Stepuro, I I; Artsukevich, A N; Ostrovskij, Yu N [AN Belorusskoj SSR, Minsk

    1981-01-01

    It has been established that a rapid photolysis of one (the most libile) disulfide bridge in bull serum albumins (BSA) and man's serum albumins (MSA) is caused by the sensitizing effect of 212 and 214 triptophan residues respectively; in fact the residues decompose simultaneously with the destruction of disulfide bond. This effect is not observed in 6-8 M guanosine. Conformation rebuilding of albumin globule is observed after the destruction of disulfide bond in albumin by UV-radiation and sodium boron hydride; it is accompanied by the decrease of accessible for fluorescent probe arginine residues, the accessibility of lysine residues being unchanged. Probe fluorescent intensity - 1.8-anilinonaphthalenesulfonate - decreases after the reduction of disulfide bond by 60-70% due to the loss of accessibility for chromophore of arginine residues.

  8. Changes in serum albumin conformation under the effect of UV-radiation

    International Nuclear Information System (INIS)

    Stepuro, I.I.; Artsukevich, A.N.; Ostrovskij, Yu.N.

    1981-01-01

    It has been established that a rapid photolysis of one (the most libile) disulfide bridge in bull serum albumins (BSA) and man's serum albumins (MSA) is caused by the sensitizing effect of 212 and 214 triptophan residues respectively; in fact the residues decompose simultaneously with the destruction of disulfide bond. This effect is not observed in 6-8 M guanosine. Conformation rebuilding of albumin globule is observed after the destruction of disulfide bond in albumin by UV-radiation and sodium boron hydride; it is accompanied by the decrease of accessible for fluorescent probe arginine residues, the accessibility of lysine residues being unchanged. Probe fluorescent intensity - 1.8-anilinonaphthalenesulfonate - decreases after the reduction of disulfide bond by 60-70% due to the loss of accessibility for chromophore of arginine residues

  9. Physiological serum copper concentrations found in malignancies cause unfolding induced aggregation of human serum albumin in vitro.

    Science.gov (United States)

    Rizvi, Asim; Furkan, Mohd; Naseem, Imrana

    2017-12-15

    Malignancies are characterized by several drastic metabolic changes, one of which is a progressive rise in the levels of serum copper. This rise in serum copper is documented across all malignancies and across malignancies in several species. This study aims to explore in vitro the effect of increased copper levels on the structure of the blood protein human serum albumin. Exposure of human serum albumin to physiologically relevant copper concentrations for 21 days resulted in structural modifications in the protein which were evident by changes in the intrinsic florescence. A loss of the predominantly alpha helical structure of human serum albumin was recorded along with a tendency to form protein aggregates. This aggregation was characterized by Thioflavin T and Congo Red assays. Rayleigh light scattering and turbidity assays confirmed aggregation. The aggregates were visually confirmed using transmission electron microscopy. This is the first report implicating increased copper levels as a cause of aggregation of blood proteins in malignancies. The physiological and biochemical implications of this phenomenon are discussed. Copyright © 2017. Published by Elsevier Inc.

  10. CSF/serum albumin ratio in dementias: a cross-sectional study on 1861 patients.

    Science.gov (United States)

    Skillbäck, Tobias; Delsing, Louise; Synnergren, Jane; Mattsson, Niklas; Janelidze, Shorena; Nägga, Katarina; Kilander, Lena; Hicks, Ryan; Wimo, Anders; Winblad, Bengt; Hansson, Oskar; Blennow, Kaj; Eriksdotter, Maria; Zetterberg, Henrik

    2017-11-01

    A connection between dementias and blood-brain barrier (BBB) dysfunction has been suggested, but previous studies have yielded conflicting results. We examined cerebrospinal fluid (CSF)/serum albumin ratio in a large cohort of patients diagnosed with Alzheimer's disease (AD, early onset [EAD, n = 130], late onset AD [LAD, n = 666]), vascular dementia (VaD, n = 255), mixed AD and VaD (MIX, n = 362), Lewy body dementia (DLB, n = 50), frontotemporal dementia (FTD, n = 56), Parkinson's disease dementia (PDD, n = 23), other dementias (other, n = 48), and dementia not otherwise specified (NOS, n = 271). We compared CSF/serum albumin ratio to 2 healthy control groups (n = 292, n = 20), between dementia diagnoses, and tested biomarker associations. Patients in DLB, LAD, VaD, MIX, other, and NOS groups had higher CSF/serum albumin ratio than controls. CSF/serum albumin ratio correlated with CSF neurofilament light in LAD, MIX, VaD, and other groups but not with AD biomarkers. Our data show that BBB leakage is common in dementias. The lack of association between CSF/serum albumin ratio and AD biomarkers suggests that BBB dysfunction is not inherent to AD but might represent concomitant cerebrovascular pathology. Copyright © 2017 Elsevier Inc. All rights reserved.

  11. Electrochemical Studies of Camptothecin and Its Interaction with Human Serum Albumin

    OpenAIRE

    Zhao, Jing; Zheng, Xiaofeng; Xing, Wei; Huang, Junyi; Li, Genxi

    2007-01-01

    Camptothecin, an anticancer component from Camptotheca acuminate, may interact with human serum albumin (HSA) at the subdomain IIA (site I), and then convert to its inactive form(carboxylate form). In this paper, the detailed electrochemical behaviors of camptothecin at a pyrolytic graphite electrode is presented. The interaction between camptothecin and HSA is also studied by electrochemical technique. By comparing with bovine serum albumin (BSA), which is highly homologous to HSA, we prove ...

  12. The effect of ionizing radiations on rat serum albumin on in vivo and in vitro

    International Nuclear Information System (INIS)

    Portakal, S.

    1984-01-01

    The effect of ionizing radiations on rat serum albumin was studied on in vivo and in vitro. Male rats (rattus norvegicus) were exposed to 225 roentgen wholebody X-irradiation on in vivo experiments. Time-course effects of irradiation on albumin level examined at immediately, 2.5 hours and 3 days after irradiation. Albumin level decreased above control level 2.5 hours after irradiation and rised within 3 days reaching control level. Pre-albumin/albumin ratio enhanced after x-irradiation. Aqueous solutions (0.5 percent) of rat serum albumin was exposed to various doses (0.2, 0.5, 1.0 and 1.9 Mrad) of 60 Co gamma irradiation on in vitro experiments. Results showed that electrophoretic mobility of serum albumin decreased after gamma irradiation. No significant change in albumin UV absorption spectrum was observed at 0.2, 0.5, 1.0 and 1.9 Mrad doses. Albumin becomes progressively less soluble in water as the radiation doses is increased. Radiation induced transformation into insoluble albumin agregates and scission products. (author)

  13. Serum Albumin Predicts Survival and Postoperative Course Following Surgery for Geriatric Hip Fracture.

    Science.gov (United States)

    Bohl, Daniel D; Shen, Mary R; Hannon, Charles P; Fillingham, Yale A; Darrith, Brian; Della Valle, Craig J

    2017-12-20

    Serum albumin level is the most well-established serum marker of malnutrition, with a serum albumin concentration malnutrition. The purpose of this study was to test if serum albumin level is associated with death, specific postoperative complications (e.g., pneumonia), length of hospital stay, and readmission following a surgical procedure for geriatric hip fracture. A retrospective cohort study of geriatric patients (≥65 years of age) undergoing a hip fracture surgical procedure as part of the American College of Surgeons National Surgical Quality Improvement Program was conducted. Outcomes were compared between patients with and without hypoalbuminemia. All comparisons were adjusted for baseline and procedural differences between populations, and patients with missing serum albumin concentration were included in analyses using a missing data indicator. There were 29,377 geriatric patients undergoing a hip fracture surgical procedure who met inclusion criteria; of these patients, 17,651 (60.1%) had serum albumin available for analysis. The prevalence of hypoalbuminemia was 45.9%. Following adjustment for baseline and procedural characteristics, the risk of death was inversely associated with serum albumin concentration as a continuous variable (adjusted relative risk, 0.59 [95% confidence interval (CI), 0.53 to 0.65]; p patients with normal albumin concentration, patients with hypoalbuminemia had higher rates of death (9.94% compared with 5.53% [adjusted relative risk, 1.52 (95% CI, 1.37 to 1.70); p patients with hypoalbuminemia at 5.67 ± 4.68 days compared with those without hypoalbuminemia at 4.99 ± 3.95 days; the adjusted difference was 0.50 day (95% CI, 0.38 to 0.63 day; p patients with hypoalbuminemia (10.91%) and those without hypoalbuminemia (9.03%); the adjusted relative risk was 1.10 (95% CI, 1.00 to 1.21). Hypoalbuminemia is a powerful independent risk factor for mortality following a surgical procedure for geriatric hip fracture. These data suggest

  14. Pretreatment serum albumin: a prognostic indicator of survival in oral cancer

    OpenAIRE

    Saurabh Bobdey; Aanchal Jain; Jignasa Sathwara; Ganesh B

    2016-01-01

    Background: Malnutrition has been recognized as a poor prognostic indicator for cancer. In recent years, the role of serum albumin as a predictor of survival in cancer has received considerable attention. Therefore, the present study was carried out to investigate whether the pretreatment serum albumin can predict the prognosis of patients with oral cancer. Methods: Medical records of 433 pathologically proven oral cancer patients diagnosed and treated from 01st January 2006 to 31st Decemb...

  15. Raman spectroscopy in investigations of mechanism of binding of human serum albumin to molecular probe fluorescein

    International Nuclear Information System (INIS)

    Vlasova, I M; Saletsky, A M

    2008-01-01

    The mechanism of binding of molecular probe fluorescein to molecules of human serum albumin was studied by the Raman spectroscopy method. The position of binding Center on human serum albumin molecule for fluorescein is determined. The amino acid residues of albumin molecule, participating in binding of fluorescein at different pH values of solution, are established. The conformation rearrangements of globules of human serum albumin, taking place at binding of fluorescein at different pH values of solution, are registered

  16. Fluorescence lifetime measurements of native and glycated human serum albumin and bovine serum albumin

    Science.gov (United States)

    Joshi, Narahari V.; Joshi, Virgina O. d.; Contreras, Silvia; Gil, Herminia; Medina, Honorio; Siemiarczuk, Aleksander

    1999-05-01

    Nonenzymatic glycation, also known as Maillard reaction, plays an important role in the secondary complications of the diabetic pathology and aging, therefore, human serum albumin (HSA) and bovine serum albumin (BSA) were glycated by a conventional method in our laboratory using glucose as the glycating agent. Fluorescence lifetime measurements were carried out with a laser strobe fluorometer equipped with a nitrogen/dye laser and a frequency doubler as a pulsed excitation source. The samples were excited at 295 nm and the emission spectra were recorded at 345 nm. The obtained decay curves were tried for double and triple exponential functions. It has been found that the shorter lifetime increases for glycated proteins as compared with that of the native ones. For example, in the case of glycated BSA the lifetime increased from 1.36 ns to 2.30 ns. Similarly, for HSA, the lifetime increases from 1.58 ns to 2.26 ns. Meanwhile, the longer lifetime changed very slightly for both proteins (from 6.52 ns to 6.72 ns). The increase in the lifetime can be associated with the environmental effect; originated from the attachment of glucose to some lysine residues. A good example is Trp 214 which is in the cage of Lys 225, Lys 212, Lys 233, Lys 205, Lys 500, Lys 199 and Lys 195. If fluorescence lifetime technique is calibrated and properly used it could be employed for assessing glycation of proteins.

  17. A discussion of serum albumin level in advanced-stage hepatocellular carcinoma: a medical oncologist's perspective.

    Science.gov (United States)

    Tanriverdi, Ozgur

    2014-11-01

    Hepatocellular carcinoma is the most common primary malignant tumor of the liver, and it is particularly prevalent in East and Southeast Asia. With surgical and/or local interventional treatment methods, survival rates for early-stage hepatocellular cancers have increased. However, it is not yet clear which staging systems are more applicable in hepatocellular carcinoma. Serum albumin level is already being used as a criterion in most staging systems. Albumin is an important serum protein in human bodily functions, but only 5 % of the daily amount needed is synthesized by the liver. The serum albumin level is affected by multifactorial situations, including capillary permeability, drugs, liver insufficiency, inflammation and/or infections, dehydration or overhydration, protein loosing disorders, and decreased nutrition intake in anorexia-malnutrition syndrome and cancer cachexia. Because of this complex situation, serum albumin level may affect many staging systems for hepatocellular carcinoma by leading to false-negative results. In this paper, the statuses of current staging systems are reviewed, and possible negative events regarding the serum albumin levels found in these staging systems are discussed.

  18. Radiation-induced Changes in the Electrophoretic Profile of Serum Albumin

    Directory of Open Access Journals (Sweden)

    Celso Vieira Lima

    2018-01-01

    Full Text Available ABSTRACT Albumin protein profiles were investigated in electrophoresis system in relation to the whole body exposition to the radiation. Two groups of rats Wistar were set up as the control (CG and the irradiated one (IG. The IG was exposed to Co-60 at a dose of 5 Gy. After a 72-hour exposition, 300 μL of blood was collected in the inferior vena cava, renal, jugular, hepatic, and pulmonary veins and the serum separated. The albumin protein was identified by vertical electrophoresis in acrylamide Commassi blue or silver stained. The calibration procedure was applied to albumin samples with well-known concentrations. The mathematical correlation was developed involving electrophoretic parameters of band intensities and sizes from gel representation, providing values of protein concentrations in comparison with standard bands with known concentrations. There were significant differences in the physiological concentrations in the jugular and pulmonary sites in relation to renal and cava regional sites. Significant differences induced by radiation in serum albumin concentration were also found in hepatic and jugular sites. Alteration of albumin concentration was found as a nearly effect from whole body irradiation. This phenomenon points out to alterations in cell metabolism in the liver justified by a possible indication of proteomics damage from radiation.

  19. Photo-physical and structural interactions between viologen phosphorus-based dendrimers and human serum albumin

    International Nuclear Information System (INIS)

    Ciepluch, Karol; Katir, Nadia; El Kadib, Abdelkrim; Weber, Monika; Caminade, Anne-Marie; Bousmina, Mostapha; Pierre Majoral, Jean; Bryszewska, Maria

    2012-01-01

    This work deals with photo-physical and structural interactions between viologen phosphorus dendrimers and human serum albumin (HSA). Viologens are derivatives of 4,4′-bipyridinium salts. Aiming to rationalize the parameters governing such interactions eight types of these polycationic dendrimers in which the generation, the number of charges, the nature of the core and of the terminal groups vary from one to another, were designed and used. The influence of viologen-based dendrimers' on human serum albumin has been investigated. The photo-physical interactions of the two systems have been monitored by fluorescence quenching of free L-tryptophan and of HSA tryptophan residue. Additionally, using circular dichroism (CD) the effect of dendrimers on the secondary structure of albumin was measured. The obtained results show that viologen dendrimers interact with human serum albumin quenching its fluorescence either by collisional (dynamic) way or by forming complexes in a ground state (static quenching). In some cases the quenching is accompanied by changes of the secondary structure of HSA. - Highlights: ► Photo-physical interactions between viologen phosphorus dendrimers and human serum albumin (HSA) were investigated. ► The viologen dendrimers can quench the fluorescence of tryptophan in HSA. ► CD spectra to explain the changes in secondary structure of albumin after exposition of dendrimers.

  20. Increase in serum albumin concentration is associated with prediabetes development and progression to overt diabetes independently of metabolic syndrome.

    Science.gov (United States)

    Jun, Ji Eun; Lee, Seung-Eun; Lee, You-Bin; Jee, Jae Hwan; Bae, Ji Cheol; Jin, Sang-Man; Hur, Kyu Yeon; Lee, Moon-Kyu; Kim, Jae Hyeon

    2017-01-01

    Serum albumin concentration is associated with both type 2 diabetes and metabolic syndrome (MetS). We sought to investigate whether baseline serum albumin and change in serum albumin could be independent risk factors for prediabetes in subjects without MetS. We further examined the effect of serum albumin on progression to overt diabetes in subjects who developed prediabetes. Among 10,792 participants without diabetes and MetS who consecutively underwent yearly health check-ups over six years, 9,807 subjects without incident MetS were enrolled in this longitudinal retrospective study. The risk of developing prediabetes (impared fasting glucose or hemoglobin A1c) was analyzed according to baseline and percent change in serum albumin concentration using Cox regression analysis. Serial changes in serum albumin concentration were measured from baseline to one year before prediabetes diagnosis, and then from the time of prediabetes diagnosis to progression to overt diabetes or final follow-up. A total of 4,398 incident cases of prediabetes developed during 35,807 person-years (median 3.8 years). The hazard ratio for incident prediabetes decreased as percent change in serum albumin concentration (quartiles and per 1%) increased in a crude and fully adjusted model. However, baseline serum albumin concentration itself was not associated with prediabetic risk. Serum albumin levels kept increasing until the end of follow-up in prediabetic subjects who returned to normal glycemic status, whereas these measures did not change in prediabetic subjects who developed type 2 diabetes. Serum albumin concentration measured at the end of follow-up was the highest in the regression group, compared to the stationary (p = 0.014) or progression groups (p = 0.009). Increase in serum albumin concentration might protect against early glycemic deterioration and progression to type 2 diabetes even in subjects without MetS.

  1. Interaction between serum albumins and sonochemically synthesized cadmium sulphide nanoparticles: a spectroscopic study

    International Nuclear Information System (INIS)

    Naveenraj, Selvaraj; Asiri, Abdullah M.; Anandan, Sambandam

    2013-01-01

    Cadmium Sulphide nanoparticles approximately 5–10 nm in size range were synthesized by sonochemical technique, which follows acoustic cavitation phenomenon and generates nanoparticles with a smaller size range and higher surface area. The in vitro binding interaction of these sonochemically synthesized CdS nanoparticles with serum albumins (SA) were investigated using UV–Vis absorption, fluorescence and circular dichroism (CD) spectroscopic techniques since CdS nanoparticles has biological applications such as cellular labelling and deep-tissue imaging. UV–Vis absorption and fluorescence studies confirm that CdS nanoparticles bind with SA through ground state complex formation (static quenching mechanism). The results suggest that sonochemically synthesized CdS nanoparticles interact with HSA more than that of BSA and these nanoparticles can be easily transported and rapidly released to the targets by serum albumins. CD studies confirmed the conformational change of serum albumins on the interaction of CdS nanoparticles.Graphical AbstractThis paper investigates the in vitro binding interaction of Cadmium Sulphide (CdS) nanoparticles with serum albumins (HSA and BSA) using the UV-vis, steady-state fluorescence, time-resolved fluorescence, synchronous fluorescence and circular dichroism (CD) spectral techniques.

  2. Photo-physical and structural interactions between viologen phosphorus-based dendrimers and human serum albumin

    Energy Technology Data Exchange (ETDEWEB)

    Ciepluch, Karol, E-mail: ciepluch@biol.uni.lodz.pl [Department of General Biophysics, University of Lodz, 141/143 Pomorska St., 90-236 Lodz (Poland); Katir, Nadia [Laboratoire de Chimie de Coordination du CNRS (LCC), 205 route de Narbonne, F-31077 Toulouse cedex 4 (France); Institute of Nanomaterials and Nanotechnology (INANOTECH)-MAScIR (Moroccan Foundation for Advanced Science, Innovation and Research), ENSET, Avenue de l' Armee Royale, Madinat El Irfane, 10100 Rabat (Morocco); El Kadib, Abdelkrim [Institute of Nanomaterials and Nanotechnology (INANOTECH)-MAScIR (Moroccan Foundation for Advanced Science, Innovation and Research), ENSET, Avenue de l' Armee Royale, Madinat El Irfane, 10100 Rabat (Morocco); Weber, Monika [Department of General Biophysics, University of Lodz, 141/143 Pomorska St., 90-236 Lodz (Poland); Caminade, Anne-Marie [Laboratoire de Chimie de Coordination du CNRS (LCC), 205 route de Narbonne, F-31077 Toulouse cedex 4 (France); Bousmina, Mostapha [Hassan II Academy of Sciences and Technology, Avenue MVI, Km4, 10220 Rabat (Morocco); Pierre Majoral, Jean [Laboratoire de Chimie de Coordination du CNRS (LCC), 205 route de Narbonne, F-31077 Toulouse cedex 4 (France); Hassan II Academy of Sciences and Technology, Avenue MVI, Km4, 10220 Rabat (Morocco); Bryszewska, Maria [Department of General Biophysics, University of Lodz, 141/143 Pomorska St., 90-236 Lodz (Poland)

    2012-06-15

    This work deals with photo-physical and structural interactions between viologen phosphorus dendrimers and human serum albumin (HSA). Viologens are derivatives of 4,4 Prime -bipyridinium salts. Aiming to rationalize the parameters governing such interactions eight types of these polycationic dendrimers in which the generation, the number of charges, the nature of the core and of the terminal groups vary from one to another, were designed and used. The influence of viologen-based dendrimers' on human serum albumin has been investigated. The photo-physical interactions of the two systems have been monitored by fluorescence quenching of free L-tryptophan and of HSA tryptophan residue. Additionally, using circular dichroism (CD) the effect of dendrimers on the secondary structure of albumin was measured. The obtained results show that viologen dendrimers interact with human serum albumin quenching its fluorescence either by collisional (dynamic) way or by forming complexes in a ground state (static quenching). In some cases the quenching is accompanied by changes of the secondary structure of HSA. - Highlights: Black-Right-Pointing-Pointer Photo-physical interactions between viologen phosphorus dendrimers and human serum albumin (HSA) were investigated. Black-Right-Pointing-Pointer The viologen dendrimers can quench the fluorescence of tryptophan in HSA. Black-Right-Pointing-Pointer CD spectra to explain the changes in secondary structure of albumin after exposition of dendrimers.

  3. A fast and reproducible method for albumin isolation and depletion from serum and cerebrospinal fluid.

    Science.gov (United States)

    Holewinski, Ronald J; Jin, Zhicheng; Powell, Matthew J; Maust, Matthew D; Van Eyk, Jennifer E

    2013-03-01

    Analysis of serum and plasma proteomes is a common approach for biomarker discovery, and the removal of high-abundant proteins, such as albumin and immunoglobins, is usually the first step in the analysis. However, albumin binds peptides and proteins, which raises concerns as to how the removal of albumin could impact the outcome of the biomarker study while ignoring the possibility that this could be a biomarker subproteome itself. The first goal of this study was to test a new commercially available affinity capture reagent from Protea Biosciences and to compare the efficiency and reproducibility to four other commercially available albumin depletion methods. The second goal of this study was to determine if there is a highly efficient albumin depletion/isolation system that minimizes sample handling and would be suitable for large numbers of samples. Two of the methods tested (Sigma and ProteaPrep) showed an albumin depletion efficiency of 97% or greater for both serum and cerebrospinal fluid (CSF). Isolated serum and CSF albuminomes from ProteaPrep spin columns were analyzed directly by LC-MS/MS, identifying 128 serum (45 not previously reported) and 94 CSF albuminome proteins (17 unique to the CSF albuminome). Serum albuminome was also isolated using Vivapure anti-HSA columns for comparison, identifying 105 proteins, 81 of which overlapped with the ProteaPrep method. © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

  4. Study the interaction between CdTe-glutathione and human serum albumin

    International Nuclear Information System (INIS)

    Yang, Qing; Zhou, Xi-min; Zhu, Yi-shuo; Chen, Xing-guo

    2013-01-01

    In this paper, glutathione (GSH) modified CdTe quantum dots (CdTe-GSH QDs) were synthesized in an aqueous solution. Then, the binding of the CdTe-GSH QDs to human serum albumin (HSA) was studied using the fluorescence spectroscopy. The quenching mechanism was investigated in terms of the association constants and basic thermodynamic parameters. The fluorescence data revealed that CdTe-GSH QDs could quench the intrinsic fluorescence of human serum albumin by a static quenching mechanism. Furthermore, alteration of the secondary protein structure in the presence of the QDs was confirmed by synchronous fluorescence spectra. - Highlights: ► In this paper, the binding of the CdTe-GSH QDs to human serum albumin (HSA) was studied using a fluorescence spectroscopy. ► The quenching mechanism was investigated in terms of the association constants and basic thermodynamic parameters. ► Furthermore, alteration of the secondary protein structure in the presence of the QDs was confirmed by synchronous fluorescence spectra. ► The research can help us assess biological toxicity of QDs and further expand the application scope of QDs.

  5. Is low serum albumin associated with postoperative complications in patients undergoing cardiac surgery?

    Science.gov (United States)

    Karas, Pamela L; Goh, Sean L; Dhital, Kumud

    2015-12-01

    A best evidence topic was written according to a structured protocol. The clinical question investigated was: is low serum albumin associated with postoperative complications in patients undergoing cardiac surgery? There were 62 papers retrieved using the reported search strategy. Of these, 12 publications embodied the best evidence to answer this clinical question. The authors, journal, date and country of the publication, patient group investigated, study design, relevant outcomes and results of these papers were tabulated. This paper includes a total of 12 589 patients, and of the papers reviewed, 4 were level 3 and 8 level 4. Each of the publications reviewed and compared either all or some of the following postoperative complications: mortality, postoperative bleeding requiring reoperation, prolonged hospital stay and ventilatory support, infection, liver dysfunction, delirium and acute kidney injury (AKI). Of the studies that examined postoperative mortality, all except for three established a significant multivariate association with low preoperative albumin level. Some scepticism is required in accepting other results that were only present in univariate analysis. While three studies examined multiple levels of serum albumin, most dichotomized the serum albumin levels into normal and abnormal groups. This led to differing classifications of hypoalbuminaemia, ranging from less than 2.5 to 4.0 g/dl. The available evidence, however, suggests that low preoperative serum albumin level in patients undergoing cardiac surgery is associated with the following: (i) increased risk of mortality after surgery and (ii) greater incidence of postoperative morbidity. While the evidence supports the use of preoperative albumin in assessing post-cardiac surgery complications, a specific level of albumin considered to be abnormal cannot be concluded from this review. © The Author 2015. Published by Oxford University Press on behalf of the European Association for Cardio

  6. Human serum albumin mediated self-assembly of gold nanoparticles into hollow spheres

    Energy Technology Data Exchange (ETDEWEB)

    Nayak, Nimai C [Singapore-MIT Alliance, Manufacturing Systems and Technology Programme, Nanyang Technological University, 65 Nanyang Drive, 637460 (Singapore); Shin, Kwanwoo [Interdisciplinary Program of Integrated Biotechnology, Sogang University, Shinsoo-dong, Mapo-gu, Seoul 121-742 (Korea, Republic of)], E-mail: ncnayak@gmail.com

    2008-07-02

    The assembly of nanoparticles in topologically predefined superstructures is an important area in nanoscale architecture. In this paper, we report an unusual aggregation phenomenon involving L-lysine capped gold nanoparticles and human serum albumin into hollow nanospheres. The electrostatic interaction between positively charged L-lysine capped gold nanoparticles and negatively charged human serum albumin at physiological pH led to the assembly of the gold nanoparticles into hollow spheres. The phenomenon can be explained by the dry hole opening mechanism.

  7. Human serum albumin mediated self-assembly of gold nanoparticles into hollow spheres

    International Nuclear Information System (INIS)

    Nayak, Nimai C; Shin, Kwanwoo

    2008-01-01

    The assembly of nanoparticles in topologically predefined superstructures is an important area in nanoscale architecture. In this paper, we report an unusual aggregation phenomenon involving L-lysine capped gold nanoparticles and human serum albumin into hollow nanospheres. The electrostatic interaction between positively charged L-lysine capped gold nanoparticles and negatively charged human serum albumin at physiological pH led to the assembly of the gold nanoparticles into hollow spheres. The phenomenon can be explained by the dry hole opening mechanism

  8. Thermodynamic parameters for binding of fatty acids to human serum albumin

    DEFF Research Database (Denmark)

    Pedersen, A O; Honoré, B; Brodersen, R

    1990-01-01

    Binding of laurate and myristate anions to human serum albumin has been studied over a range of temperatures, 5-37 degrees C, at pH 7.4. The binding curves indicate that the strength of binding of the first few molecules of fatty acid to albumin (r less than 5) decreases with increasing temperatu...

  9. Multiple binding of bilirubin to human serum albumin and cobinding with laurate

    DEFF Research Database (Denmark)

    Sato, H; Honoré, B; Brodersen, R

    1988-01-01

    Numerical analysis of multiple binding of two ligands to one carrier has been accomplished, using the principle of several sets of acceptable binding constants, with bilirubin-laurate-albumin as an example. Binding of bilirubin to defatted human serum albumin was investigated by a spectroscopic...

  10. Assessment of hepatic functional reserve for hepatic resection using {sup 99m}Tc-PMT scintigraphy in comparison with {sup 99m}Tc-GSA scintigraphy

    Energy Technology Data Exchange (ETDEWEB)

    Sakuma, Atsushi [Dokkyo Univ. School of Medicine, Mibu, Tochigi (Japan)

    2000-03-01

    {sup 99m}Tc-diethylenetriamine-pentaacetic acid-galactosyl human serum albumin({sup 99m}Tc-GSA) scintigraphy has been reported as a useful study of hepatic functional reserve recently. We have performed {sup 99m}Tc-N-pyridoxyl-5-methyl-tryptophan({sup 99m}Tc-PMT) and {sup 99m}Tc-GSA preoperatively for evaluation of hepatic functional reserve and compared the usefulness of those scintigraphy study. Twenty-four patients who were the candidates of hepatic resection underwent {sup 99m}Tc-PMT scintigraphy preoperatively. Hepatic blood flow coefficient (K value), the amount of hepatic blood flow (HBF), and the ratio of portal blood flow (PVR) were computed. {sup 99m}Tc-GSA scintigraphy was also performed within two weeks of the {sup 99m}Tc-PMT scintigraphy, and the ratio of disappearance (HH{sub 15}) and the hepatic uptake ratio (LHL{sub 15}) were computed. The relationship between K value, HBF, PVR, HH{sub 15} and LHL{sub 15} was analyzed. Their correlation with other liver function tests was also examined. K value and HBF did not show statistically significant correlations with HH{sub 15} and LHL{sub 15}, PVR correlated statistically significantly HH{sub 15} and LHL{sub 15}. K value correlated with the preoperative values of cholinesterase, Fischer ratio, {gamma}-globulin, ICGR{sub 15}, albumin, and platelet count. There was a statistically significant correlation between LHL{sub 15} and the value of cholinesterase, {gamma}-globulin, platelet count, and Fischer ratio. When the liver resection of subsegmentectomy or more was indicated in 10 patients, nine patients had LHL{sub 15} value less than 0.9 which delineated possibility of poor prognosis. However, judging from K value and HBF, liver resection was considered feasible and it was all successfully performed, resulting in good prognosis. From this study, it is suspected that {sup 99m}Tc-GSA scintigraphy reflect the severity of liver fibrosis and the amount of portal blood flows, and {sup 99m}Tc-PMT scintigraphy

  11. Relationship between ionized calcium and serum albumin level in children with idiopathic nephrotic syndrome

    Directory of Open Access Journals (Sweden)

    Viiola Irene Winata

    2016-10-01

    Full Text Available Background Nephrotic syndrome (NS patients frequently have abnormalities in calcium metabolism that manifest as hypocalcemia and reduced intestinal absorption of calcium. Hypocalcemia is initially attributed to hypoalbuminemia but it may also relate to a low level of ionized calcium. The ionized calcium level depends on the severity and duration of proteinuria. Objective To assess the rel ationship between ionized calcium and serum albumin level in idiopathic NS children. Methods An analytical study with cross-sectional design was applied to NS and healthy children between 1-14 years old in the Child Health Department of Hasan Sadikin Hospital, Bandung from December 2009 to April 2010. Ionized calcium was examined by Ca2 + analyzer AVL 980 with ion-selective electrodes (ISE methods. Results A total of34 subjects were recruited, consist of 17 NS and 17 healthy children. The mean ionized calcium and serum albumin level in NS children was 4.56 (SD 0.23 mg/dLand 1.45 (SD 0.24 g/dL, respectively. Statistical difference between ionized calcium level in NS and in healthy children was significant (P<0.05. Pearson correlation test between ionized calcium and serum albumin was significant (P<0.05 with correlation coefficient (r 0.53. We found the following equation to estimate ionized calcium (y based on the serum albumin level (x: y=3.84+0.49x. Conclusion There is a moderately positive linear relationship between ionized calcium and serum albumin level in NS children.

  12. Recombinant human serum albumin hydrogel as a novel drug delivery vehicle

    International Nuclear Information System (INIS)

    Hirose, Masaaki; Tachibana, Akira; Tanabe, Toshizumi

    2010-01-01

    Serum albumin acts as a physiological carrier for various compounds including drugs. A hydrogel consisting of recombinant human serum albumin (rHSA) was prepared to take advantage of drug binding ability of albumin for a sustained drug release carrier. The hydrogel was prepared by mixing rHSA and dithiothreitol and casted to a polystyrene mold. Hydrogel formation was thought to occur through the intermolecular interaction of the hydrophobic groups by protein denaturation. The release of sodium benzoate and salicylic acid from the hydrogel completed in 2 h, while warfarin release continued for 24 h. The total amounts of the drugs released from 100 mg of 15 and 5% rHSA hydrogel were 2.3 and 1.4 μmol for warfarin, 1.4 and 1.1 μmol for salicylic acid and 0.9 and 0.9 μmol for sodium benzoate. These results reflected the order of the binding ability of drugs for intact albumin indicating that the drug binding ability of HSA still remained after the hydrogel formation. However, fibroblast cells attached and proliferated well on the hydrogel, indicating that denaturation of rHSA proceeded to the extent to allow the cell attachment. The present rHSA hydrogel might be suitable for a sustained release carrier of drugs having affinity for albumin.

  13. Recombinant human serum albumin hydrogel as a novel drug delivery vehicle

    Energy Technology Data Exchange (ETDEWEB)

    Hirose, Masaaki, E-mail: Hirose.Masaaki@mh.mt-pharma.co.jp [Advanced Medical Research Laboratory, Research Division, Mitsubishi Tanabe Pharma Corporation, 3-16-89 Kashima, Yodogawa-ku, Osaka 532-8505 (Japan); Department of Applied Chemistry and Bioengineering, Graduate School of Engineering, Osaka City University, 3-3-138 Sugimoto, Sumiyoshi-ku, Osaka 558-8585 (Japan); Tachibana, Akira; Tanabe, Toshizumi [Department of Applied Chemistry and Bioengineering, Graduate School of Engineering, Osaka City University, 3-3-138 Sugimoto, Sumiyoshi-ku, Osaka 558-8585 (Japan)

    2010-06-15

    Serum albumin acts as a physiological carrier for various compounds including drugs. A hydrogel consisting of recombinant human serum albumin (rHSA) was prepared to take advantage of drug binding ability of albumin for a sustained drug release carrier. The hydrogel was prepared by mixing rHSA and dithiothreitol and casted to a polystyrene mold. Hydrogel formation was thought to occur through the intermolecular interaction of the hydrophobic groups by protein denaturation. The release of sodium benzoate and salicylic acid from the hydrogel completed in 2 h, while warfarin release continued for 24 h. The total amounts of the drugs released from 100 mg of 15 and 5% rHSA hydrogel were 2.3 and 1.4 {mu}mol for warfarin, 1.4 and 1.1 {mu}mol for salicylic acid and 0.9 and 0.9 {mu}mol for sodium benzoate. These results reflected the order of the binding ability of drugs for intact albumin indicating that the drug binding ability of HSA still remained after the hydrogel formation. However, fibroblast cells attached and proliferated well on the hydrogel, indicating that denaturation of rHSA proceeded to the extent to allow the cell attachment. The present rHSA hydrogel might be suitable for a sustained release carrier of drugs having affinity for albumin.

  14. Alteration of human serum albumin binding properties induced by modifications: A review

    Science.gov (United States)

    Maciążek-Jurczyk, Małgorzata; Szkudlarek, Agnieszka; Chudzik, Mariola; Pożycka, Jadwiga; Sułkowska, Anna

    2018-01-01

    Albumin, a major transporting protein in the blood, is the main target of modification that affects the binding of drugs to Sudlow's site I and II. These modification of serum protein moderates its physiological function, and works as a biomarker of some diseases. The main goal of the paper was to explain the possible alteration of human serum albumin binding properties induced by modifications such as glycation, oxidation and ageing, their origin, methods of evaluation and positive and negative meaning described by significant researchers.

  15. 125I-labeling and purification of peptide hormones and bovine serum albumin

    International Nuclear Information System (INIS)

    Nemeth, J; Jakab, B.; Szilvassy, Z.; Oroszi, G.; Roeth, E.; Magyarlaki, M.; Farkas, B.

    2002-01-01

    The iodination and separation of various diagnostically and/or experimentally important peptides including (Tyr 1 )-somatostatin-14, rat Tyr-α-calcitonin gene-related peptide (23-37), motilin and vasoactive intestinal peptide, furthermore bovine serum albumin are described. All species were iodinated by the iodogen method. The 125 I-labeled peptide products were separated by reversed-phase HPLC, the specific activities of mono-iodinated forms are near identical with the theoretical value. The labeled bovine serum albumin was separated by Sephadex G-100 gel filtration. (author)

  16. Resveratrol-loaded glycyrrhizic acid-conjugated human serum albumin nanoparticles wrapping resveratrol nanoparticles: Preparation, characterization, and targeting effect on liver tumors.

    Science.gov (United States)

    Wu, Mingfang; Lian, Bolin; Deng, Yiping; Feng, Ziqi; Zhong, Chen; Wu, Weiwei; Huang, Yannian; Wang, Lingling; Zu, Chang; Zhao, Xiuhua

    2017-08-01

    In this study, glycyrrhizic acid-conjugated human serum albumin nanoparticles wrapping resveratrol nanoparticles were prepared to establish a tumor targeting nano-sized drug delivery system. Glycyrrhizic acid was coupled to human serum albumin, and resveratrol was encapsulated in glycyrrhizic acid-conjugated human serum albumin by high-pressure homogenization emulsification. The average particle size of sample nanoparticles prepared under the optimal conditions was 108.1 ± 5.3 nm with a polydispersity index (PDI) of 0.001, and the amount of glycyrrhizic acid coupled with human serum albumin was 112.56 µg/mg. The drug encapsulation efficiency and drug loading efficiency were 83.6 and 11.5%, respectively. The glycyrrhizic acid-conjugated human serum albumin nanoparticles wrapping resveratrol nanoparticles were characterized through laser light scattering, scanning electron microscopy, Fourier-transform infrared spectroscopy, X-ray diffraction, differential scanning calorimetry, thermogravimetric analyses, and gas chromatography. The characterization results showed that resveratrol in glycyrrhizic acid-conjugated human serum albumin nanoparticles wrapping resveratrol nanoparticles existed in amorphous state and the residual amounts of chloroform and methanol in nanoparticles were separately less than the international conference on harmonization (ICH) limit. The in vitro drug-release study showed that the nanoparticles released the drug slowly and continuously. The inhibitory rate of glycyrrhizic acid-conjugated human serum albumin nanoparticles wrapping resveratrol nanoparticles was measured using 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl-2 H-tetrazolium bromide method. The IC50 values of glycyrrhizic acid-conjugated human serum albumin nanoparticles wrapping resveratrol nanoparticles and resveratrol were 62.5 and 95.5 µg/ml, respectively. The target ability of glycyrrhizic acid-conjugated human serum albumin nanoparticles wrapping resveratrol nanoparticles

  17. Study of albumin from beef blood serum in D2O solutions

    International Nuclear Information System (INIS)

    Lewandowska, D.; Podoski, T.

    1994-01-01

    Molecular dynamics of albumin obtained from beef blood serum have been investigated in heavy water solutions by means of NMR spectra. The chemical shifts as well as spin-lattice relaxation times have been measured. The number of water protons interacting with albumin molecule have been estimated

  18. Binding of ethyl pyruvate to bovine serum albumin: Calorimetric, spectroscopic and molecular docking studies

    Energy Technology Data Exchange (ETDEWEB)

    Pathak, Mallika [Department of Chemistry, Miranda House, University of Delhi, Delhi 11007 (India); Mishra, Rashmi; Agarwala, Paban K. [Department of Radiation Genetics and Epigenetics, Division of Radioprotective Drug Development Research, Institute of Nuclear Medicine and Allied Sciences, Delhi 110054 (India); Ojha, Himanshu, E-mail: himanshu.drdo@gmail.com [Department of Radiation Genetics and Epigenetics, Division of Radioprotective Drug Development Research, Institute of Nuclear Medicine and Allied Sciences, Delhi 110054 (India); Singh, Bhawna [Department of Radiation Genetics and Epigenetics, Division of Radioprotective Drug Development Research, Institute of Nuclear Medicine and Allied Sciences, Delhi 110054 (India); Singh, Anju; Kukreti, Shrikant [Nucleic Acid Research Laboratory, Department of Chemistry, University of Delhi, Delhi 11007 (India)

    2016-06-10

    Highlights: • ITC study showed binding of ethyl pyruvate with BSA with high binding affinity. • Ethyl pyruvate binding caused conformation alteration of BSA. • Fluorescence quenching mechanism is static in nature. • Electrostatic, hydrogen bonding and hydrophobic forces involved in binding. • Docking confirmed role of electrostatic, hydrogen bonding and hydrophobic forces. - Abstract: Various in vitro and in vivo studies have shown the anti-inflammatory and anticancer potential role of ethyl pyruvate. Bio-distribution of drugs is significantly influenced by the drug-serum protein binding. Therefore, the binding mechanism of the ethyl pyruvate with bovine serum albumin was investigated using UV–vis absorption, fluorescence, circular dichroism, isothermal titration calorimetry and molecular docking techniques. Absorption and fluorescence quenching studies indicated the binding of ethyl pyruvate with protein. Circular dichroism spectra of bovine serum albumin confirmed significant change in the conformation of protein upon binding. Thermodynamic data confirmed that ethyl pyruvate binds to bovine serum albumin at the two different sites with high affinity. Binding of ethyl pyruvate to bovine serum albumin involves hydrogen bonding, van der Waal and hydrophobic interactions. Further, docking studies indicated that ethyl pyruvate could bind significantly at the three binding sites. The results will definitely contribute to the development of ethyl pyruvate as drug.

  19. Circular dichroism study of the interaction between mutagens and bilirubin bound to different binding sites of serum albumins

    Science.gov (United States)

    Orlov, Sergey; Goncharova, Iryna; Urbanová, Marie

    Although recent investigations have shown that bilirubin not only has a negative role in the organism but also exhibits significant antimutagenic properties, the mechanisms of interactions between bilirubin and mutagens are not clear. In this study, interaction between bilirubin bound to different binding sites of mammalian serum albumins with structural analogues of the mutagens 2-aminofluorene, 2,7-diaminofluorene and mutagen 2,4,7-trinitrofluorenone were investigated by circular dichroism and absorption spectroscopy. Homological human and bovine serum albumins were used as chiral matrices, which preferentially bind different conformers of bilirubin in the primary binding sites and make it observable by circular dichroism. These molecular systems approximated a real system for the study of mutagens in blood serum. Differences between the interaction of bilirubin bound to primary and to secondary binding sites of serum albumins with mutagens were shown. For bilirubin bound to secondary binding sites with low affinity, partial displacement and the formation of self-associates were observed in all studied mutagens. The associates of bilirubin bound to primary binding sites of serum albumins are formed with 2-aminofluorene and 2,4,7-trinitrofluorenone. It was proposed that 2,7-diaminofluorene does not interact with bilirubin bound to primary sites of human and bovine serum albumins due to the spatial hindrance of the albumins binding domains. The spatial arrangement of the bilirubin bound to serum albumin along with the studied mutagens was modelled using ligand docking, which revealed a possibility of an arrangement of the both bilirubin and 2-aminofluorene and 2,4,7-trinitrofluorenone in the primary binding site of human serum albumin.

  20. Prediagnostic serum calcium and albumin and ovarian cancer: A nested case-control study in the Norwegian Janus Serum Bank Cohort.

    Science.gov (United States)

    Schwartz, Gary G; Tretli, Steinar; Vos, Linda; Robsahm, Trude E

    2017-08-01

    Women with higher serum calcium may be more likely to be diagnosed and die of ovarian cancer. We evaluated that finding in a large, prospective cohort. We conducted a nested case-control study using a population-based biobank from Norway. We compared 202 ovarian cancer cases and 202 controls, matched for age, date at blood draw, and county of residence, with respect to serum calcium and albumin, adjusted for anthropometric variables. We evaluated risks using the entire follow-up period as well as 2-15 years and 16-25 years ("early" and "late", respectively). For the entire follow-up, risk was significantly increased in the highest tertile of albumin and for high albumin and calcium jointly. Risks for ovarian cancer differed markedly by follow-up time. In early follow-up, women in the highest tertile of serum calcium had a 2.5-fold increased risk, adjusted for height and body mass index (OR=2.47, 95% C.I. 1.12-5.45) with a significant dose-response (p=0.024). Risk was not elevated in late follow-up (OR=0.62, 95% C.I. 0.27-1.36). Similarly, in early follow-up, women in the highest tertile of serum albumin had an increased risk (OR=2.55, 95% C.I.1.22-5.49) with a significant dose-response (p=0.009). Conversely, risk was not increased in late follow-up (OR=1.36, 95% C.I. 0.65-2.83). These data confirm a prospective association between higher serum calcium and ovarian cancer. An association in early, but not late, follow-up suggests that the higher calcium reflects the presence of existing cancer. A positive association with serum albumin is novel and should be interpreted cautiously. Copyright © 2017 The Author(s). Published by Elsevier Ltd.. All rights reserved.

  1. Iodine-123-labelled serum amyloid P component scintigraphy in amyloidosis

    International Nuclear Information System (INIS)

    Saile, R.; Deveaux, M.; Marchandise, X.; Duquesnoy, B.

    1993-01-01

    This study describes the results of scintigraphy with iodine-123-labelled serum amyloid P component (SAP) as a means of establishing the distribution of organ involvement in amyloidosis. The significance of 123 I-SAP scans obtained in 15 patients with biopsy-proven AA or AL amyloidosis is discussed. Biopsy-proven amyloidosis was typically confirmed by scintigraphy, though such confirmation was not obtained in the kidneys in six patients with histological proof of extensive renal amyloid deposition. This lack of uptake may have been due to the accumulation of a major part of the 123 I-SAP in the spleen and/or liver. Twenty-four hour whole-body retention of 123 I-SAP was higher in patients with amyloidosis than in controls. Twenty-four hour tracer accumulation of the radioactivity in the extravascular compartment was notably greater in patients than in controls and appeared to be a good diagnostic criterion. We conclude that 123 I-SAP scintigraphy may be helpful for the evaluation of organ involvement not only in patients with biopsy-proven amyloidosis but also when a biopsy cannot be performed or when a strong suspicion of amyloidosis exists in spite of repeated negative biopsises. (orig.)

  2. Study the interaction between CdTe-glutathione and human serum albumin

    Energy Technology Data Exchange (ETDEWEB)

    Yang, Qing; Zhou, Xi-min; Zhu, Yi-shuo [National Key Laboratory of Applied Organic Chemistry, Lanzhou University, Lanzhou 730000 (China); Department of Chemistry, Lanzhou University, Lanzhou 730000 (China); Chen, Xing-guo, E-mail: chenxg@lzu.edu.cn [National Key Laboratory of Applied Organic Chemistry, Lanzhou University, Lanzhou 730000 (China); Department of Chemistry, Lanzhou University, Lanzhou 730000 (China)

    2013-03-15

    In this paper, glutathione (GSH) modified CdTe quantum dots (CdTe-GSH QDs) were synthesized in an aqueous solution. Then, the binding of the CdTe-GSH QDs to human serum albumin (HSA) was studied using the fluorescence spectroscopy. The quenching mechanism was investigated in terms of the association constants and basic thermodynamic parameters. The fluorescence data revealed that CdTe-GSH QDs could quench the intrinsic fluorescence of human serum albumin by a static quenching mechanism. Furthermore, alteration of the secondary protein structure in the presence of the QDs was confirmed by synchronous fluorescence spectra. - Highlights: Black-Right-Pointing-Pointer In this paper, the binding of the CdTe-GSH QDs to human serum albumin (HSA) was studied using a fluorescence spectroscopy. Black-Right-Pointing-Pointer The quenching mechanism was investigated in terms of the association constants and basic thermodynamic parameters. Black-Right-Pointing-Pointer Furthermore, alteration of the secondary protein structure in the presence of the QDs was confirmed by synchronous fluorescence spectra. Black-Right-Pointing-Pointer The research can help us assess biological toxicity of QDs and further expand the application scope of QDs.

  3. (99m) Tc-labelled human serum albumin cannot replace (125) I-labelled human serum albumin to determine plasma volume in patients with liver disease

    DEFF Research Database (Denmark)

    Henriksen, Ulrik Lütken; Henriksen, Jens H; Bendtsen, Flemming

    2013-01-01

    Summary Background and aims Determination of plasma volume (PV) is important in several clinical situations. Thus, patients with liver disease often have augmented PV as part of their sodium–water retention. This study was undertaken to compare PV determination by two indicators: technetium......-labelled human serum albumin (99mTc-HSA) and iodine-labelled human serum albumin (125I-HSA), as the former may have advantages at repeated measurements and the latter is the classical gold standard. Study population and methods In 88 patients, (64 with liver disease, mainly cirrhosis, and 24 patients without...... In all patients, a close correlation was present between PV determined by the two indicators (r = 0·89, Pdetermined with 99mTc-HSA exceeded PV determined with 125I-HSA by 367 ml (5·2 ml kg...

  4. Development of radiochemical method of analysis of binding of tritium labeled drotaverine hydrochloride with human blood serum albumin

    International Nuclear Information System (INIS)

    Kim, A.A.; Djuraeva, G.T.; Shukurov, B.V.; Mavlyanov, I.R.

    2004-01-01

    Full text: The albumin, being a basic functional linkage of numerous endogenous and exogenous substances is the most important protein of blood plasma. At the diseases connected to liver disfunction, collected in blood metabolite reduce connecting ability of albumino. The aim of the present research was a development of radiochemical method of determination of ability of albumin to bind the tritium labeled preparation drotaverine hydrochloride (no - spa). We had developed a micromethod of definition of connecting ability of albumin, allowing to analyse 20 mkl of blood serum. The method consists in incubation of tritium labeled drotaverine hydrochloride with blood serum in vitro, the following fractionation of serum proteins by gel - filtration on a microcolumn with Sephadex G-25, and direct measurement of the radioactivity connected to fraction of proteins of blood serum. The method has been tested on a series of blood serum of control group of healthy people and on a series of blood serum of patients with hepatitis B. We received quantitative characteristics of binding of drotaverine hydrochloride with albumin of patients with hepatitis B. It was preliminary established that binding ability of serum albumin of children with various forms of acute virus hepatitis tends to decrease in comparison with group of the control. Advantage of the developed radiochemical method is high precision and the high sensitivity of detection of infringement of binding ability of albumin. Application of tritium labeled drotaverine hydrochloride allows to measure directly levels of binding of a preparation with albumin

  5. Serum total protein, albumin and globulin levels in Trypanosoma ...

    African Journals Online (AJOL)

    The effect of orally administered Scoparia dulcis on Trypanosoma brucei-induced changes in serum total protein, albumin and globulin were investigated in rabbits over a period of twenty eight days. Results obtained show that infection resulted in hyperproteinaemia, hyperglobulinaemia and hypoalbuminaemia. However ...

  6. Continuous recording of long-chain acyl-coenzyme A synthetase activity using fluorescently labeled bovine serum albumin

    DEFF Research Database (Denmark)

    Demant, Erland J.F.; Nystrøm, Birthe T.

    2001-01-01

    acyl-Coenzyme A, synthetase, activity assay, fluorescence recording, fatty acid probe, serum albumin, hydroxycoumarin, detergent, micelles, Pseudomonas fragi, rat liver microsomes......acyl-Coenzyme A, synthetase, activity assay, fluorescence recording, fatty acid probe, serum albumin, hydroxycoumarin, detergent, micelles, Pseudomonas fragi, rat liver microsomes...

  7. Labelling of human serum albumin with iodine-131 for diagnosis in nuclear medicine

    International Nuclear Information System (INIS)

    Silva Valente Goncalves, R. da.

    1979-01-01

    Labelling of 131 I-human serum albumin with I-131 from a solution of 131 I-sodium iodide using chloramine T as an oxidant agent is studied. Parameters which can influence on the labelling yield like mass of human serum albumin, and chloramine T, pH of the reaction, reaction time and activity of 131 I are also studied. The purification of the labeled product by means of IRA-410 Amberlite ion-exchange resin in chloride form and the sterilization of the 131 I-human serum albumin by its passage through a 0,22μ millipore filter are carried out. The radiochemistry control of the final product by paper chromatography and the microbiological control by cultivation of microorganisms in fluid medium: nutrient broth, sodium thioglycollate broth and Sabouraud, are performed. The stability of the radiopharmaceutical until ten days after its preparation is analysed by means of radiochemical control. (Author) [pt

  8. Diagnostic performance of initial serum albumin level for predicting in-hospital mortality among aspiration pneumonia patients.

    Science.gov (United States)

    Kim, Hyosun; Jo, Sion; Lee, Jae Baek; Jin, Youngho; Jeong, Taeoh; Yoon, Jaechol; Lee, Jeong Moon; Park, Boyoung

    2018-01-01

    The predictive value of serum albumin in adult aspiration pneumonia patients remains unknown. Using data collected during a 3-year retrospective cohort of hospitalized adult patients with aspiration pneumonia, we evaluated the predictive value of serum albumin level at ED presentation for in-hospital mortality. 248 Patients were enrolled; of these, 51 cases died (20.6%). The mean serum albumin level was 3.4±0.7g/dL and serum albumin levels were significantly lower in the non-survivor group than in the survivor group (3.0±0.6g/dL vs. 3.5±0.6g/dL). In the multivariable logistic regression model, albumin was associated with in-hospital mortality significantly (adjusted odds ratio 0.30, 95% confidential interval (CI) 0.16-0.57). The area under the receiver operating characteristics (AUROC) for in-hospital survival was 0.72 (95% CI 0.64-0.80). The Youden index was 3.2g/dL and corresponding sensitivity, specificity, positive predictive value, negative predictive value, positive and negative likelihood ratio were 68.6%, 66.5%, 34.7%, 89.1%, 2.05 and 0.47, respectively. High sensitivity (98.0%) was shown at albumin level of 4.0g/dL and high specificity (94.9%) was shown at level of 2.5g/dL. Initial serum albumin levels were independently associated with in-hospital mortality among adult patients hospitalized with aspiration pneumonia and demonstrated fair discriminative performance in the prediction of in-hospital mortality. Copyright © 2017 Elsevier Inc. All rights reserved.

  9. Humant serum-albumin som proteinkilde ved dyrkning af humane oocytter, spermatozoer og praeembryoer

    DEFF Research Database (Denmark)

    Andersen, C Y; Hay-Schmidt, Anders; Byskov, A G

    1991-01-01

    patient serum as source of protein in the culture of oocytes, spermatozoa and pre-embryos in IVF-ET treatment. The pregnancy rate per transplantation was increased from 30% in the serum group (21 pregnant out of 69 transplantations) to 39% in the albumin group (26 pregnant out of 66 transplantations...... takes place, also consists of a source of protein. In order to eliminate the variability of patient sera, a prospective, randomized investigation was performed to elucidate whether a well-defined source of protein such as human serum albumin (hSA-hSA 200 mg/ml, Statens Seruminstitute) can replace......SA is recommended as the source of protein, rather than the patient's own serum in the culture of oocytes, spermatozoa and pre-embryos in IVF-ET treatment....

  10. The value of RI scintigraphy and angiography in small intestinal bleeding; Report of eight cases

    Energy Technology Data Exchange (ETDEWEB)

    Kurosawa, Susumu; Kuwata, Hajime; Kushibiki, Kyoko; Akimoto, Kimihiko; Hashimoto, Toshiyuki; Kojima, Toshiya (Showa General Hospital, Kodaira, Tokyo (Japan))

    1991-07-01

    We retrospectively reviewed eight cases of small intestinal bleeding and assessed the value of RI scintigraphy and angiography in diagnosing the bleeding site. The patients' average age was 56.2 years. Chief complaint was melena of variable degree. In most cases neither upper endoscopy nor colonoscopy was diagnostic. RI scientigraphy (Tc-99 labeled human serum albumin) showed 75% of positive rate whereas angiography showed 66.7% (4/6) of positive rate. All four cases of leiomyosarcoma and leiomyoma demonstrated hypervascular stain and/or extra-vasation in angiography whereas RI scintigraphy failed to detect active gastrointestinal bleeding in 2 of the 4 cases. Therefore angiography was considered useful for the detection of bleeding from leiomyoma and leiomyosarcoma which are often hypervascular. Scintigraphy is thought of most value in the demonstration of small amount of bleeding with minimum vascular abnormality. (author).

  11. Effect of the conditions of isolation on the physicochemical properties of human serum albumin in the norm and with pathology

    Science.gov (United States)

    Ivanov, A. I.; Zhbankov, R. G.; Korolenko, E. A.; Korolik, E. V.; Meleshchenko, L. A.; Sarnatskaya, V. V.; Nikolaev, V. G.; Nikolaichik, V. V.; Yushko, L. A.

    1997-01-01

    Differential scanning calorimetry and IR spectrosocopy were used to investigate the effect of the procedure of isolation of human serum albumin on its physicochemical characteristics. It is shown that fractionation of blood plasma with ethylene glycol followed by ion exchange chromatography can be used to obtain albumin of normal donors that is similar to the albumin in the nonfractionated plasma according to melting thermograms. Endotherms of human serum albumin samples that were obtained by affinity chromatography and preparative electrophoresis are bimodal, unlike the monophasic for albumin obtained by polyethylene glycol precipitation. These changes result from a higher content of nonetherified fatty acids in the albumin samples obtained by affinity chromatography and from modification of the secondary protein structure in the samples obtained by electrophoresis. Analysis of melting thermograms of serum albumin from patients with uremia, chronic hepatitis, and peritonitis shows that fractionation of blood with polyethylene glycol preserves the thermodynamic characteristics of the various pathological serum albumins to the greatest extent. The present results demonstrate the advantage of polyethylene glycol fractionation for isolation of native preparations of normal and “pathological” human serum albumin.

  12. Synthesis and Characterization of Bovine Serum Albumin-Conjugated Copper Sulfide Nanocomposites

    Directory of Open Access Journals (Sweden)

    Peng Huang

    2010-01-01

    Full Text Available A simple biomolecule-assisted solution route was developed to synthesize Bovine Serum Albumin-conjugated copper sulfide (CuS/BSA nanocomposites, directly using copper salts and thioacetamide (TAA as the starting materials with a zwitterionic surfactant Bovine Serum Albumin (BSA as foaming and stabilizing agent. The CuS/BSA nanocomposites have been characterized by UV, TEM, Zeta, DLS, XRD, and FTIR. The results indicate that the as-prepared CuS/BSA nanocomposites are approximate sphere with a size distribution from 10 to 35 nm in diameter and good dispersibility, depending highly on concentration of BSA concentration. These protein-assisted synthesized nanocomposites have a great potential application in biomedical engineering and microelectronics.

  13. Low antioxidant status of serum bilirubin, uric acid, albumin and creatinine in patients with myasthenia gravis.

    Science.gov (United States)

    Yang, Dehao; Su, Zhongqian; Wu, Shengjie; Bi, Yong; Li, Xiang; Li, Jia; Lou, Kangliang; Zhang, Hongyu; Zhang, Xu

    2016-12-01

    Oxidative stress and low antioxidant status play a major role in the pathogenesis of inflammatory and autoimmune diseases. Myasthenia gravis (MG) is an autoimmune condition targeting the neuromuscular junction, and its antioxidant status is still controversial. Our study aimed to investigate the correlation between the clinical characteristics of MG and the serum antioxidant status of bilirubin (Tbil, Dbil and Ibil), uric acid, albumin and creatinine. We measured serum antioxidant molecule levels of bilirubin (Tbil, Dbil and Ibil), uric acid, albumin and creatinine in 380 individuals, including 166 MG and 214 healthy controls. We found that MG patients had significantly lower serum levels of bilirubin (Tbil, Dbil and Ibil), uric acid, albumin and creatinine than healthy controls, whether male or female. Moreover, it was also shown in our study that uric acid, albumin and creatinine levels in patients with MG were correlated with disease activity and classifications performed by the Myasthenia Gravis Foundation of America. Our findings demonstrated that serum levels of bilirubin (Tbil, Dbil and Ibil), uric acid, albumin and creatinine were reduced in patients with MG. This suggested an active oxidative process in MG patients who had low antioxidant status.

  14. On the radiolysis of desoxyribonucleic acid in presence of serum albumin

    International Nuclear Information System (INIS)

    Geiger, A.M.

    1984-01-01

    The experiments were carried out on the simple model of DNA-bovine serum albumin. The two substances were solved in 10 -2 M sodium phosphate buffer pH 7 in the ratio 1 : 10, which is about the natural ratio of nucleic acid to protein in the cell. The preparations were irradiated with various doses up to 1760 Gy, in the presence of air, nitrogen, or laughing gas. The irradiated samples were then separated over the gel sepharose CL-2B using 2 x 10 -2 M sodium phosphate buffer pH 7 with and without sodium dodecyl sulphate. Photometric measurement of the fractions was done using a wavelength of 260 nm. The protein content was determined with two different colorimetric techniques, after calibrating experiments defining the linear range. In order to determine the effect of the protein on the radiosensitivity of the DNA, samples without bovine serum albumin were irradiated in the three gaseous environments with 440 Gy. Incubation of the irradiated samples with SDS, and separation in the presence of SDS, revealed information on the covalent bonds forming between DNA and bovine serum albumin, whereas gel filtration without SDS yielded information also on non-covalent bonds. (orig./EF) [de

  15. Characterizing the Interaction between tartrazine and two serum albumins by a hybrid spectroscopic approach.

    Science.gov (United States)

    Pan, Xingren; Qin, Pengfei; Liu, Rutao; Wang, Jing

    2011-06-22

    Tartrazine is an artificial azo dye commonly used in food products. The present study evaluated the interaction of tartrazine with two serum albumins (SAs), human serum albumin (HSA) and bovine serum albumin (BSA), under physiological conditions by means of fluorescence, three-dimensional fluorescence, UV-vis absorption, and circular dichroism (CD) techniques. The fluorescence data showed that tartrazine could bind to the two SAs to form a complex. The binding process was a spontaneous molecular interaction procedure, in which van der Waals and hydrogen bond interactions played a major role. Additionally, as shown by the UV-vis absorption, three-dimensional fluorescence, and CD results, tartrazine could lead to conformational and some microenvironmental changes of both SAs, which may affect the physiological functions of SAs. The work provides important insight into the mechanism of toxicity of tartrazine in vivo.

  16. Affinity extraction of emerging contaminants from water based on bovine serum albumin as a binding agent.

    Science.gov (United States)

    Papastavros, Efthimia; Remmers, Rachael A; Snow, Daniel D; Cassada, David A; Hage, David S

    2018-03-01

    Affinity sorbents using bovine serum albumin as a binding agent were developed and tested for the extraction of environmental contaminants from water. Computer simulations based on a countercurrent distribution model were also used to study the behavior of these sorbents. Several model drugs, pesticides, and hormones of interest as emerging contaminants were considered in this work, with carbamazepine being used as a representative analyte when coupling the albumin column on-line with liquid chromatography and tandem mass spectrometry. The albumin column was found to be capable of extracting carbamazepine from aqueous solutions that contained trace levels of this analyte. Further studies of the bovine serum albumin sorbent indicated that it had higher retention under aqueous conditions than a traditional C 18 support for most of the tested emerging contaminants. Potential advantages of using these protein-based sorbents included the low cost of bovine serum albumin and its ability to bind to a relatively wide range of drugs and related compounds. It was also shown how simulations could be used to describe the elution behavior of the model compounds on the bovine serum albumin sorbents as an aid in optimizing the retention and selectivity of these supports for use with liquid chromatography or methods such as liquid chromatography with tandem mass spectrometry. © 2017 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

  17. Molecular displacement of warfarin from human serum albumin by flavonoid aglycones

    International Nuclear Information System (INIS)

    Poór, Miklós; Li, Yin; Kunsági-Máté, Sándor; Petrik, József; Vladimir-Knežević, Sanda; Kőszegi, Tamás

    2013-01-01

    The well-known 4-hydroxycoumarin derivative warfarin is a widespread anticoagulant drug. Besides its strong albumin binding property warfarin has a narrow therapeutic window. Therefore, a few percent of displacement from albumin can result in serious biological consequences. The flavonoid molecular group also shows very strong plasma albumin binding characteristics occupying the same binding site. It is plausible to hypothesize that flavonoid aglycones may be able to displace warfarin from human serum albumin (HSA). In our study the competing activities of different flavone (acacetin, apigenin, chrysin, luteolin), flavonol (galangin, quercetin) and flavanone (hesperetin, naringenin) aglycones were investigated using fluorescence spectroscopy. Our results represent that flavonoids are able to displace warfarin from the surface of HSA. On the other hand, when comparing flavone or flavonol groups to flavanones the latter group seems to be much weaker competitor. These observations were also supported by calculation of stability constants. Our investigations strongly suggest that we should reckon with the described molecular displacement. However, further in vivo studies are needed to support the findings of our model system. -- Highlights: • Various flavonoids are able to displace warfarin from human serum albumin. • Flavones and flavonols are much more effective competitors than flavanones. • Even 300 nM aglycone concentrations show the interaction with 3 μM warfarin. • Flavonoid pairs show quasi-additive desorbing property. • Flavones and flavonols are much stronger competitors than the examined drugs

  18. Molecular displacement of warfarin from human serum albumin by flavonoid aglycones

    Energy Technology Data Exchange (ETDEWEB)

    Poór, Miklós [Institute of Laboratory Medicine, University of Pécs, Pécs H-7624 (Hungary); Li, Yin; Kunsági-Máté, Sándor [Department of General and Physical Chemistry, University of Pécs, Pécs H-7624 (Hungary); János Szentágothai Research Center, H-7624 Pécs (Hungary); Petrik, József [Department of Medical Biochemistry and Hematology, Faculty of Pharmacy and Biochemistry, University of Zagreb, HR-10000 Zagreb (Croatia); Vladimir-Knežević, Sanda [Department of Pharmacognosy, Faculty of Pharmacy and Biochemistry, University of Zagreb, HR-10000 Zagreb (Croatia); Kőszegi, Tamás, E-mail: koszegit@freemail.hu [Institute of Laboratory Medicine, University of Pécs, Pécs H-7624 (Hungary)

    2013-10-15

    The well-known 4-hydroxycoumarin derivative warfarin is a widespread anticoagulant drug. Besides its strong albumin binding property warfarin has a narrow therapeutic window. Therefore, a few percent of displacement from albumin can result in serious biological consequences. The flavonoid molecular group also shows very strong plasma albumin binding characteristics occupying the same binding site. It is plausible to hypothesize that flavonoid aglycones may be able to displace warfarin from human serum albumin (HSA). In our study the competing activities of different flavone (acacetin, apigenin, chrysin, luteolin), flavonol (galangin, quercetin) and flavanone (hesperetin, naringenin) aglycones were investigated using fluorescence spectroscopy. Our results represent that flavonoids are able to displace warfarin from the surface of HSA. On the other hand, when comparing flavone or flavonol groups to flavanones the latter group seems to be much weaker competitor. These observations were also supported by calculation of stability constants. Our investigations strongly suggest that we should reckon with the described molecular displacement. However, further in vivo studies are needed to support the findings of our model system. -- Highlights: • Various flavonoids are able to displace warfarin from human serum albumin. • Flavones and flavonols are much more effective competitors than flavanones. • Even 300 nM aglycone concentrations show the interaction with 3 μM warfarin. • Flavonoid pairs show quasi-additive desorbing property. • Flavones and flavonols are much stronger competitors than the examined drugs.

  19. Crystal structure of equine serum albumin in complex with cetirizine reveals a novel drug-binding site

    OpenAIRE

    Handing, Katarzyna B.; Shabalin, Ivan G.; Szlachta, Karol; Majorek, Karolina A.; Minor, Wladek

    2016-01-01

    Serum albumin (SA) is the main transporter of drugs in mammalian blood plasma. Here, we report the first crystal structure of equine serum albumin (ESA) in complex with antihistamine drug cetirizine at a resolution of 2.1 ?. Cetirizine is bound in two sites ? a novel drug binding site (CBS1) and the fatty acid binding site 6 (CBS2). Both sites differ from those that have been proposed in multiple reports based on equilibrium dialysis and fluorescence studies for mammalian albumins as cetirizi...

  20. Drug-binding ability of human serum albumin at children with chronic virus hepatitis radiochemical definition method

    International Nuclear Information System (INIS)

    Kim, A.A.; Dadakhanov, J.A.; Djuraeva, G.T.; Shukurov, B.V.; Mavlyanov, I.R.

    2006-01-01

    Full text: The chronic virus hepatitis produces numerous abnormalities of liver function. The viruses of B, C, D, F and G hepatitis possess the ability to cause chronically proceeding diseases. Earlier we have found that binding ability of serum albumin at patients with acute forms of virus hepatitis is authentically reduced in comparison with the given parameters of control group. At an acute virus hepatitis B with middle severity the reducing of binding ability of serum albumin was observed at 70 % of patients. At an acute virus hepatitis A the reduce of binding ability of serum albumin is less expressed than at acute virus hepatitis B. At of chronic virus intoxication in human organism there is a formation and accumulation of toxic compounds in the excessive concentrations, which are not inherent to a normal metabolism. One of universal mechanisms of reaction of an organism on the increasing concentration of metabolism products is formation of complexes of various compounds with blood plasma proteins. The formation in an organism of endo- and exotoxins excessive concentrations results in blocking the binding centers of albumin molecule that causes the change of its complexing ability. The purpose of the present research: investigation of binding ability of serum albumin with use of radiochemical method at children with a chronic virus hepatitis B and C. Materials and methods. Under clinical observation there were 52 children in the age from 3 till 14 years. From them at 32 the chronic virus hepatitis B was confirmed, at 20 chronic virus - hepatitis C. Etiological diagnostics was carried out by definition of specific markers of a hepatitis B and C method IFA and PCR. Binding ability of serum albumin was defined by radiochemical method with use of the tritium labeled no-spa (drotaverine hydrochloride). The control group consists from 10 conditionally health children of similar age. Results and their discussion. The results of investigation have shown, that at a

  1. Studies on the antimicrobial properties of colloidal silver nanoparticles stabilized by bovine serum albumin.

    Science.gov (United States)

    Mathew, Thomas V; Kuriakose, Sunny

    2013-01-01

    Colloidal silver nanoparticles were synthesised using sol-gel method and these nanoparticles were stabilised by encapsulated into the scaffolds of bovine serum albumin. Silver nanoparticles and encapsulated products were characterised by FTIR, NMR, XRD, TG, SEM and TEM analyses. Silver nanoparticle encapsulated bovine serum albumin showed highly potent antibacterial activity towards the bacterial strains such as Staphylococcus aureus, Serratia marcescens, Pseudomonas aeruginosa, Escherichia coli and Klebsiella pneumoniae. Copyright © 2012 Elsevier B.V. All rights reserved.

  2. Investigation of ability of serum albumin to bind the tritium labeled drotaverine hydrochloride at virus hepatitis

    International Nuclear Information System (INIS)

    Kim, A.A.; Mavlyanov, I.R.; Shukurov, B.V.; Djuraeva, G.T.

    2005-01-01

    The most of pathological conditions, and especially liver pathologies, proceeds on the background of intoxication syndromes. One of universal mechanisms of reaction of an organism on increase of concentration of toxic metabolites is removing of metabolites with the help of one of the basic protein of blood plasma - serum albumin. The purpose of the present research was studying of serum albumin ability to bind drotaverine hydrochloride at virus hepatitis in dynamics of traditional therapy. This parameter is rather important for therapy as it is known, that serum albumin is a carrier of pharmaceutical preparations. At intoxication of organism the toxic metabolites can reduce the binding capacity of serum albumin due to competitive binding and by that to reduce efficiency of carry of pharmaceutical preparations. Application of a radiochemical method with use of tritium labeled drotaverine hydrochloride in the given research it is represented to the most effective. The method of tritium labeling of pharmacological preparation of drotaverine hydrochloride was developed. Drotaverine hydrochloride was labeled by thermally activated tritium. The system of purification of tritium labeled drotaverine hydrochloride by thin layer chromatography (TLC) has been developed. Tritium labeled preparation of drotaverine hydrochloride was purified by TLC on silica gel in system isopropanol : ammonia : water (8:1:1). The output of purified tritium labeled preparation of drotaverine hydrochloride was about 25 %. The received preparation had specific radioactivity - 3,2 MBq/mg (37,4 mCi/mmol), radiochemical purity of a preparation was 95 %. We had been developed a micromethod of definition of binding ability of albumin, allowing analyze 20 microliters of blood serum. The method consists in incubation of tritium labeled drotaverine hydrochloride with blood serum in vitro, the following fractionation of serum proteins by gel - filtration on a microcolumn with Sephadex G-25, and direct

  3. Arterial blood pressure but not serum albumin concentration correlates with ADC ratio values in pediatric posterior reversible encephalopathy syndrome

    Energy Technology Data Exchange (ETDEWEB)

    Furtado, Andre; Zuccoli, Giulio [Section of Neuroradiology Children' s Hospital of Pittsburgh of UPMC, Department of Radiology, Pittsburgh, PA (United States); Hsu, Ariel [University of Pittsburgh Medical Center, Department of Radiology, Pittsburgh, PA (United States); La Colla, Luca [University of Parma, Department of Anesthesiology, Parma (Italy)

    2015-07-15

    Posterior reversible encephalopathy syndrome (PRES) is a clinical-radiological entity affecting both adults and children characterized by neurotoxicity often in setting of hypertension coupled with distinct brain magnetic resonance imaging features. Decreased serum albumin level has been suggested to correlate with the presence of vasogenic brain edema in adult PRES. Serum albumin has thus been hypothesized to protect against neurotoxicity in PRES by reducing vasogenic brain edema through its role in maintaining plasma osmotic pressure and endothelial integrity. The purpose of our study was to investigate if such correlation between decreased serum albumin level and PRES-related vasogenic edema could be found in children. We conducted a retrospective study of 25 pediatric patients diagnosed with PRES. Underlying clinical conditions, presenting symptoms, blood pressures, and serum albumin levels at onset of symptoms were collected. Brain MR imaging studies were reviewed. We used a quantitative method to evaluate the degree of vasogenic edema by measuring apparent diffusion coefficient (ADC) values of the T2-FLAIR hyperintense brain lesions. No significant correlation was found between serum albumin level and degree of PRES-related vasogenic edema. A significant correlation was found between elevated blood pressure and degree of vasogenic edema in the temporal lobes (p = 0.02 and 0.04, respectively) but not in the other cerebral lobes or cerebellum. Our initial results suggest blood pressure, not serum albumin level, as a main biomarker for brain edema in children with PRES. Thus, our study does not suggest a protective role of serum albumin against PRES-related neurotoxicity in children. (orig.)

  4. Functional bone marrow scintigraphy in psoriatics

    International Nuclear Information System (INIS)

    Munz, D.; Altmeyer, P.; Chilf, G.; Schlesinger, G.; Holzmann, H.; Hoer, G.

    1982-01-01

    24 psoriatics as well as 24 normal healthy adults were studied by functional bone marrow scintigraphy using Tc-99m-labeled human serum albumin millimicrospheres (Tc-99m-HSA-MM). Functional bone marrow scintigraphy is an in vivo test system for the assessment of various functional properties of fixed macrophages. 58% of psoriatics who had no systemic drug treatment demonstrated peripheral extension of the bone marrow space indicating hyperplasia of bone marrow macrophages. This phenomenon could be observed only in one normal subject who was a high-performance sportsman. 83% (n=6) of psoriatics with cirrhosis of liver demonstrated bone marrow extension. The 'capacity' of bone marrow macrophages to engulf Tc-99m-HSA-MM ('uptake ratio') was diminished in 42% of non-treated as well as 66% of psoriatics treated with aromatic retinoid. The phagocytic and proteolytic turnover of Tc-99m-HSA-MM in bone marrow, spleen, and liver was found to be accelerated in 66% of non-treated psoriatics, normal, accelerated or delayed in psoriatics treated with aromatic retinoid as well as considerably delayed in all of the psoriatics with cirrhosis of liver. Functional bone marrow scintigraphy proved to be an appropriate in vivo test system to reveal abnormalities of fixed macrophages in psoriatics. Furthermore, theratpeutic effects as well as influences of pre-existing disorders on different macrophage populations can be assessed. (Author)

  5. O2-mediated oxidation of ferrous nitrosylated human serum heme-albumin is limited by nitrogen monoxide dissociation

    International Nuclear Information System (INIS)

    Ascenzi, Paolo; Gullotta, Francesca; Gioia, Magda; Coletta, Massimo; Fasano, Mauro

    2011-01-01

    Research highlights: → Human serum heme-albumin displays globin-like properties. → O 2 -mediated oxidation of ferrous nitrosylated human serum heme-albumin. → Allosteric modulation of human serum heme-albumin reactivity. → Rifampicin is an allosteric effector of human serum heme-albumin. → Human serum heme-albumin is a ROS and NOS scavenger. -- Abstract: Human serum heme-albumin (HSA-heme-Fe) displays globin-like properties. Here, kinetics of O 2 -mediated oxidation of ferrous nitrosylated HSA-heme-Fe (HSA-heme-Fe(II)-NO) is reported. Values of the first-order rate constants for O 2 -mediated oxidation of HSA-heme-Fe(II)-NO (i.e., for ferric HSA-heme-Fe formation) and for NO dissociation from HSA-heme-Fe(II)-NO (i.e., for NO replacement by CO) are k = 9.8 x 10 -5 and 8.3 x 10 -4 s -1 , and h = 1.3 x 10 -4 and 8.5 x 10 -4 s -1 , in the absence and presence of rifampicin, respectively, at pH = 7.0 and T = 20.0 o C. The coincidence of values of k and h indicates that NO dissociation represents the rate limiting step of O 2 -mediated oxidation of HSA-heme-Fe(II)-NO. Mixing HSA-heme-Fe(II)-NO with O 2 does not lead to the formation of the transient adduct(s), but leads to the final ferric HSA-heme-Fe derivative. These results reflect the fast O 2 -mediated oxidation of ferrous HSA-heme-Fe and highlight the role of drugs in modulating allosterically the heme-Fe-atom reactivity.

  6. Growth Status and Its Relationship with Serum Lipids and Albumin in Children with Cystic Fibrosis

    Directory of Open Access Journals (Sweden)

    Gholam Hossein Fallahi

    2016-05-01

    Full Text Available Cystic fibrosis (CF is an autosomal recessive disease, which affects many organs as it impairs chloride channel. This study was performed to evaluate growth status and its relationship with some laboratory indices such as Cholesterol (chol, Triglyceride (TG, albumin and total protein in children with CF referred to pediatrics center. This study was designed as a cross-sectional study in one year section. Demographic features were compared with standard percentiles curves. Chol, TG, albumin, total protein, prothrombin time, and hemoglobin were measured. Stool exams were also performed. A questionnaire was designed to obtain a history of the first presentation of disease, birth weight, type of labor and parent relativity. In 52% of patients, failure to thrive (FTT was the first presentation. Steatorrhea and respiratory infections were the first presentations, which were seen in 13.7% and 33% of the cases, respectively. The weight of 88% of patients was below the 15th percentile while 82% had a height percentile below 15th. Head circumference in 53% of patients was below the 15th percentile. There was a significant association between weight percentile and serum albumin and total protein (P=0.03 and P=0.007, respectively. There was also a significant relationship between height percentile and serum albumin and total protein (P<0.001 and P<0.000, respectively. The relationships between head circumference and serum albumin and total protein were also significant (P=0.006 and P<0.000, respectively. There was also a significant association between height percentile and hemoglobin. The decrease in anthropometric percentiles leads to decreased serum albumin and total protein.

  7. Gamma scintigraphic analysis of albumin flux in patients with acute respiratory distress syndrome

    International Nuclear Information System (INIS)

    Sugerman, H.J.; Tatum, J.L.; Burke, T.S.; Strash, A.M.; Glauser, F.L.

    1984-01-01

    Computerized gamma-scintigraphy provides a new method for the analysis of albumin flux in patients with pulmonary permeability edema. In this technique, 10 mCi of 99 mTc -tagged human serum albumin is administered and lung:heart radioactivity ratios are determined. This ratio remains constant unless there is a leak of albumin, when a rising ratio with time, called the ''slope index'' (SI), is seen. Thirty-five scintigraphic studies were obtained in 28 patients by means of a portable computerized gamma-camera. Thirteen of these patients had clinical evidence of the acute respiratory distress syndrome (ARDS) and six had or were recovering from left ventricular induced congestive heart failure (CHF). Five of the patients with CHF and pulmonary capillary wedge pressure (PCWP) below 30 mm Hg had normal scintigraphic studies. The patients with ARDS were found to have significantly higher SIs than patients who did not have, or had recovered from, ARDS. Positive SIs were present from 1 to 8 days following the apparent onset of ARDS in seven studies in five patients. Recovery of gas exchange was associated with a return to a normal SI in four patients. In conclusion, computerized gamma-scintigraphy was a sensitive, noninvasive tool for the detection of a pathologic increase in pulmonary protein flux. Positive scintigraphic findings were associated with significantly impaired gas exchange. The method documented that the leak of albumin in patients with ARDS may last for days but resolves with recovery

  8. Bovine serum albumin adsorption onto functionalized polystyrene lattices: A theoretical modeling approach and error analysis

    Science.gov (United States)

    Beragoui, Manel; Aguir, Chadlia; Khalfaoui, Mohamed; Enciso, Eduardo; Torralvo, Maria José; Duclaux, Laurent; Reinert, Laurence; Vayer, Marylène; Ben Lamine, Abdelmottaleb

    2015-03-01

    The present work involves the study of bovine serum albumin adsorption onto five functionalized polystyrene lattices. The adsorption measurements have been carried out using a quartz crystal microbalance. Poly(styrene-co-itaconic acid) was found to be an effective adsorbent for bovine serum albumin molecule adsorption. The experimental isotherm data were analyzed using theoretical models based on a statistical physics approach, namely monolayer, double layer with two successive energy levels, finite multilayer, and modified Brunauer-Emmet-Teller. The equilibrium data were then analyzed using five different non-linear error analysis methods and it was found that the finite multilayer model best describes the protein adsorption data. Surface characteristics, i.e., surface charge density and number density of surface carboxyl groups, were used to investigate their effect on the adsorption capacity. The combination of the results obtained from the number of adsorbed layers, the number of adsorbed molecules per site, and the thickness of the adsorbed bovine serum albumin layer allows us to predict that the adsorption of this protein molecule can also be distinguished by monolayer or multilayer adsorption with end-on, side-on, and overlap conformations. The magnitudes of the calculated adsorption energy indicate that bovine serum albumin molecules are physisorbed onto the adsorbent lattices.

  9. Selective analysis of human serum albumin based on SEC-ICP-MS after labelling with iophenoxic acid

    DEFF Research Database (Denmark)

    Dersch, Julie Maria; Nguyen, Tam T. T. N.; Østergaard, Jesper

    2015-01-01

    Human serum albumin (HSA) is the most abundant protein in the human plasma. HSA has several physiological roles in the human body, including storage and transport. Owing to the predominance of albumin in plasma, HSA is often involved in the protein binding of drugs. The aim of this work was to de...... plasma and urine samples and for studying the binding of cisplatin to proteins in the human plasma.......Human serum albumin (HSA) is the most abundant protein in the human plasma. HSA has several physiological roles in the human body, including storage and transport. Owing to the predominance of albumin in plasma, HSA is often involved in the protein binding of drugs. The aim of this work...... was to develop a selective, quantitative method for determining albumin in plasma with the purpose of clarifying the fate of metal-based drugs in biological systems. The method can also be applied for determination of urine albumin, which is of relevance in diagnostics of kidney disease. A selective method...

  10. Crystals of Human Serum Albumin for Use in Genetic Engineering and Rational Drug Design

    Science.gov (United States)

    Carter, Daniel C. (Inventor)

    1994-01-01

    This invention pertains to crystals of serum albumin and processes for growing them. The purpose of the invention is to provide crystals of serum albumin which can be studied to determine binding sites for drugs. Form 2 crystals grow in the monoclinic space P2(sub 1), and possesses the following unit cell constraints: a = 58.9 +/- 7, b = 88.3 +/- 7, c = 60.7 +/- 7, Beta = 101.0 +/- 2 degrees. One advantage of the invention is that it will allow rational drug design

  11. Relationship between cobalamin-dependent metabolites and both serum albumin and alpha1 -proteinase inhibitor concentrations in hypocobalaminemic dogs of 7 different breeds.

    Science.gov (United States)

    Grützner, Niels; Suchodolski, Jan S; Steiner, Jörg M

    2014-12-01

    Increased serum concentrations of homocysteine (HCY) and methylmalonic acid (MMA), the 2 main cobalamin-dependent metabolites, as well as decreased serum albumin and canine alpha1 -proteinase inhibitor (cα1 -PI) concentrations have previously been described in hypocobalaminemic dogs with gastrointestinal disease. However, no studies have been conducted to evaluate potential relationships between these serum biomarkers. The aim of this study was to evaluate the relationship between HCY and MMA, 2 cobalamin-dependent metabolites, and both serum albumin and cα1 -PI concentrations in hypocobalaminemic dogs. Serum samples from 285 dogs including 7 different breeds (Beagle, Boxer, Cocker Spaniel, German Shepherd, Labrador Retriever, Chinese Shar-Pei, and Yorkshire Terrier) with hypocobalaminemia were used. Serum HCY, MMA, albumin, and cα1 -PI concentrations were determined. There was a significant correlation between serum HCY and albumin concentrations, as well as serum HCY and cα1 -PI concentrations (ρ = 0.62 and ρ = 0.37, respectively; P  .05). In addition, significant breed-specific correlations were observed between serum MMA and albumin concentrations in German Shepherds, and serum HCY and MMA concentrations in Chinese Shar-Peis with hypocobalaminemia. This study shows a correlation between serum albumin and cα1 -PI and HCY concentrations, but not with serum MMA concentration in dogs with hypocobalaminemia. In addition, significant breed-specific correlations were observed between serum MMA and albumin concentrations in German Shepherds, as well as serum HCY and MMA concentrations in Chinese Shar-Peis, emphasizing the unique metabolic interactions in those dog breeds affected by hypocobalaminemia. © 2014 American Society for Veterinary Clinical Pathology.

  12. Gender-partitioned patient medians of serum albumin requested by general practitioners for the assessment of analytical stability

    DEFF Research Database (Denmark)

    Hansen, Steen Ingemann; Petersen, Per Hyltoft; Lund, Flemming

    2017-01-01

    BACKGROUND: Recently, the use of separate gender-partitioned patient medians of serum sodium has revealed potential for monitoring analytical stability within the optimum analytical performance specifications for laboratory medicine. The serum albumin concentration depends on whether a patient...... patients were closely related despite considerable variation due to the current analytical variation. This relationship was confirmed by the calculated half-range for the monthly ratio between the genders of 0.44%, which surpasses the optimum analytical performance specification for bias of serum albumin...... (0.72%). The weekly ratio had a half-range of 1.83%, which surpasses the minimum analytical performance specifications of 2.15%. CONCLUSIONS: Monthly gender-partitioned patient medians of serum albumin are useful for monitoring of long-term analytical stability, where the gender medians are two...

  13. Quantitative aspects of recognition of the antibiotic drug oxytetracycline by bovine serum albumin: Calorimetric and spectroscopic studies

    Energy Technology Data Exchange (ETDEWEB)

    Keswani, Neelam; Choudhary, Sinjan [Department of Chemistry, Indian Institute of Technology Bombay, Powai, Mumbai 400 076 (India); Kishore, Nand [Department of Chemistry, Indian Institute of Technology Bombay, Powai, Mumbai 400 076 (India)

    2013-03-15

    Highlights: ► Thermodynamics of oxytetracycline (OTC)-bovine serum albumin (BSA) binding addressed. ► ITC and fluorescence spectroscopic analysis provide values of binding constant. ► Binding is mainly ionic, hydrophobic with minor hydrogen bonding contribution. ► Quantitative effects of OTC on BSA stability provided by DSC. ► Preferential complexation of one domain of BSA by OTC at site II is suggested. -- Abstract: A quantitative understanding of the mode of interaction of drugs with target proteins provides a guide for the synthesis of new drug molecules. The binding of the antibiotic drug oxytetracycline with serum albumin has been studied by a combination of isothermal titration calorimetry (ITC), differential scanning calorimetry (DSC), steady-state and time-resolved fluorescence spectroscopy, and circular dichroism spectroscopy. The values of the binding constant (K), enthalpy change (ΔH), entropy (ΔS), and stoichiometry of binding have been determined along with the associated conformational changes in the protein. Oxytetracycline binds to bovine serum albumin with a 1:1 stoichiometry and with a weakly temperature dependent association constant of 1.8 · 10{sup 4} at T = 298.15 K. The effect of ionic strength, tetrabutylammonium bromide, and sucrose on the thermodynamic parameters obtained from ITC and DSC measurements indicate involvement of predominantly ionic and hydrophobic interactions with a minor hydrogen bonding contribution in the drug-protein complexation. The DSC results on the binding of oxytetracycline with bovine serum albumin in the absence and presence of these additives provide quantitative information on the effect of drugs on the stability of bovine serum albumin, and suggest preferential complexation of one of the domains of the protein. The results further indicate that the drug occupies binding site II on bovine serum albumin.

  14. Quantitative aspects of recognition of the antibiotic drug oxytetracycline by bovine serum albumin: Calorimetric and spectroscopic studies

    International Nuclear Information System (INIS)

    Keswani, Neelam; Choudhary, Sinjan; Kishore, Nand

    2013-01-01

    Highlights: ► Thermodynamics of oxytetracycline (OTC)-bovine serum albumin (BSA) binding addressed. ► ITC and fluorescence spectroscopic analysis provide values of binding constant. ► Binding is mainly ionic, hydrophobic with minor hydrogen bonding contribution. ► Quantitative effects of OTC on BSA stability provided by DSC. ► Preferential complexation of one domain of BSA by OTC at site II is suggested. -- Abstract: A quantitative understanding of the mode of interaction of drugs with target proteins provides a guide for the synthesis of new drug molecules. The binding of the antibiotic drug oxytetracycline with serum albumin has been studied by a combination of isothermal titration calorimetry (ITC), differential scanning calorimetry (DSC), steady-state and time-resolved fluorescence spectroscopy, and circular dichroism spectroscopy. The values of the binding constant (K), enthalpy change (ΔH), entropy (ΔS), and stoichiometry of binding have been determined along with the associated conformational changes in the protein. Oxytetracycline binds to bovine serum albumin with a 1:1 stoichiometry and with a weakly temperature dependent association constant of 1.8 · 10 4 at T = 298.15 K. The effect of ionic strength, tetrabutylammonium bromide, and sucrose on the thermodynamic parameters obtained from ITC and DSC measurements indicate involvement of predominantly ionic and hydrophobic interactions with a minor hydrogen bonding contribution in the drug-protein complexation. The DSC results on the binding of oxytetracycline with bovine serum albumin in the absence and presence of these additives provide quantitative information on the effect of drugs on the stability of bovine serum albumin, and suggest preferential complexation of one of the domains of the protein. The results further indicate that the drug occupies binding site II on bovine serum albumin

  15. Solution behaviour of Human Serum Albumin and GLP-1variants

    DEFF Research Database (Denmark)

    Sønderby, Pernille

    interaction is critical for the long term stability of a pharmaceutical. Protein complex formation is important for extended half-life in vivo and is essential to cellular communication such as the induction of the insulin response. This thesis focuses on human serum albumin (HSA) as a central player...

  16. Cu(II) bis(thiosemicarbazone) radiopharmaceutical binding to serum albumin: further definition of species dependence and associated substituent effects

    International Nuclear Information System (INIS)

    Basken, Nathan E.; Green, Mark A.

    2009-01-01

    Introduction: The pyruvaldehyde bis(N 4 -methylthiosemicarbazonato)copper(II) (Cu-PTSM) and diacetyl bis(N 4 -methylthiosemicarbazonato)copper(II) (Cu-ATSM) radiopharmaceuticals exhibit strong, species-dependent binding to the IIA site of human serum albumin (HSA), while the related ethylglyoxal bis(thiosemicarbazonato)copper(II) (Cu-ETS) radiopharmaceutical appears to exhibit only nonspecific binding to HSA and animal serum albumins. Methods: To further probe the structural basis for the species dependence of this albumin binding interaction, we examined protein binding of these three radiopharmaceuticals in solutions of albumin and/or serum from a broader array of mammalian species (rat, sheep, donkey, rabbit, cow, pig, dog, baboon, mouse, cat and elephant). We also evaluated the albumin binding of several copper(II) bis(thiosemicarbazone) chelates offering more diverse substitution of the ligand backbone. Results: Cu-PTSM and Cu-ATSM exhibit a strong interaction with HSA that is not apparent with the albumins of other species, while the binding of Cu-ETS to albumin is much less species dependent. The strong interaction of Cu-PTSM with HSA does not appear to simply correlate with variation, relative to the animal albumins, of a single amino acid lining HSA's IIA site. Those agents that selectively interact with HSA share the common feature of only methyl or hydrogen substitution at the carbon atoms of the diimine fragment of the ligand backbone. Conclusions: The interspecies variations in albumin binding of Cu-PTSM and Cu-ATSM are not simply explained by unique amino acid substitutions in the IIA binding pocket of the serum albumins. However, the specific affinity for this region of HSA is disrupted when substituents bulkier than a methyl group appear on the imine carbons of the copper bis(thiosemicarbazone) chelate.

  17. Cu(II) bis(thiosemicarbazone) radiopharmaceutical binding to serum albumin: further definition of species dependence and associated substituent effects

    Energy Technology Data Exchange (ETDEWEB)

    Basken, Nathan E. [Division of Nuclear Pharmacy, Department of Industrial and Physical Pharmacy, Purdue University, West Lafayette, IN 47907 (United States); Green, Mark A. [Division of Nuclear Pharmacy, Department of Industrial and Physical Pharmacy, Purdue University, West Lafayette, IN 47907 (United States)], E-mail: magreen@purdue.edu

    2009-07-15

    Introduction: The pyruvaldehyde bis(N{sup 4}-methylthiosemicarbazonato)copper(II) (Cu-PTSM) and diacetyl bis(N{sup 4}-methylthiosemicarbazonato)copper(II) (Cu-ATSM) radiopharmaceuticals exhibit strong, species-dependent binding to the IIA site of human serum albumin (HSA), while the related ethylglyoxal bis(thiosemicarbazonato)copper(II) (Cu-ETS) radiopharmaceutical appears to exhibit only nonspecific binding to HSA and animal serum albumins. Methods: To further probe the structural basis for the species dependence of this albumin binding interaction, we examined protein binding of these three radiopharmaceuticals in solutions of albumin and/or serum from a broader array of mammalian species (rat, sheep, donkey, rabbit, cow, pig, dog, baboon, mouse, cat and elephant). We also evaluated the albumin binding of several copper(II) bis(thiosemicarbazone) chelates offering more diverse substitution of the ligand backbone. Results: Cu-PTSM and Cu-ATSM exhibit a strong interaction with HSA that is not apparent with the albumins of other species, while the binding of Cu-ETS to albumin is much less species dependent. The strong interaction of Cu-PTSM with HSA does not appear to simply correlate with variation, relative to the animal albumins, of a single amino acid lining HSA's IIA site. Those agents that selectively interact with HSA share the common feature of only methyl or hydrogen substitution at the carbon atoms of the diimine fragment of the ligand backbone. Conclusions: The interspecies variations in albumin binding of Cu-PTSM and Cu-ATSM are not simply explained by unique amino acid substitutions in the IIA binding pocket of the serum albumins. However, the specific affinity for this region of HSA is disrupted when substituents bulkier than a methyl group appear on the imine carbons of the copper bis(thiosemicarbazone) chelate.

  18. Association between Serum Albumin Concentration and Ketosis Risk in Hospitalized Individuals with Type 2 Diabetes Mellitus.

    Science.gov (United States)

    Cheng, Po-Chung; Hsu, Shang-Ren; Cheng, Yun-Chung

    2016-01-01

    Objective. This study examined the association between serum albumin concentration and ketosis risk in hospitalized individuals with type 2 diabetes mellitus (T2DM). Methods. A retrospective cross-sectional study was conducted at a medical center in Taiwan. Inclusion criteria were endocrinology ward inpatients exceeding 21 years of age, with preexisting diagnosis of T2DM, and blood glucose above 13.9 millimoles per liter (mmol/L) at admission. Individuals without measurement of serum albumin, urine ketone, or hemoglobin A1C, or harboring active infection, myocardial infarction, cerebrovascular event, cirrhosis, malignancy, or overt proteinuria were excluded. Using serum albumin concentration below 3.0 grams per deciliter to define hypoalbuminemia, 151 hypoalbuminemic cases and 104 normoalbuminemic controls were enrolled. The presence of ketones in urine established ketosis. Results. The prevalence of ketonuria was 48% in hypoalbuminemic subjects compared to 30% in normoalbuminemic controls (odds ratio (OR): 2.15; 95% confidence interval (CI): 1.26-3.57; P = 0.004). Moreover, among the 156 subjects with serum beta-hydroxybutyrate measurement in addition to urine ketone, 33% of the hypoalbuminemic individuals had ketonemia exceeding 3 mmol/L compared to 19% of those with normoalbuminemia (OR: 2.12, 95% CI: 0.99-4.48, P = 0.051). Conclusions. Serum albumin concentration is inversely associated with ketosis risk in hospitalized individuals with T2DM.

  19. Characterization of the interaction between 3-Oxotabersonine and two serum albumins by using spectroscopic techniques

    International Nuclear Information System (INIS)

    Wang, Qing; Yan, Jin; He, Jiawei; Bai, Keke; Li, Hui

    2013-01-01

    3-Oxotabersonine (OTAB) is a component of Voacanga africana, which is a type of traditional drug in Africa widely used for treating diseases. This study examines the interaction of OTAB with bovine serum albumin (BSA) and human serum albumin (HSA) under physiological conditions. The interaction between OTAB and BSA/HSA was investigated using fluorescence spectroscopy, Fourier transform infrared (FT-IR) spectroscopy, circular dichroism (CD) spectroscopy, and molecular modeling under simulated physiological conditions. The experimental results confirm that the quenching mechanism is a static quenching process. The binding site number (n) and the apparent binding constant (K) were measured at various temperatures. The thermodynamic parameters, namely, enthalpy change (ΔH) and entropy change (ΔS), were calculated. Furthermore, the structural changes in the serum albumin that affected the OTAB binding were determined using FT-IR. The binding site was assumed to be located in site I of the BSA/HSA (subdomain IIA). -- Highlights: ► Make use of the 3-Oxotabersonine firstly extracted from seeds of Voacanga africana Stapf to study the drug–protein system. ► Use two kinds of similar structure serum albumins to do a comparative study. ► FT-IR was used to study the conformational change of BSA and HSA. ► Use the BSA and HSA structure obtained from the Brookhaven Protein Data Bank for molecular docking

  20. Characterization of the interaction between 3-Oxotabersonine and two serum albumins by using spectroscopic techniques

    Energy Technology Data Exchange (ETDEWEB)

    Wang, Qing; Yan, Jin; He, Jiawei; Bai, Keke [College of Chemical Engineering, Sichuan University, Chengdu 610065 (China); Li, Hui, E-mail: lihuilab@sina.com [College of Chemical Engineering, Sichuan University, Chengdu 610065 (China)

    2013-06-15

    3-Oxotabersonine (OTAB) is a component of Voacanga africana, which is a type of traditional drug in Africa widely used for treating diseases. This study examines the interaction of OTAB with bovine serum albumin (BSA) and human serum albumin (HSA) under physiological conditions. The interaction between OTAB and BSA/HSA was investigated using fluorescence spectroscopy, Fourier transform infrared (FT-IR) spectroscopy, circular dichroism (CD) spectroscopy, and molecular modeling under simulated physiological conditions. The experimental results confirm that the quenching mechanism is a static quenching process. The binding site number (n) and the apparent binding constant (K) were measured at various temperatures. The thermodynamic parameters, namely, enthalpy change (ΔH) and entropy change (ΔS), were calculated. Furthermore, the structural changes in the serum albumin that affected the OTAB binding were determined using FT-IR. The binding site was assumed to be located in site I of the BSA/HSA (subdomain IIA). -- Highlights: ► Make use of the 3-Oxotabersonine firstly extracted from seeds of Voacanga africana Stapf to study the drug–protein system. ► Use two kinds of similar structure serum albumins to do a comparative study. ► FT-IR was used to study the conformational change of BSA and HSA. ► Use the BSA and HSA structure obtained from the Brookhaven Protein Data Bank for molecular docking.

  1. Diagnostic performance of I-123-labeled serum amyloid P component scintigraphy in patients with amyloidosis

    NARCIS (Netherlands)

    Hazenberg, BPC; van Rijswijk, MH; Piers, DA; Lub-de Hooge, MN; Vellenga, E; Haagsma, EB; Hawkins, PN; Jager, PL

    Purpose: To assess the diagnostic accuracy and additional information provided by I-123-labeled serum amyloid P component ( SAP) scintigraphy in patients with systemic and localized amyloidosis. Subjects and Methods: I-123-labeled human SAP was injected intravenously into 20 controls and 189

  2. A multispectroscopic and molecular docking investigation of the binding interaction between serum albumins and acid orange dye

    Science.gov (United States)

    Naveenraj, Selvaraj; Solomon, Rajadurai Vijay; Mangalaraja, Ramalinga Viswanathan; Venuvanalingam, Ponnambalam; Asiri, Abdullah M.; Anandan, Sambandam

    2018-03-01

    The interaction of Acid Orange 10 (AO10) with bovine serum albumin (BSA) was investigated comparatively with that of human serum albumin (HSA) using multispectroscopic techniques for understanding their toxic mechanism. Further, density functional theory calculations and docking studies have been carried out to gain more insights into the nature of interactions existing between AO10 and serum albumins. The fluorescence results suggest that AO10 quenched the fluorescence of BSA through the combination of static and dynamic quenching mechanism. The same trend was followed in the interaction of AO10 with HSA. In addition to the type of quenching mechanism, the fluorescence spectroscopic results suggest that the binding occurs near the tryptophan moiety of serum albumins and the binding. AO10 has more binding affinity towards BSA than HSA. An AO10-Trp model has been created to explicitly understand the Csbnd Htbnd π interactions from Bader's quantum theory of atoms in molecules analysis which confirmed that AO10 bind more strongly with BSA than that of HSA due to the formation of three hydrogen bonds with BSA whereas it forms two hydrogen bonds in the case of HSA. These obtained results provide an in-depth understanding of the interaction of the acid azo dye AO10 with serum albumins. This interaction study provides insights into the underlying reasons for toxicity of AO10 relevant to understand its effect on bovids and humans during the blood transportation process.

  3. Can Serum Albumin Level and Total Lymphocyte Count be Surrogates for Malnutrition to Predict Wound Complications After Total Knee Arthroplasty?

    Science.gov (United States)

    Morey, Vivek M; Song, Young Dong; Whang, Ji Sup; Kang, Yeon Gwi; Kim, Tae Kyun

    2016-06-01

    Although the serum albumin level and total lymphocyte count (TLC) have been reported as valid and reliable markers for defining malnutrition, their cutoff levels and predictive values for wound complications in patients undergoing total knee arthroplasty (TKA) remain questionable. A total of 3169 TKAs performed between April 2003 and December 2013 were retrospectively reviewed. We determined the prevalence of malnutrition on applying different definitions, with various cutoff values of serum albumin and TLC and analyzed the variations in outcome. The differences between groups with and without malnutrition in terms of functional outcome and complications were determined using Student's t test and analysis of variance. Multivariate logistic regression analysis was conducted to identify the independent risk factors. Among all the patients (N = 3169), the serum albumin level and TLC varied widely, with means of 4.1 g/dL and 2189 cells/mm(3), respectively. The prevalence of malnutrition (21%) as per the conventional definition (serum albumin level malnutrition was defined as serum albumin malnutrition for predicting wound complications after TKA. Copyright © 2015 Elsevier Inc. All rights reserved.

  4. Human serum albumin homeostasis: a new look at the roles of synthesis, catabolism, renal and gastrointestinal excretion, and the clinical value of serum albumin measurements

    Directory of Open Access Journals (Sweden)

    Levitt DG

    2016-07-01

    Full Text Available David G Levitt,1,* Michael D Levitt2,* 1Department of Integrative Biology and Physiology, University of Minnesota, 2Research Service, Veterans Affairs Medical Center, Minneapolis, MN, USA *These authors contributed equally to this work Abstract: Serum albumin concentration (CP is a remarkably strong prognostic indicator of morbidity and mortality in both sick and seemingly healthy subjects. Surprisingly, the specifics of the pathophysiology underlying the relationship between CP and ill-health are poorly understood. This review provides a summary that is not previously available in the literature, concerning how synthesis, catabolism, and renal and gastrointestinal clearance of albumin interact to bring about albumin homeostasis, with a focus on the clinical factors that influence this homeostasis. In normal humans, the albumin turnover time of about 25 days reflects a liver albumin synthesis rate of about 10.5 g/day balanced by renal (≈6%, gastrointestinal (≈10%, and catabolic (≈84% clearances. The acute development of hypoalbuminemia with sepsis or trauma results from increased albumin capillary permeability leading to redistribution of albumin from the vascular to interstitial space. The best understood mechanism of chronic hypoalbuminemia is the decreased albumin synthesis observed in liver disease. Decreased albumin production also accounts for hypoalbuminemia observed with a low-protein and normal caloric diet. However, a calorie- and protein-deficient diet does not reduce albumin synthesis and is not associated with hypoalbuminemia, and CP is not a useful marker of malnutrition. In most disease states other than liver disease, albumin synthesis is normal or increased, and hypoalbuminemia reflects an enhanced rate of albumin turnover resulting either from an increased rate of catabolism (a poorly understood phenomenon or enhanced loss of albumin into the urine (nephrosis or intestine (protein-losing enteropathy. The latter may occur

  5. Interaction of serum albumins with cyclodextrins: How safe is the use ...

    Indian Academy of Sciences (India)

    Interaction of cyclodextrins with human and bovine serum albumin: A combined spectroscopic and computational investigation. Saptarshi Ghosh, Bijan Kumar Paul, Nitin Chattopadhyay*. Department of Chemistry, Jadavpur University, Kolkata - 700 032, India. *Corresponding author: Fax: 91-33-2414 6584. E-mail: ...

  6. [Peculiarities of secondary structure of serum albumin of some representatives of the animal kingdom].

    Science.gov (United States)

    Pekhymenko, G V; Kuchmerovskaia, T M

    2011-01-01

    Methods of infrared (IR) spectroscopy and circular dichroism (CD) are suitable techniques for detection of proteins structural changes. These methods were used for determinating peculiarities of the secondary structure of serum albumins in some representatives of two classes of reptiles: Horsfield's tortoise (Testudo horsfieldi), water snake (Natrix tessellata) and grass snake (Natrix natrix) and birds: domestic goose (Anser anser), domestic chicken (Gallus domesticus), domestic duck (Anas platyrhyncha) and dove colored (Columba livia). An analysis of IR spectra and spectra obtained by the method of CD of serum albumins of both classes representatives revealed that beta-folding structure and alpha-helical sections that form the alpha-conformation play an important role in conformational structure formation of polypeptide chain and also disordered sites of molecules of these proteins. It was observed that certain redistribution depending on animals species exists, in the formation of secondary structure of serum albumins of the investigated representatives of reptiles and birds classes between the content of beta-folding structure, alpha-helical sections and disordered sites in molecules of these proteins.

  7. 99mTc-sucralfate scintigraphy in inflammatory bowel disease

    International Nuclear Information System (INIS)

    Mortensen, P.B.; Lech, Y.; Moeller-Petersen, J.; Vilien, M.; Fallingborg, J.; Ekelund, S.

    1989-01-01

    Technetium-99m-labelled albumin-sucralfate was orally administered to 11 patients (Crohn's disease, 8; ulcerative colitis, 3) and 3 healthy volunteers. Serial scintigraphy was performed, and scintigraphic interpretations were compared with radiographic end endoscopic findings in an open study. It was not possible in any patient to relate the scintigraphic findings to the localizations of inflammatory bowel disease, nor was it possible to distinguish the scans in the patients from the scans of the healthy volunteers. It is concluded the 99m Tc-albumin-sucralfate scintigraphy is of no value in the detection of inflammatory bowel disease. 8 refs

  8. Antioxidant flavonoids bind human serum albumin

    Science.gov (United States)

    Kanakis, C. D.; Tarantilis, P. A.; Polissiou, M. G.; Diamantoglou, S.; Tajmir-Riahi, H. A.

    2006-10-01

    Human serum albumin (HSA) is a principal extracellular protein with a high concentration in blood plasma and carrier for many drugs to different molecular targets. Flavonoids are powerful antioxidants and prevent DNA damage. The antioxidative protections are related to their binding modes to DNA duplex and complexation with free radicals in vivo. However, flavonoids are known to inhibit the activities of several enzymes such as calcium phospholipid-dependent protein kinase, tyrosine protein kinase from rat lung, phosphorylase kinase, phosphatidylinositol 3-kinase and DNA topoisomerases that exhibit the importance of flavonoid-protein interaction. This study was designed to examine the interaction of human serum albumin (HSA) with quercetin (que), kaempferol (kae) and delphinidin (del) in aqueous solution at physiological conditions, using constant protein concentration of 0.25 mM (final) and various drug contents of 1 μM-1 mM. FTIR and UV-vis spectroscopic methods were used to determine the polyphenolic binding mode, the binding constant and the effects of flavonoid complexation on protein secondary structure. The spectroscopic results showed that flavonoids are located along the polypeptide chains through H-bonding interactions with overall affinity constant of Kque = 1.4 × 10 4 M -1, Kkae = 2.6 × 10 5 M -1 and Kdel = 4.71 × 10 5 M -1. The protein secondary structure showed no alterations at low pigment concentration (1 μM), whereas at high flavonoid content (1 mM), major reduction of α-helix from 55% (free HSA) to 42-46% and increase of β-sheet from 15% (free HSA) to 17-19% and β-anti from 7% (free HSA) to 10-20% occurred in the flavonoid-HSA adducts. The major reduction of HSA α-helix is indicative of a partial protein unfolding upon flavonoid interaction.

  9. Calorimetric investigation of diclofenac drug binding to a panel of moderately glycated serum albumins.

    Science.gov (United States)

    Indurthi, Venkata S K; Leclerc, Estelle; Vetter, Stefan W

    2014-08-01

    Glycation alters the drug binding properties of serum proteins and could affect free drug concentrations in diabetic patients with elevated glycation levels. We investigated the effect of bovine serum albumin glycation by eight physiologically relevant glycation reagents (glucose, ribose, carboxymethyllysine, acetoin, methylglyoxal, glyceraldehyde, diacetyl and glycolaldehyde) on diclofenac drug binding. We used this non-steroidal anti-inflammatory drug diclofenac as a paradigm for acidic drugs with high serum binding and because of its potential cardiovascular risks in diabetic patients. Isothermal titration calorimetry showed that glycation reduced the binding affinity Ka of serum albumin and diclofenac 2 to 6-fold by reducing structural rigidity of albumin. Glycation affected the number of drug binding sites in a glycation reagent dependent manner and lead to a 25% decrease for most reagent, expect for ribose, with decreased by 60% and for the CML-modification, increased the number of binding sites by 60%. Using isothermal titration calorimetry and differential scanning calorimetry we derived the complete thermodynamic characterization of diclofenac binding to all glycated BSA samples. Our results suggest that glycation in diabetic patients could significantly alter the pharmacokinetics of the widely used over-the-counter NSDAI drug diclofenac and with possibly negative implications for patients. Copyright © 2014 Elsevier B.V. All rights reserved.

  10. Binding of streptomycin with bovine serum albumin: Energetics and conformational aspects

    International Nuclear Information System (INIS)

    Jha, Niki S.; Kishore, Nand

    2009-01-01

    Thermodynamics of the binding of antibiotic streptomycin to bovine serum albumin have been studied using isothermal titration calorimetry in combination with fluorescence, UV-vis and circular dichroism spectroscopies. The values of van't Hoff enthalpy calculated from the temperature dependence of the binding constant do not agree with the calorimetric enthalpies indicating temperature dependent conformational changes in the protein upon binding. With increase in the ionic strength, reduction in the binding affinity of streptomycin to BSA is observed suggesting the predominance of electrostatic interactions in the binding. The contribution of hydrophobic interactions in the binding is also demonstrated by decrease in binding affinity in the presence of tetrabutylammonium bromide (TBAB). The value of binding affinity in the presence of sucrose indicates that hydrogen bonding is not a significant contribution in complexation. The results have permitted quantitative evaluation of the interaction of streptomycin with bovine serum albumin

  11. Synthesis of fluorine-18 radio-labeled serum albumins for PET blood pool imaging

    International Nuclear Information System (INIS)

    Basuli, Falguni; Li, Changhui; Xu, Biying; Williams, Mark; Wong, Karen; Coble, Vincent L.; Vasalatiy, Olga; Seidel, Jurgen; Green, Michael V.; Griffiths, Gary L.; Choyke, Peter L.; Jagoda, Elaine M.

    2015-01-01

    We sought to develop a practical, reproducible and clinically translatable method of radiolabeling serum albumins with fluorine-18 for use as a PET blood pool imaging agent in animals and man. Fluorine-18 radiolabeled fluoronicotinic acid-2,3,5,6-tetrafluorophenyl ester, [ 18 F]F-Py-TFP was prepared first by the reaction of its quaternary ammonium triflate precursor with [ 18 F]tetrabutylammonium fluoride ([ 18 F]TBAF) according to a previously published method for peptides, with minor modifications. The incubation of [ 18 F]F-Py-TFP with rat serum albumin (RSA) in phosphate buffer (pH 9) for 15 min at 37–40 °C produced fluorine-18-radiolabeled RSA and the product was purified using a mini-PD MiniTrap G-25 column. The overall radiochemical yield of the reaction was 18–35% (n = 30, uncorrected) in a 90-min synthesis. This procedure, repeated with human serum albumin (HSA), yielded similar results. Fluorine-18-radiolabeled RSA demonstrated prolonged blood retention (biological half-life of 4.8 hours) in healthy awake rats. The distribution of major organ radioactivity remained relatively unchanged during the 4 hour observation periods either by direct tissue counting or by dynamic PET whole-body imaging except for a gradual accumulation of labeled metabolic products in the bladder. This manual method for synthesizing radiolabeled serum albumins uses fluorine-18, a widely available PET radionuclide, and natural protein available in both pure and recombinant forms which could be scaled up for widespread clinical applications. These preclinical biodistribution and PET imaging results indicate that [ 18 F]RSA is an effective blood pool imaging agent in rats and might, as [ 18 F]HSA, prove similarly useful as a clinical imaging agent

  12. Synthesis of fluorine-18 radio-labeled serum albumins for PET blood pool imaging.

    Science.gov (United States)

    Basuli, Falguni; Li, Changhui; Xu, Biying; Williams, Mark; Wong, Karen; Coble, Vincent L; Vasalatiy, Olga; Seidel, Jurgen; Green, Michael V; Griffiths, Gary L; Choyke, Peter L; Jagoda, Elaine M

    2015-03-01

    We sought to develop a practical, reproducible and clinically translatable method of radiolabeling serum albumins with fluorine-18 for use as a PET blood pool imaging agent in animals and man. Fluorine-18 radiolabeled fluoronicotinic acid-2,3,5,6-tetrafluorophenyl ester, [(18)F]F-Py-TFP was prepared first by the reaction of its quaternary ammonium triflate precursor with [(18)F]tetrabutylammonium fluoride ([(18)F]TBAF) according to a previously published method for peptides, with minor modifications. The incubation of [(18)F]F-Py-TFP with rat serum albumin (RSA) in phosphate buffer (pH9) for 15 min at 37-40 °C produced fluorine-18-radiolabeled RSA and the product was purified using a mini-PD MiniTrap G-25 column. The overall radiochemical yield of the reaction was 18-35% (n=30, uncorrected) in a 90-min synthesis. This procedure, repeated with human serum albumin (HSA), yielded similar results. Fluorine-18-radiolabeled RSA demonstrated prolonged blood retention (biological half-life of 4.8 hours) in healthy awake rats. The distribution of major organ radioactivity remained relatively unchanged during the 4 hour observation periods either by direct tissue counting or by dynamic PET whole-body imaging except for a gradual accumulation of labeled metabolic products in the bladder. This manual method for synthesizing radiolabeled serum albumins uses fluorine-18, a widely available PET radionuclide, and natural protein available in both pure and recombinant forms which could be scaled up for widespread clinical applications. These preclinical biodistribution and PET imaging results indicate that [(18)F]RSA is an effective blood pool imaging agent in rats and might, as [(18)F]HSA, prove similarly useful as a clinical imaging agent. Published by Elsevier Inc.

  13. Intraarterial Scintigraphy in recurrent Cervix Cancer - The Evaluation of Radionuclide therapeutic Trials -

    International Nuclear Information System (INIS)

    Kim, Eun Young; Suh, Jin Suck; Park, Chang Yun; Lee, Jong Tae; Yoo, Hyung Sik

    1990-01-01

    We performed 17 intraarterial scintigraphies in six patients with recurrent cervix cancer. With Seldinger method, the agent (four different radiopharmaceuticals) was perfused at the same speed of infusion of anticancer drugs (25 cc/hour) through internal iliac artery. There were four different radiopharmaceuticals; 131 I-Lipiodol, 99m Tc(Technetium)-HSA (Human Serum Albumin), 99m Tc-Sucralfate and 99m Tc-MAA (Macroaggregated Albumin). We evaluate the distribution pattern of radioactivity by the use of ratio of Tumor/Extratumor uptake (T/ET ratio). Our results reveals that 99m Tc-MAA scan showed the highest T/ET ratio and the other were not ideal agents for intraarterial therapy of recurrent cervix cancer. In conclusion, an ideal radioisotope and tracer which can block capillary, for example MAA, should be re-evaluated or produced in order to treat the patient with recurrent cervix cancer.

  14. Mechanism of anti-HIV activity of succinylated human serum albumin

    NARCIS (Netherlands)

    Kuipers, ME; Berg, HVD; Swart, PJ; Laman, Jon; Meijer, DKF; Kopelman, MHGM; Huisman, H

    1999-01-01

    In the present study, we described the interaction of succinylated human serum albumin (Suc-HSA), a negatively charged anti-HIV-1 active protein, with HIV-1 gp120 and in detail with the third variable domain of gp120 (V3 loop). To this end, different assay formats were tested in which gp120- and

  15. Study of Interactions of an Anticancer Drug Neratinib With Bovine Serum Albumin: Spectroscopic and Molecular Docking Approach

    OpenAIRE

    Tanveer A. Wani; Ahmed H. Bakheit; Ahmed H. Bakheit; M. A. Abounassif; Seema Zargar

    2018-01-01

    Binding of therapeutic agents to plasma proteins, particularly to serum albumin, provides valuable information in the drug development. This study was designed to evaluate the binding interaction of neratinib with bovine serum albumin (BSA). Neratinib blocks HER2 signaling and is effective in trastuzumab-resistant breast cancer treatment. Spectrofluorometric, UV spectrophotometric, and fourier transform infrared (FT-IR) and molecular docking experiments were performed to study this interactio...

  16. Supplements in human islet culture: human serum albumin is inferior to fetal bovine serum.

    Science.gov (United States)

    Avgoustiniatos, Efstathios S; Scott, William E; Suszynski, Thomas M; Schuurman, Henk-Jan; Nelson, Rebecca A; Rozak, Phillip R; Mueller, Kate R; Balamurugan, A N; Ansite, Jeffrey D; Fraga, Daniel W; Friberg, Andrew S; Wildey, Gina M; Tanaka, Tomohiro; Lyons, Connor A; Sutherland, David E R; Hering, Bernhard J; Papas, Klearchos K

    2012-01-01

    Culture of human islets before clinical transplantation or distribution for research purposes is standard practice. At the time the Edmonton protocol was introduced, clinical islet manufacturing did not include culture, and human serum albumin (HSA), instead of fetal bovine serum (FBS), was used during other steps of the process to avoid the introduction of xenogeneic material. When culture was subsequently introduced, HSA was also used for medium supplementation instead of FBS, which was typically used for research islet culture. The use of HSA as culture supplement was not evaluated before this implementation. We performed a retrospective analysis of 103 high-purity islet preparations (76 research preparations, all with FBS culture supplementation, and 27 clinical preparations, all with HSA supplementation) for oxygen consumption rate per DNA content (OCR/DNA; a measure of viability) and diabetes reversal rate in diabetic nude mice (a measure of potency). After 2-day culture, research preparations exhibited an average OCR/DNA 51% higher (p < 0.001) and an average diabetes reversal rate 54% higher (p < 0.05) than clinical preparations, despite 87% of the research islet preparations having been derived from research-grade pancreata that are considered of lower quality. In a prospective paired study on islets from eight research preparations, OCR/DNA was, on average, 27% higher with FBS supplementation than that with HSA supplementation (p < 0.05). We conclude that the quality of clinical islet preparations can be improved when culture is performed in media supplemented with serum instead of albumin.

  17. Serum Albumin as a Prognostic Marker for Serious Non-AIDS Endpoints in the Strategic Timing of Antiretroviral Treatment (START) Study

    DEFF Research Database (Denmark)

    Ronit, Andreas; Sharma, Shweta; Baker, Jason V

    2018-01-01

    of Antiretroviral Treatment (START) study (NCT00867048) with serum albumin as a fixed and time-updated predictor. Models with exclusion of events during initial follow-up years were built to assess the ability of serum albumin to predict beyond shorter periods of time. Secondarily, we considered hospitalizations...... of serious non-AIDS events (hazard ratio, 0.37 [95% confidence interval, .20-.71]; P = .002). Similar results were obtained in a time-updated model, after controlling for interleukin 6, and after excluding initial follow-up years. Serum albumin was independently associated with hospitalization......Background: Serum albumin may be used to stratify human immunodeficiency virus (HIV)-infected persons with high CD4 count according to their risk of serious non-AIDS endpoints. Methods: Cox proportional hazards models were used to analyze the risk of serious non-AIDS events in the Strategic Timing...

  18. Elevated serum creatinine and low albumin are associated with poor outcomes in patients with liposarcoma.

    Science.gov (United States)

    Panotopoulos, Joannis; Posch, Florian; Funovics, Philipp T; Willegger, Madeleine; Scharrer, Anke; Lamm, Wolfgang; Brodowicz, Thomas; Windhager, Reinhard; Ay, Cihan

    2016-03-01

    Low serum albumin levels and impaired kidney function have been associated with decreased survival in patients with a variety of cancer types. In a retrospective cohort study, we analyzed 84 patients with liposarcoma treated at from May 1994 to October 2011. Uni- and multivariable Cox proportional hazard models and competing risk analyses were performed to evaluate the association between putative biomarkers with disease-specific and overall survival. The median age of the study population was 51.7 (range 19.6-83.8) years. In multivariable analysis adjusted for AJCC tumor stage, serum creatinine was highly associated with disease-specific survival (Subdistribution Hazard ratio (SHR) per 1 mg/dl increase = 2.94; 95%CI 1.39-6.23; p = 0.005). High albumin was associated with improved overall and disease-specific survival (Hazard Ratio (HR) per 10 units increase = 0.50; 95%CI 0.26-0.95; p = 0.033 and SHR = 0.64; 95%CI 0.42-1.00; p = 0.049). The serum albumin-creatinine-ratio emerged to be associated with both overall and disease-specific survival after adjusting for AJCC tumor stage (HR = 0.95; 95%CI 0.92-0.99; p = 0.011 and SHR = 0.96; 95%CI 0.93-0.99; p = 0.08). Our study provides evidence for a tumor-stage-independent association between higher creatinine and lower albumin with worse disease-specific survival. Low albumin and a high albumin-creatinine-ratio independently predict poor overall survival. Our work identified novel prognostic biomarkers for prognosis of patients with liposarcoma. © 2015 Orthopaedic Research Society. Published by Wiley Periodicals, Inc.

  19. Use of mep HyperCel for polishing of human serum albumin.

    Science.gov (United States)

    McCann, Karl B; Vucica, Yvonne; Wu, John; Bertolini, Joseph

    2014-10-15

    The manufacture of human serum albumin by chromatographic procedures involves gel filtration chromatography as a final polishing step. Despite this step being essential to remove high molecular weight impurity proteins and thus ensure a stable and safe final product, it is relatively inefficient. This paper explores the use of hydrophobic charge induction chromatographic media, MEP HyperCel as an alternative to Sephacryl S200HR gel filtration for the polishing of human serum albumin derived by ion exchange chromatographic purification of Cohn Supernatant I. The use of MEP HyperCel results in a product with a higher purity than achieved with gel filtration and in a less time consuming manner and with potential resource savings. MEP HyperCel appears to have great potential for incorporation into downstream processes in the plasma fractionation industry as an efficient means of achieving polishing of intermediates or capture of proteins of interest. Copyright © 2014 Elsevier B.V. All rights reserved.

  20. Evaluation of the binding effect of human serum albumin on the properties of granules.

    Science.gov (United States)

    Kristó, Katalin; Bajdik, János; Eros, István; Pintye-Hódi, Klára

    2008-11-01

    The main objective of this study was the application of a solution of human serum albumin as a granulating fluid. The properties of the granules formed were evaluated and compared with those when a conventional binder was applied in the same concentration. The powder mixture contained a soluble (mannitol) and an insoluble component (different types of cellulose). The protein solution applied exerted an appropriate aggregating effect if the system contained microcrystalline celluloses. Powdered cellulose was not suitable for the granulation with human serum albumin solution. As compared with the same concentration of the conventionally applied cellulose ethers as binder, the prepared granules exhibited a larger particle size, a significantly better compressibility, a higher breaking hardness and a favourable deformation process. These findings mainly reflect the good adhesive properties of the protein. The best compressibility and mechanical behaviour were attained on the application of the microcrystalline cellulose Vivapur type 105. This favourable behaviour may be connected with the wettability of cellulose. These results suggest that the formulation of tablets may be easier from an active agent in the serum that binds to albumin (e.g. interferon) since the amount of additives (binder) can be reduced.

  1. sup 99m Tc-sucralfate scintigraphy in inflammatory bowel disease

    Energy Technology Data Exchange (ETDEWEB)

    Mortensen, P.B.; Lech, Y.; Moeller-Petersen, J.; Vilien, M.; Fallingborg, J. (Aalborg Sygehus (Denmark)); Ekelund, S. (Copenhagen County Hospital (Denmark))

    1989-01-01

    Technetium-99m-labelled albumin-sucralfate was orally administered to 11 patients (Crohn's disease, 8; ulcerative colitis, 3) and 3 healthy volunteers. Serial scintigraphy was performed, and scintigraphic interpretations were compared with radiographic end endoscopic findings in an open study. It was not possible in any patient to relate the scintigraphic findings to the localizations of inflammatory bowel disease, nor was it possible to distinguish the scans in the patients from the scans of the healthy volunteers. It is concluded the {sup 99m}Tc-albumin-sucralfate scintigraphy is of no value in the detection of inflammatory bowel disease. 8 refs.

  2. Serum albumin level predicts initial intravenous immunoglobulin treatment failure in Kawasaki disease.

    Science.gov (United States)

    Kuo, Ho-Chang; Liang, Chi-Di; Wang, Chih-Lu; Yu, Hong-Ren; Hwang, Kao-Pin; Yang, Kuender D

    2010-10-01

    Kawasaki disease (KD) is a systemic vasculitis primarily affecting children who are initial IVIG treatment. This study was conducted to investigate the risk factors for initial IVIG treatment failure in KD. Children who met KD diagnosis criteria and were admitted for IVIG treatment were retrospectively enrolled for analysis. Patients were divided into IVIG-responsive and IVIG-resistant groups. Initial laboratory data before IVIG treatment were collected for analysis. A total of 131 patients were enrolled during the study period. At 48 h after completion of initial IVIG treatment, 20 patients (15.3%) had an elevated body temperature. Univariate analysis showed that patients who had initial findings of high neutrophil count, abnormal liver function, low serum albumin level (≤2.9 g/dL) and pericardial effusion were at risk for IVIG treatment failure. Multivariate analysis with a logistic regression procedure showed that serum albumin level was considered the independent predicting factor of IVIG resistance in patients with KD (p = 0.006, OR = 40, 95% CI: 52.8-562). There was no significant correlation between age, gender, fever duration before IVIG treatment, haemoglobin level, total leucocyte and platelet counts, C-reactive protein level, or sterile pyuria and initial IVIG treatment failure. The specificity and sensitivity for prediction of IVIG treatment failure in this study were 96% and 34%, respectively. Pre-IVIG treatment serum albumin levels are a useful predictor of IVIG resistance in patients with KD. © 2010 The Author(s)/Journal Compilation © 2010 Foundation Acta Paediatrica.

  3. Monoclonal antibodies specific to sailfish serum albumin: development of an assay for the identification of fish species in the field.

    Science.gov (United States)

    Rossi, E A; Shepard, S R; Poyer, J C; Hartmann, J X

    1992-06-01

    Balb/c mice were immunized with albumin purified from sailfish (Istiophorus albicans) serum. Hybridomas were produced and screened by ELISA for reactivity with the purified albumins of sailfish, blue marlin (Makaira nigricans) and white marlin (Tetrapturus albidus). Monoclonal antibodies (MAbs) from 16 different clones exhibited activity against sailfish albumin. Thirteen of the MAbs showed cross-reactivity with the marlin species. Three MAbs exhibited distinct specificity for sailfish albumin. One of these species specific MAbs (M2D1) was conjugated to horseradish peroxidase (HRP) in order to construct an ELISA for identification of sailfish from serum. The ELISA for sailfish correctly identified eight sailfish from 26 billfish serum samples. The MAb-peroxidase conjugate was highly specific toward sailfish in that no reaction against heterologous species was detected.

  4. Determination of serum albumin, analytical challenges: a French multicenter study.

    Science.gov (United States)

    Rossary, Adrien; Blondé-Cynober, Françoise; Bastard, Jean-Philippe; Beauvieux, Marie-Christine; Beyne, Pascale; Drai, Jocelyne; Lombard, Christine; Anglard, Ingrid; Aussel, Christian; Claeyssens, Sophie; Vasson, Marie-Paule

    2017-06-01

    Among the biological markers of morbidity and mortality, albumin holds a key place in the range of criteria used by the High Authority for Health (HAS) for the assessment of malnutrition and the coding of information system medicalization program (PMSI). If the principle of quantification methods have not changed in recent years, the dispersion of external evaluations of the quality (EEQ) data shows that the standardization using the certified reference material (CRM) 470 is not optimal. The aim of this multicenter study involving 7 sites, conducted by a working group of the French Society of Clinical Biology (SFBC), was to assess whether the albuminemia values depend on the analytical system used. The albumin from plasma (n=30) and serum (n=8) pools was quantified by 5 different methods [bromocresol green (VBC) and bromocresol purple (PBC) colorimetry, immunoturbidimetry (IT), immunonephelometry (IN) and capillary electrophoresis (CE)] using 12 analyzers. Bland and Altman's test evaluated the difference between the results obtained by the different methods. For example, a difference as high as 13 g/L was observed for the same sample between the methods (p albumin across the range of values tested compared to PBC (p albumin values inducing a difference of performance between the immunoprecipitation methods (IT vs IN, p albumin results are related to the technical/analyzer tandem used. This variability is usually not taken into account by the clinician. Thus, clinicians and biologists have to be aware and have to check, depending on the method used, the albumin thresholds identified as risk factors for complications related to malnutrition and PMSI coding.

  5. Serum albumin predicts survival in patients with hilar cholangiocarcinoma.

    Science.gov (United States)

    Waghray, Abhijeet; Sobotka, Anastasia; Marrero, Carlos Romero; Estfan, Bassam; Aucejo, Federico; Narayanan Menon, K V

    2017-02-01

    Hilar cholangiocarcinoma is a devastating malignancy with incidence varying by geography and other risk factors. Rapid progression of disease and delays in diagnosis restrict the number of patients eligible for curative therapy. The objective of this study was to determine prognostic factors of overall survival in all patients presenting with hilar cholangiocarcinoma. All adult patients with histologically confirmed hilar cholangiocarcinoma from 2003 to 2013 were evaluated for predictors of survival using demographic factors, laboratory data, symptoms and radiological characteristics at presentation. A total of 116 patients were identified to have pathological diagnosis of hilar cholangiocarcinoma and were included in the analysis. Patients with a serum albumin level >3.0 g/dL (P 3.0 g/dL was identified as an independent predictor of overall survival (hazard ratio 0.31; 95% confidence interval 0.14-0.70) with a survival benefit of 44 weeks. This study was the largest analysis to date of prognostic factors in patients with hilar cholangiocarcinoma. A serum albumin level >3.0 g/dL conferred an independent survival advantage with a significantly greater length of survival. © The Author(s) 2016. Published by Oxford University Press and Sixth Affiliated Hospital of Sun Yat-Sen University.

  6. SPECTROPHOTOMETRIC ANALYSIS OF BOVINE SERUM ALBUMIN IN PRESENCE OF 1-(4-METHYLPHENYL)-3-PHENYLPROP-2-EN-1-ONES

    OpenAIRE

    S. Garg; N. Raghav

    2013-01-01

    A series of chalcones was synthesized by the Claisen-Schmidt condensation and the structures of 1- (4-methylphenyl)-3-phenylprop-2-en-1-ones were established with the help of IR and NMR study, then their effect was observed on bovine serum albumin. We have found that the synthesized chalcones interacted with bovine serum albumin and produce a great effect on their presence.

  7. Spectroscopic analysis of the interaction between tetra-(p-sulfoazophenyl-4-aminosulfonyl-substituted aluminum (III phthalocyanines and serum albumins

    Directory of Open Access Journals (Sweden)

    Liqin Zheng

    2017-03-01

    Full Text Available The binding interaction between tetra-(p-sulfoazophenyl-4-aminosulfonyl-substituted aluminum (III phthalocyanine (AlPc, and two-serum albumins (bovine serum albumin (BSA and human serum albumin (HSA has been investigated. AlPc could quench the intrinsic fluorescence of BSA and HSA through a static quenching process. The primary and secondary binding sites of AlPc on BSA were domain I and III of BSA. The primary binding site of AlPc on HSA was domain I, and the secondary binding sites of AlPc on HSA were found at domains I and II. Our results suggest that AlPc readily interact with BSA and HSA implying that the amphiphilic substituents AlPc may contribute to their transportation in the blood.

  8. Contribution to the study of plasmatic fibrinogen and serum albumin: effects of irradiation; Contribution a l'etude du fibrinogene et de la serum-albumine plasmatiques - effets de l'irradiation

    Energy Technology Data Exchange (ETDEWEB)

    Suscillon, M [Commissariat a l' Energie Atomique, Centre d' Etudes Nucleaires de Grenoble, 38 (France)

    1967-07-01

    The author studies the modifications of properties and structure of serum albumin and fibrinogen solution when subjected to radiation of low energy (X rays). On the other hand, two original techniques are exposed: 1. Amperometric determination of fibrin stabilizing factor or factor XIII of hemostasis. 2. Spectrophotometric study of fibrin formation kinetics. Then showing off and quantitative determination of platelets fibrinogen is exposed. (author) [French] L'auteur etudie les modifications des proprietes et de la structure des molecules de serum-albumine et de fibrinogene en solution soumise a un flux de RX de basse energie. D'autre part deux techniques originales sont exposees : 1. Dosage amperometrique du facteur stabilisant de la fibrine. 2. Etude spectrophotometrique de la cinetique de la fibro-formation. Enfin une mise en evidence et un dosage du fibrinogene plaquettaire sont presentes. (auteur)

  9. Comparison of Tc-99m GSA scintigraphy and CT volumetry for evaluation in portal vein embolization.

    Science.gov (United States)

    Kono, Yumiko; Kariya, Shuji; Komemushi, Atsushi; Nakatani, Miyuki; Yoshida, Rie Yagi; Suzuki, Satoshi; Ha-Kawa, Sung Kil; Utsunomiya, Keita; Ueno, Yasuhiro; Satoi, Sohei; Kaibori, Masaki; Kon, Masanori; Tanigawa, Noboru

    2014-08-01

    To determine the correlation of the rate of change of each future remnant liver (FRL) before and after portal vein embolization (PVE), by CT volumetry and Tc-99m galactosyl human serum albumin scintigraphy (GSA scintigraphy). From December 2007 to July 2012, ten patients underwent PVE before hepatic resection. CT volumetry and GSA scintigraphy were performed before and after PVE. The FRL was divided at Cantlie's line for CT volumetry, and volume change rates before and after PVE were calculated. The maximum removal rate (Rmax) was calculated using a radiopharmacokinetic model in GSA scintigraphy. The FRL Rmax change rates before and after PVE were calculated. The correlation between the volume change rates and the Rmax change rates was analyzed. The FRL volume change rate was 1.28 ± 0.26 (mean ± SD); the FRL hypertrophied in all patients significantly (p = 0.005). The FRL Rmax change rate was 1.66 ± 0.75; excluding one patient, there was significant FRL Rmax increase (p = 0.022). Although both increased significantly, no correlation between the volume change rate and the Rmax change rate was observed. No correlation was observed between the FRL volume rate and the Rmax rate.

  10. Biomimetic coprecipitation of calcium phosphate and bovine serum albumin on titanium alloy

    NARCIS (Netherlands)

    Liu, Yuelian; Layrolle, Pierre; de Bruijn, Joost Dick; van Blitterswijk, Clemens; de Groot, K.

    2001-01-01

    Titanium alloy implants were precoated biomimetically with a thin and dense layer of calcium phosphate and then incubated either in a supersaturated solution of calcium phosphate or in phosphate-buffered saline, each containing bovine serum albumin (BSA) at various concentrations, under

  11. Neutralization of X4- and R5-tropic HIV-1 NL4-3 variants by HOCl-modified serum albumins

    Directory of Open Access Journals (Sweden)

    Schwalbe Birco

    2010-06-01

    Full Text Available Abstract Background Myeloperoxidase (MPO, an important element of the microbicidal activity of neutrophils, generates hypochlorous acid (HOCl from H2O2 and chloride, which is released into body fluids. Besides its direct microbicidal activity, HOCl can react with amino acid residues and HOCl-modified proteins can be detected in vivo. Findings This report is based on binding studies of HOCl-modified serum albumins to HIV-1 gp120 and three different neutralization assays using infectious virus. The binding studies were carried out by surface plasmon resonance spectroscopy and by standard ELISA techniques. Virus neutralization assays were carried out using HIV-1 NL4-3 virus and recombinant strains with CXCR4 and CCR5 coreceptor usage. Viral infection was monitored by a standard p24 or X-gal staining assay. Our data demonstrate that HOCl-modified mouse-, bovine- and human serum albumins all bind to the HIV-1 NL4-3 gp120 (LAV glycoprotein in contrast to non-modified albumin. Binding of HOCl-modified albumin to gp120 correlated to the blockade of CD4 as well as that of V3 loop specific monoclonal antibody binding. In neutralization experiments, HOCl-modified serum albumins inhibited replication and syncytium formation of the X4- and R5-tropic NL4-3 isolates in a dose dependent manner. Conclusions Our data indicate that HOCl-modified serum albumin veils the binding site for CD4 and the V3 loop on gp120. Such masking of the viral gp120/gp41 envelope complex might be a simple but promising strategy to inactivate HIV-1 and therefore prevent infection when HOCl-modified serum albumin is applied, for example, as a topical microbicide.

  12. Trend of Changes in Serum Albumin and Its Relation with Sex, Age, and BMI Following Laparoscopic Mini-gastric Bypass Surgery in Morbid Obese Cases.

    Science.gov (United States)

    Karimi, Mehrdad; Kabir, Ali; Nejatifar, Masoumeh; Pazouki, Abdolreza

    2018-03-01

    The aim of this study is to investigate the pattern of changes in serum albumin level after mini-gastric bypass (MGB) and its association with gender, age, and body mass index (BMI) of the patients. This cohort study was conducted on 196 morbidly obese patients undergoing MGB followed for 1 year. The data on BMI, serum albumin level, demographic, anthropometric, biochemical variables and comorbidities were gathered before and after (3, 6, and 12 months) surgery. The trend of changes in BMI and serum albumin of the patients was investigated by repeated measures tests using general linear model (GLM) and generalized estimating equations (GEE) approaches. The mean age, baseline median BMI, and albumin of the patients were 41.34 ± 11.03 years, 44.54 kg/m 2 , and 4.00 g/dl, respectively. There was a chronologically significant trend of decline in BMI (P age grouping and baseline serum albumin level (P = 0.017 and 0.001, respectively). This trend had fluctuations in patients older than 40 years with baseline serum albumin level of 3.50-3.90 g/dl. For patients with any age and baseline serum albumin level of 4.00-4.90 g/dl, this trend was stable in all periods of follow-up. MGB is an effective technique to lose weight. The trend of changes in serum albumin level was affected by its baseline levels and age.

  13. Longitudinal Associations among Renal Urea Clearance-Corrected Normalized Protein Catabolic Rate, Serum Albumin, and Mortality in Patients on Hemodialysis.

    Science.gov (United States)

    Eriguchi, Rieko; Obi, Yoshitsugu; Streja, Elani; Tortorici, Amanda R; Rhee, Connie M; Soohoo, Melissa; Kim, Taehee; Kovesdy, Csaba P; Kalantar-Zadeh, Kamyar

    2017-07-07

    There are inconsistent reports on the association of dietary protein intake with serum albumin and outcomes among patients on hemodialysis. Using a new normalized protein catabolic rate (nPCR) variable accounting for residual renal urea clearance, we hypothesized that higher baseline nPCR and rise in nPCR would be associated with higher serum albumin and better survival among incident hemodialysis patients. Among 36,757 incident hemodialysis patients in a large United States dialysis organization, we examined baseline and change in renal urea clearance-corrected nPCR as a protein intake surrogate and modeled their associations with serum albumin and mortality over 5 years (1/2007-12/2011). Median nPCRs with and without accounting for renal urea clearance at baseline were 0.94 and 0.78 g/kg per day, respectively (median within-patient difference, 0.14 [interquartile range, 0.07-0.23] g/kg per day). During a median follow-up period of 1.4 years, 8481 deaths were observed. Baseline renal urea clearance-corrected nPCR was associated with higher serum albumin and lower mortality in the fully adjusted model ( P trend urea clearance-corrected nPCR during the first 6 months was also associated with attaining high serum albumin (≥3.8 g/dl) and lower mortality ( P trend urea clearance, higher levels of renal urea clearance-corrected nPCR consistently showed lower mortality risk. Among incident hemodialysis patients, higher dietary protein intake represented by nPCR and its changes over time appear to be associated with increased serum albumin levels and greater survival. nPCR may be underestimated when not accounting for renal urea clearance. Compared with the conventional nPCR, renal urea clearance-corrected nPCR may be a better marker of mortality. Copyright © 2017 by the American Society of Nephrology.

  14. Evaluation of the binding interaction between bovine serum albumin and dimethyl fumarate, an anti-inflammatory drug by multispectroscopic methods

    Science.gov (United States)

    Jattinagoudar, Laxmi; Meti, Manjunath; Nandibewoor, Sharanappa; Chimatadar, Shivamurti

    2016-03-01

    The information of the quenching reaction of bovine serum albumin with dimethyl fumarate is obtained by multi-spectroscopic methods. The number of binding sites, n and binding constants, KA were determined at different temperatures. The effect of increasing temperature on Stern-Volmer quenching constants (KD) indicates that a dynamic quenching mechanism is involved in the interaction. The analysis of thermodynamic quantities namely, ∆H° and ∆S° suggested hydrophobic forces playing a major role in the interaction between dimethyl fumarate and bovine serum albumin. The binding site of dimethyl fumarate on bovine serum albumin was determined by displacement studies, using the site probes viz., warfarin, ibuprofen and digitoxin. The determination of magnitude of the distance of approach for molecular interactions between dimethyl fumarate and bovine serum albumin is calculated according to the theory of Förster energy transfer. The CD, 3D fluorescence spectra, synchronous fluorescence measurements and FT-IR spectral results were indicative of the change in secondary structure of the protein. The influence of some of the metal ions on the binding interaction was also studied.

  15. Profile of total protein, albumin, globulin and albumin globulin ratio in bulls

    Directory of Open Access Journals (Sweden)

    Ida Zahidah Irfan

    2014-06-01

    Full Text Available Determination of serum total protein concentration and main fractions (albumin and globulin can be used as an important diagnostic tool in clinical biochemistry. Several factors can affect the concentration of total protein, albumin, globulin and albumin globulin ratio (A/G. The aim of this study is to obtain serum protein profiles, albumin, globulin and A/G ratio based on breed, age and BCS (body condition score. Blood samples from 160 bulls were collected. Blood chemistry were analyzed by photometer principle using a commercial kit. There were significant (P<0.001 breed variation on total protein, albumin, globulin and albumin globulin ratio. Significant age differences were observed on total protein and albumin concentration (P<0.001, while globulin concentration and A/G ratio were also significant (P<0.05. Amongs groups of BCS, significant difference was verified only in the albumin concentration (P<0.05. The concentration of total proteins, albumins and globulins in the serum of the bulls are higher than standard values for cattle, while A/G ratio is lower.

  16. Gender-partitioned patient medians of serum albumin requested by general practitioners for the assessment of analytical stability.

    Science.gov (United States)

    Hansen, Steen Ingemann; Petersen, Per Hyltoft; Lund, Flemming; Fraser, Callum G; Sölétormos, György

    2018-04-25

    Recently, the use of separate gender-partitioned patient medians of serum sodium has revealed potential for monitoring analytical stability within the optimum analytical performance specifications for laboratory medicine. The serum albumin concentration depends on whether a patient is sitting or recumbent during phlebotomy. We therefore investigated only examinations requested by general practitioners (GPs) to provide data from sitting patients. Weekly and monthly patient medians of serum albumin requested by GP for both male and female patients were calculated from the raw data obtained from three analysers in the hospital laboratory on examination of samples from those >18 years. The half-range of medians were applied as an estimate of the maximum bias. Further, the ratios between the two medians were calculated (females/males). The medians for male and female patients were closely related despite considerable variation due to the current analytical variation. This relationship was confirmed by the calculated half-range for the monthly ratio between the genders of 0.44%, which surpasses the optimum analytical performance specification for bias of serum albumin (0.72%). The weekly ratio had a half-range of 1.83%, which surpasses the minimum analytical performance specifications of 2.15%. Monthly gender-partitioned patient medians of serum albumin are useful for monitoring of long-term analytical stability, where the gender medians are two independent estimates of changes in (delta) bias: only results requested by GP are of value in this application to ensure that all patients are sitting during phlebotomy.

  17. Kinetics of the Adsorption of Bovine Serum Albumin of White Wine ...

    African Journals Online (AJOL)

    This study investigates the kinetics of adsorption of bovine serum albumin, BSA, in white wine model solutions onto activated carbon, AC, and alumina, AL. Pseudo-first order and pseudo-second order models were applied to determine the rate and mechanism of adsorption of the white wine protein during the haze removal ...

  18. Preparation of Tc-99m human serum albumin using stannous citrate and stannous chloride

    International Nuclear Information System (INIS)

    El-Asrag, H.A.; El-Wetery, A.S.; El-Mohty, A.A.

    1988-01-01

    99mTc-albumin is widely used as radioactive indicator in the measurement of cardiac output by external counting techniques and in blood volume studies. The quality of 99mTc-albumin depends on the method of preparation. A comparative study had been carried out on the 99mTc-albumin preparation by the stannous chloride, stannous tartarate and stannous citrate method. The different parameters investigated for each method include: pH, albumin concentration, reductant concentration and ascorbic acid as antioxidant stabilizer. The biological distribution of 99mTc-albumin, prepared by different methods, were determined in mice and rats. A procedure was developed for the preparation of stannous human serum albumin (HSA) kit for human application the kit provides a freeze dried sterile formulation for reconstitution with sterile 99mTc pertechnetate solution to give 99mTc-Hsa, the effect of irradiation sterilization on the freeze dried kit was studied by spectrophotometric determination and biological distribution in mice and rats

  19. Interactions of nanobubbles with bovine serum albumin and papain films on gold surfaces.

    Science.gov (United States)

    Kolivoska, Viliam; Gál, Miroslav; Hromadová, Magdaléna; Lachmanová, Stepánka; Pospísil, Lubomír

    2011-12-01

    Nanobubbles formed on monocrystalline gold/water interface by means of the ethanol-to-water solvent exchange were exposed to the solutions of either bovine serum albumin or papain proteins. Both proteins do not change the position of nanobubbles in water, as observed by in situ tapping mode atomic force microscopy imaging before and after the introduction of the protein. The aqueous environment was subsequently replaced by ethanol. While all nanobubbles were found to dissolve in ethanol in the presence of bovine serum albumin, most of them survived when papain was employed. The protective ability of papain was ascribed to its resistance towards the protein denaturation in aqueous solutions of ethanol. The authors employed in situ atomic force nanolithography to investigate the nanomorphology of the papain/nanobubble assemblies in ethanol.

  20. Comparisons among serum, egg albumin and yolk concentrations of corticosterone as biomarkers of basal and stimulated adrenocortical activity of laying hens.

    Science.gov (United States)

    Cook, N J; Renema, R; Wilkinson, C; Schaefer, A L

    2009-09-01

    1. Serial blood samples from individual birds were analysed for corticosterone concentrations under basal and stimulated conditions, and matched to eggs from the same birds for comparison to albumin and yolk concentrations of corticosterone. 2. Serum corticosterone exhibited increases in response to stimulation by ACTH and Handling stress. There were no significant increases in egg albumin or yolk concentrations of corticosterone following stimulation. 3. Several significant correlations were observed between the mean and area under the curve (AUC) measurements of serum corticosterone concentrations with albumin and yolk corticosterone concentrations in eggs laid from 1 to 2 d later. 4. The results demonstrated a relationship between endogenous concentrations of serum corticosterone that reflected daily adrenocortical output with albumin and yolk corticosterone concentrations in eggs laid the following day. 5. The results do not support the concept of albumin and yolk concentrations of corticosterone as biomarkers of acute adrenocortical responses to stimulation.

  1. A study on human serum albumin influence on glycation of fibrinogen

    International Nuclear Information System (INIS)

    Kielmas, Martyna; Szewczuk, Zbigniew; Stefanowicz, Piotr

    2013-01-01

    Highlights: •The glycation of fibrinogen was investigated by isotopic labeling method. •The potential glycation sites in fibrinogen were identified. •Human serum albumin (HSA) inhibits the glycation of fibrinogen. •The effect of HSA on fibrinogen glycation is sequence-dependent. -- Abstract: Although in vivo glycation proceeds in complex mixture of proteins, previous studies did not take in consideration the influence of protein–protein interaction on Maillard reaction. The aim of our study was to test the influence of human serum albumin (HSA) on glycation of fibrinogen. The isotopic labeling using [ 13 C 6 ] glucose combined with LC-MS were applied as tool for identification possible glycation sites in fibrinogen and for evaluation the effect of HSA on the glycation level of selected amino acids in fibrinogen. The obtained data indicate that the addition of HSA protects the fibrinogen from glycation. The level of glycation in presence of HSA is reduced by 30–60% and depends on the location of glycated residue in sequence of protein

  2. A study on human serum albumin influence on glycation of fibrinogen

    Energy Technology Data Exchange (ETDEWEB)

    Kielmas, Martyna; Szewczuk, Zbigniew; Stefanowicz, Piotr, E-mail: Piotr.stefanowicz@chem.uni.wroc.pl

    2013-09-13

    Highlights: •The glycation of fibrinogen was investigated by isotopic labeling method. •The potential glycation sites in fibrinogen were identified. •Human serum albumin (HSA) inhibits the glycation of fibrinogen. •The effect of HSA on fibrinogen glycation is sequence-dependent. -- Abstract: Although in vivo glycation proceeds in complex mixture of proteins, previous studies did not take in consideration the influence of protein–protein interaction on Maillard reaction. The aim of our study was to test the influence of human serum albumin (HSA) on glycation of fibrinogen. The isotopic labeling using [{sup 13}C{sub 6}] glucose combined with LC-MS were applied as tool for identification possible glycation sites in fibrinogen and for evaluation the effect of HSA on the glycation level of selected amino acids in fibrinogen. The obtained data indicate that the addition of HSA protects the fibrinogen from glycation. The level of glycation in presence of HSA is reduced by 30–60% and depends on the location of glycated residue in sequence of protein.

  3. [Changes in the secondary and tertiary structure of serum albumin in interactions with ligands of various structures].

    Science.gov (United States)

    Trinus, F P; Braver-Chernobul'skaia, B S; Luĭk, A I; Boldeskul, A E; Velichko, A N

    1984-01-01

    High affinity interactions between blood serum albumin and five substances of various chemical structure, exhibiting distinct physiological activity, were accompanied by alterations in the protein tertiary structure, while the albumin secondary structure was involved in conformational transformation after less effective affinity binding.

  4. Capping of Silybin with β-Cyclodextrin Influences its Binding with Bovine Serum Albumin: A Study by Fluorescence Spectroscopy and Molecular Modeling

    Energy Technology Data Exchange (ETDEWEB)

    Natesan, Sudha; Sowrirajan, Chandrasekaran; Dhanaraj, Premnath; Enoch, Israel V. M. V. [Karunya Univ., Tamil Nadu (India)

    2014-07-15

    The association of silybin with β-cyclodextrin and its influence on silybin's binding with bovine serum albumin are reported. The stoichiometry, binding constant, and the structure of silybin-β-cyclodextrin inclusion complex are reported. The titrations of silybin with bovine serum albumin in the absence and presence of β-cyclodextrin are carried out and the differences in binding strengths are discussed. Molecular modeling is used to optimize the sites and mode of binding of silybin with bovine serum albumin. Forster resonance energy transfer is calculated and the proximity of interacting molecules is reported in the presence and absence of β-cyclodextrin.

  5. Capping of Silybin with β-Cyclodextrin Influences its Binding with Bovine Serum Albumin: A Study by Fluorescence Spectroscopy and Molecular Modeling

    International Nuclear Information System (INIS)

    Natesan, Sudha; Sowrirajan, Chandrasekaran; Dhanaraj, Premnath; Enoch, Israel V. M. V.

    2014-01-01

    The association of silybin with β-cyclodextrin and its influence on silybin's binding with bovine serum albumin are reported. The stoichiometry, binding constant, and the structure of silybin-β-cyclodextrin inclusion complex are reported. The titrations of silybin with bovine serum albumin in the absence and presence of β-cyclodextrin are carried out and the differences in binding strengths are discussed. Molecular modeling is used to optimize the sites and mode of binding of silybin with bovine serum albumin. Forster resonance energy transfer is calculated and the proximity of interacting molecules is reported in the presence and absence of β-cyclodextrin

  6. Biological Interaction of Molybdenocene Dichloride with Bovine Serum Albumin Using Fluorescence Spectroscopy

    Science.gov (United States)

    Domínguez, Moralba; Cortes-Figueroa, Jose´ E.; Meléndez, Enrique

    2018-01-01

    Bioinorganic topics are ubiquitous in the inorganic chemistry curriculum; however, experiments to enhance understanding of related topics are scarce. In this proposed laboratory, upper undergraduate students assess the biological interaction of molybdenocene dichloride (Cp2MoCl2) with bovine serum albumin (BSA) by fluorescence spectroscopy.…

  7. Evaluation of usefulness of Tc-99m-GSA liver scintigraphy in chronic liver diseases

    International Nuclear Information System (INIS)

    Fukui, Hiroyuki; Kashiwagi, Toru; Kasahara, Akinori

    1991-01-01

    Liver scintigraphy was performed using a newly developed radiopharmaceutical, Tc-99m-DTPA-galactosyl-human-serum-albumin (Tc-99m-GSA), which binds specifically to the receptors on the hepatic cell surface, in 15 patients with chronic liver disease. The scintigraphy was evaluated qualitatively and quantitatively, and the results were compared with those obtained from the Tc-99m-PMT or Tc-99m-sn-phytate scintigraphy, and the liver function tests. The Tc-99m-GSA scintigraphy showed clear liver images in chronic hepatitis. However, in liver cirrhosis, the liver images were not clear and the cardiac images still existed 40 minutes after administration of Tc-99m-GSA, suggesting that the image quality of the Tc-99m-GSA scintigrams may be inferior to that of Tc-99m-sn-phytate or Tc-99m-PMT in some cases of severe liver dysfunction. The time-activity curves of the heart and liver were analyzed by non-linear regression analysis. The clearance rate from plasma (Kd) were obtained from the time-activity curve of the heart, and the hepatic uptake rate (Ku), hepatic excretion rate (Ke) and peak time of hepatic uptake-excretion curve (PT) were obtained from the time-activity curve of the liver. Kd, Ku, and PT values were more significantly decreased or prolonged in the patients with chronic hepatitis. Kd, Ku, and PT values had positive correlations with the result of the serum liver function tests, ICG-R15 and ICG-K. Ku and PT values had also correlations with the histological degree of hepatic fibrosis. On the other hand, the indices obtained using Tc-99m-PMT or Tc-99m-sn-phytate did not have correlations with the histological degrees of hepatic fibrosis. It is concluded that the liver scintigraphy using Tc-99m-GSA may be useful and give different information from those with conventional liver scintigraphies in evaluating chronic liver diseases. (author)

  8. Ionization of tyrosine residues in human serum albumin and in its complexes with bilirubin and laurate

    DEFF Research Database (Denmark)

    Honoré, B; Brodersen, R

    1992-01-01

    Spectrophotometric titration of human serum albumin indicates that ionization of the 18 tyrosine residues takes place between pH 9 and 12.7. A Hill plot indicates that protons dissociate co-operatively from tyrosine residues, in pure albumin between pH 11.0 and 11.4 with a Hill coefficient 1.7, a...

  9. Reversible covalent binding of neratinib to human serum albumin in vitro.

    Science.gov (United States)

    Chandrasekaran, Appavu; Shen, Li; Lockhead, Susan; Oganesian, Aram; Wang, Jianyao; Scatina, JoAnn

    2010-12-01

    Neratinib (HKI-272), an irreversible inhibitor of Her 2 tyrosine kinase, is currently in development as an alternative for first and second line therapy in metastatic breast cancer patients who overexpress Her 2. Following incubation of [(14)C]neratinib in control human plasma at 37°C for 6 hours, about 60% to 70% of the radioactivity was not extractable, due to covalent binding to albumin. In this study, factors that could potentially affect the covalent binding of neratinib to plasma proteins, specifically to albumin were investigated. When [(14)C]neratinib was incubated at 10 μg/mL in human serum albumin (HSA) or control human plasma, the percent binding increased with time; the highest percentages of binding (46 and 67%, respectively) were observed at 6 hours, the longest duration of incubation examined. Binding increased with increasing temperature; the highest percentages of binding to HSA or human plasma (59 and 78%) were observed at 45°C, the highest temperature tested. The binding also increased with increasing pH of incubation; the highest percentages of binding (56 and 65%) were observed at pH 8.5, the highest pH value tested. The percentages of binding were similar (53% to 57%) when a wide range of concentrations of [(14)C]neratinib (50 ng/mL to 10 μg/mL) were incubated with human plasma at 37°C for 6 hours, indicating that the binding was independent of the substrate concentration, especially in the therapeutic range (50 to 200 ng/mL). When human plasma proteins containing covalently bound [(14)C]neratinb were suspended in a 10 fold volume of phosphate buffer at pH 4.0, 6.0, 7.4, and 8.5, and further incubated at 37°C for ~ 16 hours, about 45%, 44%, 32%, and 12% of the total radioactivity, respectively, was released as unchanged [(14)C]neratinib, indicating that the binding is reversible in nature, with more released at pH 7.4 and below. In conclusion, the covalent binding of neratinib to serum albumin is pH, time and temperature dependent, but

  10. Contribution to the study of plasmatic fibrinogen and serum albumin: effects of irradiation; Contribution a l'etude du fibrinogene et de la serum-albumine plasmatiques - effets de l'irradiation

    Energy Technology Data Exchange (ETDEWEB)

    Suscillon, M. [Commissariat a l' Energie Atomique, Centre d' Etudes Nucleaires de Grenoble, 38 (France)

    1967-07-01

    The author studies the modifications of properties and structure of serum albumin and fibrinogen solution when subjected to radiation of low energy (X rays). On the other hand, two original techniques are exposed: 1. Amperometric determination of fibrin stabilizing factor or factor XIII of hemostasis. 2. Spectrophotometric study of fibrin formation kinetics. Then showing off and quantitative determination of platelets fibrinogen is exposed. (author) [French] L'auteur etudie les modifications des proprietes et de la structure des molecules de serum-albumine et de fibrinogene en solution soumise a un flux de RX de basse energie. D'autre part deux techniques originales sont exposees : 1. Dosage amperometrique du facteur stabilisant de la fibrine. 2. Etude spectrophotometrique de la cinetique de la fibro-formation. Enfin une mise en evidence et un dosage du fibrinogene plaquettaire sont presentes. (auteur)

  11. Peculiarities of the introduction of technetium isotopes into protein molecules - of human serum albumin as an example

    International Nuclear Information System (INIS)

    Stanko, V.I.; Ovsyannikov, N.N.; Zuykova, N.P.; Gouskov, A.F.; Kovalchouk, N.D.

    1978-07-01

    Pecularities of the introduction of the radioisotope technetium 99m into the molecules of human serum albumin have been investigated. Tin not only participates in the Tc(V11) reduction process, but is incorporated into the originating Tc albumin complex. It is shown that no more than four technetium atoms enter into bond with an albumin molecule. The authors express their opinion that in order to produce high-quality protein preparations, the albumin has to be modified through a polyfunctional complexing agent which forms an entirely saturated coordination complex with Tc(IV)

  12. Pecularities of the introduction of technetium isotopes into protein molecules using human serum albumin as an example

    International Nuclear Information System (INIS)

    Stanko, V.I.; Ovsyannikov, N.N.; Sujkova, N.P.; Gus'kov, A.F.; Koval'chuk, N.D.

    1978-01-01

    Pecularities of the introduction of the radioisotope technetium 99m into the molecules of human serum albumin have been investigated. Tin not only participates in the Tc(VII) reduction process, but is incorporated into the originating Tc albumin complex. It is shown that no more than four technetium atoms enter into bond with an albumin molecule. The authors express their opinion that in order to produce high-quality protein preparations, the albumin has to be modified through a polyfunctional complexing agent which forms an entirely saturated coordination complex with Tc(IV). (author)

  13. Interaction of silicon nanoparticles with the molecules of bovine serum albumin in aqueous solutions

    International Nuclear Information System (INIS)

    Anenkova, K A; Sergeeva, I A; Petrova, G P; Fedorova, K V; Osminkina, L A; Timoshenko, Viktor Yu

    2011-01-01

    Using the method of photon-correlation spectroscopy, the coefficient of translational diffusion D t and the hydrodynamic radius R of the particles in aqueous solutions of the bovine serum albumin, containing silicon nanoparticles, are determined. The character of the dependence of these parameters on the concentration of the protein indicates the absence of interaction between the studied particles in the chosen range of albumin concentrations 0.2 - 1.0 mg mL -1 . (optical technologies in biophysics and medicine)

  14. Unveiling the stimulatory effects of tartrazine on human and bovine serum albumin fibrillogenesis: Spectroscopic and microscopic study

    Science.gov (United States)

    Al-Shabib, Nasser Abdulatif; Khan, Javed Masood; Alsenaidy, Mohammad A.; Alsenaidy, Abdulrahman M.; Khan, Mohd Shahnawaz; Husain, Fohad Mabood; Khan, Mohammad Rashid; Naseem, Mohammad; Sen, Priyankar; Alam, Parvez; Khan, Rizwan Hasan

    2018-02-01

    Amyloid fibrils are playing key role in the pathogenesis of various neurodegenerative diseases. Generally anionic molecules are known to induce amyloid fibril in several proteins. In this work, we have studied the effect of anionic food additive dye i.e., tartrazine (TZ) on the amyloid fibril formation of human serum albumins (HSA) and bovine serum albumin (BSA) at pHs 7.4 and 3.5. We have employed various biophysical methods like, turbidity measurements, Rayleigh Light Scattering (RLS), Dynamic Light Scattering (DLS), intrinsic fluorescence, Congo red assay, far-UV CD, transmission electron microscopy (TEM) and atomic force microscopy (AFM) to decipher the mechanism of TZ-induce amyloid fibril formation in both the serum albumins at pHs 7.4 and 3.5. The obtained results suggest that both the albumins forms amyloid-like aggregates in the presence of 1.0 to 15.0 mM of TZ at pH 3.5, but no amyloid fibril were seen at pH 7.4. The possible cause of TZ-induced amyloid fibril formation is electrostatic and hydrophobic interaction because sulfate group of TZ may have interacted electrostatically with positively charged amino acids of the albumins at pH 3.5 and increased protein-protein and protein-TZ interactions leading to amyloid fibril formation. The TEM, RLS and DLS results are suggesting that BSA forms bigger size amyloids compared to HSA, may be due to high surface hydrophobicity of BSA.

  15. Immobilization of Bovine Serum Albumin Upon Multiwall Carbon Nanotube for High Speed Humidity Sensing Application.

    Science.gov (United States)

    Bhattacharya, Sankhya; Sasmal, Milan

    2016-01-01

    We present a high-speed humidity sensor based on immobilization of bovine serum albumin upon multiwall carbon nanotube (IBC). A simple and versatile drop casting technique was employed to make the humidity sensor using novel material IBC at room temperature. IBC was synthesized using easy solution process technique. The working principle of the IBC humidity sensor depends upon the variation of output current or conductance with the exposure of different humidity level. Humidity sensing properties of our device is explained on the basis of charge transfer from water molecules to IBC and bovine serum albumin to multiwall carbon nanotube (MWCNT). Our sensor exhibits faster response time around 1.2 s and recovery time 1.5 s respectively.

  16. Clinical significance of changes of serum APN, plasma VEGF, Hcy and urine albumin levels in patients with DM2 nephrosis

    International Nuclear Information System (INIS)

    Zhang Yuejin; Zhang Xinfang; Hu Ying

    2011-01-01

    Objective: Explore type 2 diabetes mellitus (DM2) and complicating with kidney disease patients homocysteine (Hcy), adiponectin (APN), vascular endothelial growth factor (VEGF) and urine albumin change relations. Methods: A normal controls and no complications of diabetes groups, combined with nephropathy. A comparison were measured of serum APN, plasma VEGF, Hcy and urine albumin level among. Results: Two groups of patients with diabetes fasting blood glucose level were no significant difference. Also there is no difference of BUN and Cr in three groups urine albumin in diabetic-nephropathy albumin increased significantly (P<0.01), than without complications group. Three groups of Hcy concentrations were significantly higher than that of normal control group (P<0.01), serum APN, plasma VEGF level obviously lower than normal control group, which increased in patients with nephropathy increased or reduced more apparently no complications group also have obvious difference (P<0.01). Conclusion: In patients with diabetes in two groups, plasma Hcy and urine albumin were significantly higher APN, and VEGF decreased significantly. In patients with nephropathy manifested more apparently, but renal damage did not enter decompensated period, clinically necessary for people with diabetes testing serum APN, plasma VEGF, Hcy and urine Albumin level, promptly intervention to prevent or relieve the further development of diabetes. (authors)

  17. Serum albumin and muscle strength: a longitudinal study in older men and women

    NARCIS (Netherlands)

    Schalk, B.W.M.; Penninx, B.W.J.H.; Bouter, L.M.; Deeg, D.J.H.; Visser, M.

    2005-01-01

    OBJECTIVES: To examine whether low serum albumin is associated with low muscle strength and future decline in muscle strength in community-dwelling older men and women. DESIGN: Population-based cohort study. SETTING: The Longitudinal Aging Study Amsterdam. PARTICIPANTS: Six hundred seventy-six women

  18. Condition of the centers of linkage of serum albumin in cancer gynecological patients at beam therapy

    International Nuclear Information System (INIS)

    Malenchenko, A.F.; Belyakovskij, V.N.; Lukovskaya, N.D.; Prigozhaya, T.I.; Stasenkova, S.V.

    2009-01-01

    With the use of the method of fluorescent probes the condition of the centers of linkage of serum albumin in healthy women and in the cancer patients, passing a course of beam therapy, is analyzed at different modes. It is shown that general concentration of albumin in healthy persons and cancer patients are in the limits of normal values, however parameters of effective concentration of albumin, reserve of albumin linkage and toxicity index of patients statistically, for certain, differ in comparison with those in the control group. Carrying out the beam therapy course both split and not split promotes an increase of values of toxicity index. (authors)

  19. Clinical significance of preoperative serum albumin level for prognosis in surgically resected patients with non-small cell lung cancer: Comparative study of normal lung, emphysema, and pulmonary fibrosis.

    Science.gov (United States)

    Miura, Kentaro; Hamanaka, Kazutoshi; Koizumi, Tomonobu; Kitaguchi, Yoshiaki; Terada, Yukihiro; Nakamura, Daisuke; Kumeda, Hirotaka; Agatsuma, Hiroyuki; Hyogotani, Akira; Kawakami, Satoshi; Yoshizawa, Akihiko; Asaka, Shiho; Ito, Ken-Ichi

    2017-09-01

    This study was performed to clarify whether preoperative serum albumin level is related to the prognosis of non-small cell lung cancer patients undergoing surgical resection, and the relationships between serum albumin level and clinicopathological characteristics of lung cancer patients with emphysema or pulmonary fibrosis. We retrospectively evaluated 556 patients that underwent surgical resection for non-small cell lung cancer. The correlation between preoperative serum albumin level and survival was evaluated. Patients were divided into three groups according to the findings on chest high-resolution computed tomography (normal lung, emphysema, and pulmonary fibrosis), and the relationships between serum albumin level and clinicopathological characteristics, including prognosis, were evaluated. The cut-off value of serum albumin level was set at 4.2g/dL. Patients with low albumin levels (albumin emphysema group (n=48) and pulmonary fibrosis group (n=45) were significantly lower than that in the normal lung group (n=463) (p=0.009 and pulmonary fibrosis groups, but not in the emphysema group. Preoperative serum albumin level was an important prognostic factor for overall survival and recurrence-free survival in patients with resected non-small cell lung cancer. Divided into normal lung, emphysema, and pulmonary fibrosis groups, serum albumin level showed no influence only in patients in the emphysema group. Copyright © 2017 Elsevier B.V. All rights reserved.

  20. Locations of the three primary binding sites for long-chain fatty acids on bovine serum albumin

    International Nuclear Information System (INIS)

    Hamilton, J.A.; Era, S.; Bhamidipati, S.P.; Reed, R.G.

    1991-01-01

    Binding of 13 C-enriched oleic acid to bovine serum albumin and to three large proteolytic fragments of albumin - two complementary fragments corresponding to the two halved of albumin and one fragment corresponding to the carboxyl-terminal domain - yielded unique patterns of NMR resonances (chemical shifts and relative intensities) that were used to identify the locations of binding of the first 5 mol of oleic acid to the multidomain albumin molecule. The first 3 mol of oleic acid added to intact albumin generated three distinct NMR resonances as a result of simultaneous binding of oleic acid to three heterogeneous sites (primary sites). This distribution suggests albumin to be a less symmetrical binding molecule than theoretical models predict. This work also demonstrates the power of NMR for the study of microenvironments of individual fatty acid binding sites in specific domain

  1. Photodynamically generated bovine serum albumin radicals

    DEFF Research Database (Denmark)

    Silvester, J A; Timmins, G S; Davies, Michael Jonathan

    1998-01-01

    Porphyrin-sensitized photoxidation of bovine serum albumin (BSA) results in oxidation of the protein at (at least) two different, specific sites: the Cys-34 residue giving rise to a thiyl radical (RS.); and one or both of the tryptophan residues (Trp-134 and Trp-214) resulting in the formation...... of tertiary carbon-centred radicals and disruption of the tryptophan ring system. In the case of porphyrins such as hematoporphyrin, which bind at specific sites on BSA, these species appear to arise via long-range transfer of damage within the protein structure, as the binding site is some distance from...... the ultimate site of radical formation. This transfer of damage is shown to depend on a number of factors including the conformation of the protein, the presence of blocking groups and pH. Alteration of the protein conformation results in radical formation at additional (or alternative) sites, as does blocking...

  2. Fluorescence resonance energy transfer: A promising tool for investigation of the interaction between 1-anthracene sulphonate and serum albumins

    International Nuclear Information System (INIS)

    Banerjee, Paltu; Ghosh, Saptaparni; Sarkar, Arindam; Bhattacharya, Subhash Chandra

    2011-01-01

    This present investigation has revealed that steady state as well as time-resolved fluorescence techniques can serve as highly sensitive monitors for exploring the interaction of fluorescent probe 1-anthracene sulphonate (1-AS) with model transport proteins, bovine serum albumin (BSA) and human serum albumin (HSA).We have focused on fluorescence resonance energy transfer (FRET) between excited tryptophan in transport proteins to 1-AS, for the study of relaxation dynamics of biological molecules.

  3. Interaction of glucocorticoids and progesterone derivatives with human serum albumin.

    Science.gov (United States)

    Abboud, Rola; Akil, Mohammad; Charcosset, Catherine; Greige-Gerges, Hélène

    2017-10-01

    Glucocorticoids (GCs) and progesterone derivatives (PGDs) are steroid hormones with well-known biological activities. Their interaction with human serum albumin (HSA) may control their distribution. Their binding to albumin is poorly studied in literature. This paper deals with the interaction of a series of GCs (cortisol, cortisone, prednisolone, prednisone, 6-methylprednisolone and 9-fluorocortisol acetate) and PGDs (progesterone, hydroxylated PGDs, methylated PGDs and dydrogesterone) with HSA solution (pH 7.4) at molar ratios steroid to HSA varying from 0 to 10. Similar titrations were conducted using Trp aqueous solution. Fluorescence titration method and Fourier transform infrared spectroscopy (FTIR) are used. PGDs (except dydrogesterone), cortisone and 9-fluorocortisol acetate affected weakly the fluorescence of Trp in buffer solution while they decreased in a dose-dependent manner that of HSA. Their binding constants to HSA were then calculated. Moreover, displacement experiment was performed using bilirubin as a site marker. The binding constant of bilirubin to albumin was determined in the absence and presence of a steroid at a molar ratio steroid to HSA of 1. The results indicate that the steroids bind to HSA at site I in a pocket different from that of bilirubin. Furthermore, the peak positions of amide I and amide II bands of HSA were shifted in the presence of progesterone, dydrogesterone and GCs. Also a variation was observed in amide I region indicating the formation of hydrogen bonding between albumin and steroids. Copyright © 2017 Elsevier B.V. All rights reserved.

  4. Crystal structure of equine serum albumin in complex with cetirizine reveals a novel drug binding site.

    Science.gov (United States)

    Handing, Katarzyna B; Shabalin, Ivan G; Szlachta, Karol; Majorek, Karolina A; Minor, Wladek

    2016-03-01

    Serum albumin (SA) is the main transporter of drugs in mammalian blood plasma. Here, we report the first crystal structure of equine serum albumin (ESA) in complex with antihistamine drug cetirizine at a resolution of 2.1Å. Cetirizine is bound in two sites--a novel drug binding site (CBS1) and the fatty acid binding site 6 (CBS2). Both sites differ from those that have been proposed in multiple reports based on equilibrium dialysis and fluorescence studies for mammalian albumins as cetirizine binding sites. We show that the residues forming the binding pockets in ESA are highly conserved in human serum albumin (HSA), and suggest that binding of cetirizine to HSA will be similar. In support of that hypothesis, we show that the dissociation constants for cetirizine binding to CBS2 in ESA and HSA are identical using tryptophan fluorescence quenching. Presence of lysine and arginine residues that have been previously reported to undergo nonenzymatic glycosylation in CBS1 and CBS2 suggests that cetirizine transport in patients with diabetes could be altered. A review of all available SA structures from the PDB shows that in addition to the novel drug binding site we present here (CBS1), there are two pockets on SA capable of binding drugs that do not overlap with fatty acid binding sites and have not been discussed in published reviews. Copyright © 2016 Elsevier Ltd. All rights reserved.

  5. Relationship between trajectories of serum albumin levels and technique failure according to diabetic status in peritoneal dialysis patients: A joint modeling approach

    Directory of Open Access Journals (Sweden)

    Mehri Khoshhali

    2017-06-01

    Full Text Available Background: In peritoneal dialysis, technique failure is an important metric to be considered. This study was performed in order to identify the relationship between trajectories of serum albumin levels and peritoneal dialysis technique failure on end-stage renal disease patients according to diabetic status. Furthermore, this study was performed to reveal predictors of serum albumin and technique failure simultaneously. Methods: This retrospective cohort study included 300 (189 non-diabetic and 111 diabetic end-stage renal disease patients on continuous ambulatory peritoneal dialysis treated in Al-Zahra Hospital, Isfahan, Iran, from May 2005 to March 2015. Bayesian joint modeling was carried out in order to determine the relationship between trajectories of serum albumin levels and peritoneal dialysis technique failure in the patients according to diabetic status. Death from all causes was considered as a competing risk. Results: Using joint modeling approach, a relationship between trajectories of serum albumin with hazard of transfer to hemodialysis was estimated as −0.720 (95% confidence interval [CI], −0.971 to −0.472 for diabetic and −0.784 (95% CI, −0.963 to −0.587 for non-diabetic patients. From our findings it was showed that predictors of low serum albumin over time were time on peritoneal dialysis for diabetic patients and increase in age and time on peritoneal dialysis, history of previous hemodialysis, and lower body mass index in non-diabetic patients. Conclusion: The results of current study showed that controlling serum albumin over time in non-diabetic and diabetic patients undergoing continuous ambulatory peritoneal dialysis treatment can decrease risk of adverse outcomes during the peritoneal dialysis period.

  6. Fab-dsFv: A bispecific antibody format with extended serum half-life through albumin binding.

    Science.gov (United States)

    Davé, Emma; Adams, Ralph; Zaccheo, Oliver; Carrington, Bruce; Compson, Joanne E; Dugdale, Sarah; Airey, Michael; Malcolm, Sarah; Hailu, Hanna; Wild, Gavin; Turner, Alison; Heads, James; Sarkar, Kaushik; Ventom, Andrew; Marshall, Diane; Jairaj, Mark; Kopotsha, Tim; Christodoulou, Louis; Zamacona, Miren; Lawson, Alastair D; Heywood, Sam; Humphreys, David P

    2016-10-01

    An antibody format, termed Fab-dsFv, has been designed for clinical indications that require monovalent target binding in the absence of direct Fc receptor (FcR) binding while retaining substantial serum presence. The variable fragment (Fv) domain of a humanized albumin-binding antibody was fused to the C-termini of Fab constant domains, such that the VL and VH domains were individually connected to the Cκ and CH1 domains by peptide linkers, respectively. The anti-albumin Fv was selected for properties thought to be desirable to ensure a durable serum half-life mediated via FcRn. The Fv domain was further stabilized by an inter-domain disulfide bond. The bispecific format was shown to be thermodynamically and biophysically stable, and retained good affinity and efficacy to both antigens simultaneously. In in vivo studies, the serum half-life of Fab-dsFv, 2.6 d in mice and 7.9 d in cynomolgus monkeys, was equivalent to Fab'-PEG.

  7. Palmitate and stearate binding to human serum albumin. Determination of relative binding constants

    DEFF Research Database (Denmark)

    Vorum, H; Fisker, K; Honoré, B

    1997-01-01

    Multiple binding equilibria of two apparently insoluble ligands, palmitate and stearate, to defatted human serum albumin were studied in a 66 mM sodium phosphate buffer (pH 7.4) at 37 degrees C, by determination of dialytic exchange rates of ligands among identical equilibrium solutions. The expe...

  8. The fluorescence spectroscopic studies on the interaction of novel aminophosphinic acids with bovine serum albumin

    Energy Technology Data Exchange (ETDEWEB)

    Kaboudin, B., E-mail: kaboudin@iasbs.ac.ir [Department of Chemistry, Institute for Advanced Studies in Basic Sciences (IASBS), Gava Zang, Zanjan 45137-66731 (Iran, Islamic Republic of); Moradi, K.; Faghihi, M.R.; Mohammadi, F. [Department of Chemistry, Institute for Advanced Studies in Basic Sciences (IASBS), Gava Zang, Zanjan 45137-66731 (Iran, Islamic Republic of)

    2013-07-15

    Six novel aminomethylphosphinic acids have been synthesized and characterized. The interaction between the aminophosphinic acids and bovine serum albumin (BSA) was investigated using fluorescence spectroscopy. The experimental results showed that the fluorescence quenching of BSA by aminophosphinic acids is a result of the formation of aminophosphinic acid–BSA complex; static quenching and non-radiative energy transferring were confirmed to result in the fluorescence quenching. The number of binding sites n, the apparent binding constant K{sub A} and the corresponding thermodynamic parameters were calculated at different temperatures. The process of binding of the aminophosphinic acid molecules to BSA was a spontaneous molecular interaction procedure in which entropy increased and Gibbs free energy decreased. Hydrophobic interaction force plays a major role in stabilizing the complex. The effect of aminophosphinic acids on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy. -- Graphical abstarct: The binding interactions of the water-soluble aminoalkylphosphinic acids APA 1–6 to bovine serum albumin (BSA) showed that the interaction process was spontaneous and the major interaction forces were found to be hydrophobic. Highlights: ► Binding of novel aminophosphinic acids with bovine serum albumin. ► Hydrophobic and hydrogen bonding attraction play major role in the binding process. ► Binding did not cause conformational changes in the protein. ► The quenching mechanism of fluorescence of BSA by aminophosphinic acids is a static quenching process.

  9. The fluorescence spectroscopic studies on the interaction of novel aminophosphinic acids with bovine serum albumin

    International Nuclear Information System (INIS)

    Kaboudin, B.; Moradi, K.; Faghihi, M.R.; Mohammadi, F.

    2013-01-01

    Six novel aminomethylphosphinic acids have been synthesized and characterized. The interaction between the aminophosphinic acids and bovine serum albumin (BSA) was investigated using fluorescence spectroscopy. The experimental results showed that the fluorescence quenching of BSA by aminophosphinic acids is a result of the formation of aminophosphinic acid–BSA complex; static quenching and non-radiative energy transferring were confirmed to result in the fluorescence quenching. The number of binding sites n, the apparent binding constant K A and the corresponding thermodynamic parameters were calculated at different temperatures. The process of binding of the aminophosphinic acid molecules to BSA was a spontaneous molecular interaction procedure in which entropy increased and Gibbs free energy decreased. Hydrophobic interaction force plays a major role in stabilizing the complex. The effect of aminophosphinic acids on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy. -- Graphical abstarct: The binding interactions of the water-soluble aminoalkylphosphinic acids APA 1–6 to bovine serum albumin (BSA) showed that the interaction process was spontaneous and the major interaction forces were found to be hydrophobic. Highlights: ► Binding of novel aminophosphinic acids with bovine serum albumin. ► Hydrophobic and hydrogen bonding attraction play major role in the binding process. ► Binding did not cause conformational changes in the protein. ► The quenching mechanism of fluorescence of BSA by aminophosphinic acids is a static quenching process

  10. Density and radioactivity distribution of respirable range human serum albumin aerosol

    International Nuclear Information System (INIS)

    Raghunath, B.; Somasundaram, S.; Soni, P.S.

    1988-01-01

    Dry human serum albumin (HSA) aerosol in the respirable size range was generated using the BARC nebulizer. The aerosol was sampled using Lovelace Aerosol Particle Separator (LAPS) and the density of HSA was determined. Labelling of HSA with 99m TcO 4 - was done, both in HSA solution and with dry denatured HSA particles, to study the distribution of radioactivity in both cases. The results are discussed. (author)

  11. Biomolecular Interaction Study of Cyclolinopeptide A with Human Serum Albumin

    Directory of Open Access Journals (Sweden)

    Ben Rempel

    2010-01-01

    Full Text Available The kinetics, energetics, and structure of Cyclolinopeptide A binding with Human Serum Albumin were investigated with surface plasmon resonance and circular dichroism. The complex is formed through slow recognition kinetics that is temperature sensitive in the range of 20°C–37°C. The overall reaction was observed to be endothermic (ΔH=204 kJ mol−1 and entropy driven (ΔS=746 J mol−1K−1 with overall small changes to the tertiary structure.

  12. Nitric oxide circulates in mammalian plasma primarily as an S-nitroso adduct of serum albumin.

    Science.gov (United States)

    Stamler, J S; Jaraki, O; Osborne, J; Simon, D I; Keaney, J; Vita, J; Singel, D; Valeri, C R; Loscalzo, J

    1992-01-01

    We have recently shown that nitric oxide or authentic endothelium-derived relaxing factor generated in a biologic system reacts in the presence of specific protein thiols to form S-nitrosoprotein derivatives that have endothelium-derived relaxing factor-like properties. The single free cysteine of serum albumin, Cys-34, is particularly reactive toward nitrogen oxides (most likely nitrosonium ion) under physiologic conditions, primarily because of its anomalously low pK; given its abundance in plasma, where it accounts for approximately 0.5 mM thiol, we hypothesized that this plasma protein serves as a reservoir for nitric oxide produced by the endothelial cell. To test this hypothesis, we developed a methodology, which involves UV photolytic cleavage of the S--NO bond before reaction with ozone for chemiluminescence detection, with which to measure free nitric oxide, S-nitrosothiols, and S-nitrosoproteins in biologic systems. We found that human plasma contains approximately 7 microM S-nitrosothiols, of which 96% are S-nitrosoproteins, 82% of which is accounted for by S-nitroso-serum albumin. By contrast, plasma levels of free nitric oxide are only in the 3-nM range. In rabbits, plasma S-nitrosothiols are present at approximately 1 microM; 60 min after administration of NG-monomethyl-L-arginine at 50 mg/ml, a selective and potent inhibitor of nitric oxide synthetases, S-nitrosothiols decreased by approximately 40% (greater than 95% of which were accounted for by S-nitrosoproteins, and approximately 80% of which was S-nitroso-serum albumin); this decrease was accompanied by a concomitant increase in mean arterial blood pressure of 22%. These data suggest that naturally produced nitric oxide circulates in plasma primarily complexed in S-nitrosothiol species, principal among which is S-nitroso-serum albumin. This abundant, relatively long-lived adduct likely serves as a reservoir with which plasma levels of highly reactive, short-lived free nitric oxide can be

  13. Photoexcited riboflavin induces oxidative damage to human serum albumin

    Science.gov (United States)

    Hirakawa, Kazutaka; Yoshioka, Takuto

    2015-08-01

    Photoexcited riboflavin induced damage of human serum albumin (HSA), a water soluble protein, resulting in the diminishment of fluorescence from the tryptophan residue. Because riboflavin hardly photosensitized singlet oxygen generation and sodium azide, a singlet oxygen quencher, did not inhibit protein damage, electron transfer-mediated oxidation of HSA was speculated. Fluorescence lifetime of riboflavin was not affected by HSA, suggesting that the excited triplet state of riboflavin is responsible for protein damage through electron transfer. In addition, the preventive effect of xanthone derivatives, triplet quenchers, on photosensitized protein damage could be evaluated using this photosensitized reaction system of riboflavin and HSA.

  14. Tc-99 m-GSA liver scintigraphy in alcoholic liver cirrhosis

    International Nuclear Information System (INIS)

    Itano, Satoshi; Harada, Masaru; Nagamatsu, Hiroaki

    2003-01-01

    We compared 15 alcoholic liver cirrhosis patients with 10 viral liver cirrhosis patients using technetium-99 m-galactosyl human serum albumin (Tc-99 m-GSA) liver scintigraphy and could clinically reveal the disorder of metabolism of asialoglycoprotein in alcoholic liver cirrhosis. Receptor index (LHL 15 = liver count divided by the sum of liver and heart counts at 15 minutes) was significantly (p <0.01) lower in patients with alcoholic cirrhosis (median: 0.821), compared with patients with viral cirrhosis (0.915). Grading score, which was an index showed by the difference in the isotope uptake patterns between liver and heart, was significantly (p <0.01) worse in patients with alcoholic cirrhosis, compared with patients with viral cirrhosis. These results suggested that alcoholic liver cirrhosis had a specific disorder of a metabolic function for asialoglycoprotein. (author)

  15. Dual-phase 99mTc-MIBI scintigraphy with delayed neck and thorax SPECT/CT and bone scintigraphy in patients with primary hyperparathyroidism. Correlation with clinical or pathological variables

    International Nuclear Information System (INIS)

    Qiu, Zhongling; Shen, Chentian; Zhu, Ruisen; Luo, Quanyong; Wu, Bo

    2014-01-01

    The purpose of this study was to assess the relationship between 99m Tc-MIBI and 99m Tc-MDP bone scintigraphy and clinical or pathological variables, including preoperative serum PTH levels and tumor diameter, in patients with newly diagnosed PHPT. Dual phase 99m Tc-MIBI planar scintigraphy was performed in 244 patients with PHPT. Of these patients, 155 underwent 99m Tc-MDP bone scintigraphy to detect bone changes before parathyroidectomy. Factors influencing 99m Tc-MIBI scintigraphy and 99m Tc-MDP bone scintigraphy detection rate were assessed using univariate and multivariate logistic regression analysis; optimal cutoff values for predicting positive 99m Tc-MIBI and 99m Tc-MDP bone scintigraphy were evaluated using ROC analysis. Among 244 patients, 174 (71.31%) patients with 181 foci had a positive 99m Tc-MIBI planar scintigraphy; delayed neck and thorax SPECT/CT could identify and locate the 99m Tc-MIBI lesions but could not find more lesions than planar scintigraphy. 70 (28.69%) patients had a negative 99m Tc-MIBI planar scintigraphy. Tumor diameter, serum PTH level and symptoms were statistically significant predictive factors in predicting positive 9m Tc-MIBI scintigraphy both univariate and multivariate logistic regression analyses. The optimal thresholds for tumor diameter and serum PTH by ROC analysis were 1.03 cm and 127.60 ng/L, respectively. Among 155 patients with bone scintigraphy, 99m Tc-MDP bone scintigraphy showed positive finding in 80 (51.61%) patients and negative finding in 75 patients. Univariate logistic regression analysis showed that patient age, sex, tumor diameter and PTH level (≥150 ng/L) were statistically significant in predicting positive 99m Tc-MDP bone scintigraphy. Multivariate logistic regression analysis showed both tumor diameter and PTH ≥150 ng/L were statistically significant in predicting positive 99m Tc-MDP bone scintigraphy. The optimal thresholds for tumor diameter and serum PTH by ROC analysis were 1.96 cm and 163

  16. The impact of change in albumin assay on reference intervals, prevalence of 'hypoalbuminaemia' and albumin prescriptions.

    Science.gov (United States)

    Coley-Grant, Deon; Herbert, Mike; Cornes, Michael P; Barlow, Ian M; Ford, Clare; Gama, Rousseau

    2016-01-01

    We studied the impact on reference intervals, classification of patients with hypoalbuminaemia and albumin infusion prescriptions on changing from a bromocresol green (BCG) to a bromocresol purple (BCP) serum albumin assay. Passing-Bablok regression analysis and Bland-Altman plot were used to compare Abbott BCP and Roche BCG methods. Linear regression analysis was used to compare in-house and an external laboratory Abbott BCP serum albumin results. Reference intervals for Abbott BCP serum albumin were derived in two different laboratories using pathology data from adult patients in primary care. Prescriptions for 20% albumin infusions were compared one year before and one year after changing the albumin method. Abbott BCP assay had a negative bias of approximately 6 g/L compared with Roche BCG method.There was good agreement (y = 1.04 x - 1.03; R(2 )= 0.9933) between in-house and external laboratory Abbott BCP results. Reference intervals for the serum albumin Abbott BCP assay were 31-45 g/L, different to those recommended by Pathology Harmony and the manufacturers (35-50 g/L). Following the change in method there was a large increase in the number of patients classified as hypoalbuminaemic using Pathology Harmony references intervals (32%) but not when retrospectively compared to locally derived reference intervals (16%) compared with the previous year (12%). The method change was associated with a 44.6% increase in albumin prescriptions. This equated to an annual increase in expenditure of £35,234. We suggest that serum albumin reference intervals be method specific to prevent misclassification of albumin status in patients. Change in albumin methodology may have significant impact on hospital resources. © The Author(s) 2015.

  17. Serum Albumin and Cerebro-cardiovascular Mortality During a 15-year Study in a Community-based Cohort in Tanushimaru, a Cohort of the Seven Countries Study.

    Science.gov (United States)

    Umeki, Yoko; Adachi, Hisashi; Enomoto, Mika; Fukami, Ako; Nakamura, Sachiko; Nohara, Yume; Nakao, Erika; Sakaue, Akiko; Tsuru, Tomoko; Morikawa, Nagisa; Fukumoto, Yoshihiro

    Objective There is little long-term data on the association between the serum albumin levels and mortality in community-based populations. We aimed to determine whether the serum albumin level is an independent risk factor for all-cause and cause-specific death in a community-based cohort study in Japan. Methods In 1999, we performed a periodic epidemiological survey over a 15-year period in a population of 1,905 healthy subjects (783 males, 1,122 females) who were older than 40 years of age and who resided in Tanushimaru, a rural community, in Japan. Over the course of the study, we periodically examined the blood chemistry of the study subjects, including their serum albumin levels. Their baseline serum albumin levels were categorized into quartiles. Results The baseline albumin levels were significantly associated with age (inversely), body mass index (BMI), diastolic blood pressure, lipid profiles [high density lipoprotein-cholesterol (HDL-c), low-density lipoprotein-cholesterol (LDL-c) and triglycerides] and estimated glomerular filtration rate (eGFR). After adjusting for confounders, a Cox proportional hazards regression analysis demonstrated that a low serum albumin level was an independent predictor of all-cause death [hazard ratio (HR): 0.39, 95% confidence interval (CI): 0.24-0.65], cancer death (HR: 0.43, 95% CI: 0.18-0.99), death from infection (HR: 0.21, 95% CI: 0.06-0.73) and cerebro-cardiovascular death (HR: 0.19, 95% CI: 0.06-0.63). The HRs for all-cause and cerebro-cardiovascular death in the highest quartile vs. the lowest quartile of albumin after adjusting for confounders were 0.59 (95%CI:0.39-0.88) and 0.15 (95%CI: 0.03-0.66), respectively. Conclusion The serum albumin level was thus found to be a predictor of all-cause and cerebro-cardiovascular death in a general population.

  18. Covalent Modification of Human Serum Albumin by the Natural Sesquiterpene Lactone Parthenolide

    Directory of Open Access Journals (Sweden)

    Michael Plöger

    2015-04-01

    Full Text Available The reactivity of parthenolide (PRT, a natural sesquiterpene lactone from Tanacetum parthenium (Asteraceae, with human serum albumin (HSA was studied by UHPLC/+ESI-QqTOF MS analysis after tryptic digestion of albumin samples after incubation with this compound. It was found that the single free cysteine residue, C34, of HSA (0.6 mM reacted readily with PRT when incubated at approximately 13-fold excess of PRT (8 mM. Time-course studies with PRT and its 11β,13-dihydro derivative at equimolar ratios of the reactants revealed that PRT under the chosen conditions reacts preferably with C34 and does so exclusively via its α-methylene-γ-lactone moiety, while the epoxide structure is not involved in the reaction.

  19. Covalent binding of nitrogen mustards to the cysteine-34 residue in human serum albumin

    NARCIS (Netherlands)

    Noort, D.; Hulst, A.G.; Jansen, R.

    2002-01-01

    Covalent binding of various clinically important nitrogen mustards to the cysteine-34 residue of human serum albumin, in vitro and in vivo, is demonstrated. A rapid method for detection of these adducts is presented, based on liquid chromatography-tandem mass spectrometry analysis of the adducted

  20. Clinical need for both scintigraphy with technetium-99m GSA and per-rectal portal scintigraphy in some patients with chronic liver disease

    Energy Technology Data Exchange (ETDEWEB)

    Shiomi, Susumu; Iwata, Yoshinori; Sasaki, Nobumitsu [Osaka City Univ. (Japan). Medical School] (and others)

    1999-08-01

    Scintigraphy with {sup 99m}Tc-diethylenetriaminepentaacetate with galactosyl human serum albumin ({sup 99m}Tc-GSA) and per-rectal portal scintigraphy are useful for evaluating hepatic functional reserve and portal circulation, respectively. We did the procedures simultaneously in some patients to examine the relationship between hepatic functional reserve and portal circulation in chronic liver disease. Scintigraphy with {sup 99m}Tc-GSA was done in 10 healthy subjects, 45 patients with chronic hepatitis, and 165 patients with cirrhosis. Fifty-seven patients (13 with hepatitis and 44 with cirrhosis) also underwent per-rectal portal scintigraphy with {sup 99m}Tc-pertechnetate within two weeks. A receptor index was calculated by dividing the radioactivity of the liver region of interest (ROI) by that of the liver-plus-heart ROI at 15 min after the injection of {sup 99m}Tc-GSA. The index of blood clearance was calculated by dividing the radioactivity of the heart ROI at 15 min by that of the heart ROI at 3 min. A solution containing {sup 99m}Tc-pertechnetate was instilled into the rectum, and serial scintigrams were taken while radioactivity curves for the liver and heart were recorded sequentially. A per-rectal portal shunt index was determined by calculating the ratio of counts for the liver to counts for the heart integrated for 24 seconds immediately after the appearance of the liver time-activity curve. The median receptor index was lower for more severe liver disorders, increasing in the order of chronic hepatitis, compensated cirrhosis and decompensated cirrhosis, and the median index of blood clearance was higher. The median receptor index was significantly lower when a complication (varices, ascites, or encephalopathy) was present, and the median index of blood clearance was higher. The shunt index was correlated significantly with the two other indices, but these values for some one-third of the patients disagreed in either indices. Scintigraphy with {sup 99m

  1. The mechanism of energy transfer from poly-p-benzoylphenylacetimido-bovine serum albumin to small-molecule quenchers

    International Nuclear Information System (INIS)

    Mariano, P.S.; Glover, G.I.; Wilkinson, T.J.

    1976-01-01

    Results of a quantitative photochemical study of poly-p-benzoyl-phenylacetimido-bovine serum albumin in the presence of small-molecule triplet quenchers are reported. The efficiency of quenching by organic salts containing low triplet energy chromophores has been shown to be qualitatively dependent on their predicted association constants to the modified protein. In addition, quenching was inhibited by salts of organic acids which possess high binding affinities for the protein but do not contain chromophores of low triplet energy. Quantitative treatment of the quenching and inhibition data yielded results which strongly support the operation of an 'affinity controlled' mechanism for triplet energy transfer from the benzophenone moieties of the modified-bovine serum albumin to quenchers such as α-naphthylacetate and trans-cinnamate. (author)

  2. Biophysical studies of interaction between hydrolysable tannins isolated from Oenothera gigas and Geranium sanguineum with human serum albumin.

    Science.gov (United States)

    Sekowski, Szymon; Ionov, Maksim; Kaszuba, Mateusz; Mavlyanov, Saidmukhtar; Bryszewska, Maria; Zamaraeva, Maria

    2014-11-01

    Tannins, secondary plant metabolites, possess diverse biological activities and can interact with biopolymers such as lipids or proteins. Interactions between tannins and proteins depend on the structures of both and can result in changes in protein structure and activity. Because human serum albumin is the most abundant protein in plasma and responsible for interactions with important biological compounds (e.g. bilirubin) and proper blood pressure, therefore, it is very important to investigate reactions between HSA and tannins. This paper describes the interaction between human serum albumin (HSA) and two tannins: bihexahydroxydiphenoyl-trigalloylglucose (BDTG) and 1-O-galloyl-4,6-hexahydroxydiphenoyl-β-d-glucose (OGβDG), isolated from Geranium sanguineum and Oenothera gigas leafs, respectively. Optical (spectrofluorimetric) and chiral optical (circular dichroism) methods were used in this study. Fluorescence analysis demonstrated that OGβDG quenched HSA fluorescence more strongly than BDTG. Both OGβDG and BDTG formed complexes with albumin and caused a red shift of the fluorescence spectra but did not significantly change the protein secondary structure. Our studies clearly demonstrate that the tested tannins interact very strongly with human serum albumin (quenching constant K=88,277.26±407.04 M(-1) and K=55,552.67±583.07 M(-1) respectively for OGβDG and BDTG) in a manner depending on their chemical structure. Copyright © 2014 Elsevier B.V. All rights reserved.

  3. Perfusion lung scintigraphy in primary broncho-pulmonary cancer

    International Nuclear Information System (INIS)

    Lapergue, Paul.

    1976-01-01

    Research on primary broncho-pulmonary cancer has called extensively on scintigraphy and it seemed interesting to weigh up the pros and cons of the technique in this particular case. Our intention is to sum up objectively from recent documents the applications of scintigraphy in the study of primary broncho-pulmonary cancers and to attempt, on the basis of the results compiled, to show what benefits have been gained from this technique and to find out whether it has any pre-surgical value and of what kind. The technique was invariable; the tracer consists of human albumin macro-aggregates labelled with technetium 99m which by its short half-life and slight penetration enables four exposures to be taken during the same examination (front, back, right and left profiles), thus reducing the risks of mistaken diagnoses due to the use of a single incidence. Similarly the detection method was always the scintillation camera which explores the whole organ at once, considerably shortening the examination time. Lung scintigraphy by perfusion of labelled human albumin macro-aggregates offers the great advantage of being simple to use and harmless. It is easy to understand the important place it has taken in the range of methods available for lung circulation exploration [fr

  4. Effect of Temperature on Tolbutamide Binding to Glycated Serum Albumin

    Directory of Open Access Journals (Sweden)

    Agnieszka Szkudlarek

    2017-03-01

    Full Text Available Glycation process occurs in protein and becomes more pronounced in diabetes when an increased amount of reducing sugar is present in bloodstream. Glycation of protein may cause conformational changes resulting in the alterations of its binding properties even though they occur at a distance from the binding sites. The changes in protein properties could be related to several pathological consequences such as diabetic and nondiabetic cardiovascular diseases, cataract, renal dysfunction and Alzheimer’s disease. The experiment was designed to test the impact of glycation process on sulfonylurea drug tolbutamide-albumin binding under physiological (T = 309 K and inflammatory (T = 311 K and T = 313 K states using fluorescence and UV-VIS spectroscopies. It was found in fluorescence analysis experiments that the modification of serum albumin in tryptophanyl and tyrosyl residues environment may affect the tolbutamide (TB binding to albumin in subdomain IIA and/or IIIA (Sudlow’s site I and/or II, and also in subdomains IB and IIB. We estimated the binding of tolbutamide to albumin described by a mixed nature of interaction (specific and nonspecific. The association constants Ka (L∙mol−1 for tolbutamide at its high affinity sites on non-glycated albumin were in the range of 1.98–7.88 × 104 L∙mol−1 (λex = 275 nm, 1.20–1.64 × 104 L∙mol−1 (λex = 295 nm and decreased to 1.24–0.42 × 104 L∙mol−1 at λex = 275 nm (T = 309 K and T = 311 K and increased to 2.79 × 104 L∙mol−1 at λex = 275 nm (T = 313 K and to 4.43–6.61 × 104 L∙mol−1 at λex = 295 nm due to the glycation process. Temperature dependence suggests the important role of van der Waals forces and hydrogen bonding in hydrophobic interactions between tolbutamide and both glycated and non-glycated albumin. We concluded that the changes in the environment of TB binding of albumin in subdomain IIA and/or IIIA as well as in subdomains IB and IIB influence on

  5. Albumin extravasation in bicuculline-induced blood-brain barrier dysfunction

    International Nuclear Information System (INIS)

    Persson, L.I.; Rosengren, L.E.; Johansson, B.B.

    1980-01-01

    The extravasation of endogeneous rat albumin and exogeneous 125 I-labeled human serum albumin was compared in rats subjected to bicuculline-induced blood-brain barrier dysfunction. The correlation between rocket immunoelectrophoretic assays of endogeneous rat albumin and 125 I-labeled human serum albumin, assayed by gamma scintillation counting, was good irrespective of whether 125 I-labeled albumin was studied in whole brain tissue or in brain homogenates. The ratio of brain to serum albumin was similar with the two assay methods. (author)

  6. Labeling of human serum albumin with 105Rh-cysteine complexes

    International Nuclear Information System (INIS)

    Lo, J.M.; Pillai, M.R.A.; John, C.S.; Troutner, D.E.

    1990-01-01

    The conjugation of a complex formed by reacting RhCl 3 with cysteine to human serum albumin has been investigated. Approximately 50% of the rhodium (labelled with 105 Rh) was converted to the complex. Conjugation of the complex to HSA via the ECDI method resulted in yields of ∼ 40% of the total rhodium or ∼ 80% of the Rh-cysteine complex. No conjugation was observed in the absence of the ECDI. At approximately equal molar concentrations of rhodium and HSA, an average of ∼ 0.4 rhodium atoms per HSA molecule was achieved. (author)

  7. Study on the interaction of the toxic food additive carmoisine with serum albumins: A microcalorimetric investigation

    International Nuclear Information System (INIS)

    Basu, Anirban; Kumar, Gopinatha Suresh

    2014-01-01

    Highlights: • Carmoisine binds to both the serum albumins with affinity of the order of 10 6 M −1 . • The binding was favored by negative enthalpy and positive entropy changes. • The binding was dominated by hydrophobic forces. • Carmoisine enhanced the thermal stability of both the proteins remarkably. - Abstract: The interaction of the synthetic azo dye and food colorant carmoisine with human and bovine serum albumins was studied by microcalorimetric techniques. A complete thermodynamic profile of the interaction was obtained from isothermal titration calorimetry studies. The equilibrium constant of the complexation process was of the order of 10 6 M −1 and the binding stoichiometry was found to be 1:1 with both the serum albumins. The binding was driven by negative standard molar enthalpy and positive standard molar entropy contributions. The binding affinity was lower at higher salt concentrations in both cases but the same was dominated by mostly non-electrostatic forces at all salt concentrations. The polyelectrolytic forces contributed only 5–8% of the total standard molar Gibbs energy change. The standard molar enthalpy change enhanced whereas the standard molar entropic contribution decreased with rise in temperature but they compensated each other to keep the standard molar Gibbs energy change almost invariant. The negative standard molar heat capacity values suggested the involvement of a significant hydrophobic contribution in the complexation process. Besides, enthalpy–entropy compensation phenomenon was also observed in both the systems. The thermal stability of the serum proteins was found to be remarkably enhanced on binding to carmoisine

  8. Combined determination of serum type IV collagen with urine Tamm-Horsfall protein and albumin for early diagnosis in diabetic retinopathy

    International Nuclear Information System (INIS)

    Wang Hong; Zhang Aihua; Ren Yuguo

    2003-01-01

    Objective: To study the relationship between changes of serum type IV collagen, urine Tamm-horsfall protein, albumin and development of diabetic retinopathy (DR) in patients with type 2 diabetes mellitus. Methods: Serum CIV, urine THP and Alb were determined with ELISA and RIA respectively in 76 patients with type 2 diabetes mellitus (NDR26, BDR26, PDR24) and 30 controls. Results: Values of the three markers were significantly different among the three groups of patients (p < 0.01; p < 0.01; p < 0.001 respectively). Conclusion: Serum type IV collagens, urine Tamm-Horsfall protein and albumin were sensitive indicators in predicting diabetic retinopathy

  9. Bovine Serum Albumin binding to CoCrMo nanoparticles and the influence on dissolution

    International Nuclear Information System (INIS)

    Simoes, T A; Brown, A P; Milne, S J; Brydson, R M D

    2015-01-01

    CoCrMo alloys exhibit good mechanical properties, excellent biocompatibility and are widely utilised in orthopaedic joint replacements. Metal-on-metal hip implant degradation leads to the release of metal ions and nanoparticles, which persist through the implant's life and could be a possible cause of health complications. This study correlates preferential binding between proteins and metal alloy nanoparticles to the alloy's corrosion behaviour and the release of metal ions. TEM images show the formation of a protein corona in all particles immersed in albumin containing solutions. Only molybdenum release was significant in these tests, suggesting high dissolution of this element when CoCrMo alloy nanoparticles are produced as wear debris in the presence of serum albumin. The same trend was observed during extended exposure of molybdenum reference nanoparticles to albumin. (paper)

  10. Gamma-scintigraphy; La gammascintigraphie

    Energy Technology Data Exchange (ETDEWEB)

    Desgrez, H.A. [Commissariat a l' Energie Atomique, Saclay (France). Centre d' Etudes Nucleaires

    1960-06-15

    Gamma-scintigraphy is a medical technique making it possible to fix the image of certain organs after the concentration in these of emitting radioactive products. It is already widely used in the case of the thyroid gland with iodine-132 by applying the isotope iodine 131. The study of the liver and gall bladder is carried out using colloidal gold 198 and Bengal pink marked with iodine 131. Serum albumin marked with iodine 131 makes it possible to study rachidian blockages. Other applications can already be foreseen in this direction. (author) [French] La gammascintigraphie est une technique medicale permettant de faire l'image de certains organes apres concentration dans ceux-ci de produits radioactifs emetteurs. Son utilisation deja repandue en ce qui concerne la thyroidine et l'iode-131 est possible avec l'iode-132 pour cette meme glande. Avec l'or colloidal 198 et le rose bengale marque a l'iode-131, on pratique des etudes du foie et de la vesicule biliaire. La serumalbumine marquee a l'iode-131 permet d'etudier les blocages rachidiens. D'autres possibilites sont des maintenant envisageables dans cette direction. (auteur)

  11. Gamma-scintigraphy; La gammascintigraphie

    Energy Technology Data Exchange (ETDEWEB)

    Desgrez, H A [Commissariat a l' Energie Atomique, Saclay (France). Centre d' Etudes Nucleaires

    1960-06-15

    Gamma-scintigraphy is a medical technique making it possible to fix the image of certain organs after the concentration in these of emitting radioactive products. It is already widely used in the case of the thyroid gland with iodine-132 by applying the isotope iodine 131. The study of the liver and gall bladder is carried out using colloidal gold 198 and Bengal pink marked with iodine 131. Serum albumin marked with iodine 131 makes it possible to study rachidian blockages. Other applications can already be foreseen in this direction. (author) [French] La gammascintigraphie est une technique medicale permettant de faire l'image de certains organes apres concentration dans ceux-ci de produits radioactifs emetteurs. Son utilisation deja repandue en ce qui concerne la thyroidine et l'iode-131 est possible avec l'iode-132 pour cette meme glande. Avec l'or colloidal 198 et le rose bengale marque a l'iode-131, on pratique des etudes du foie et de la vesicule biliaire. La serumalbumine marquee a l'iode-131 permet d'etudier les blocages rachidiens. D'autres possibilites sont des maintenant envisageables dans cette direction. (auteur)

  12. Investigation of the interaction between isomeric derivatives and human serum albumin by fluorescence spectroscopy and molecular modeling

    Energy Technology Data Exchange (ETDEWEB)

    Wang, Ruiyong, E-mail: wangry@zzu.edu.cn; Dou, Huanjing; Yin, Yujing; Xie, Yuanzhe; Sun, Li; Liu, Chunmei; Dong, Jingjing; Huang, Gang; Zhu, Yanyan; Song, Chuanjun, E-mail: chjsong@zzu.edu.cn; Chang, Junbiao, E-mail: changjunbiao@zzu.edu.cn

    2014-10-15

    In this paper, we have synthesized 9H-pyrrolo[1,2-a]indol-9-ones and the isomeric indeno[2,1-b]pyrrol-8-ones. The interactions of human serum albumin with series of isomeric derivatives have been studied by spectrophotometric methods. Results show the intrinsic fluorescence is quenched by the derivatives with a static quenching procedure. The thermodynamics parameters indicate that van der Waals forces and hydrogen bonds play a major role in the interactions. The results of synchronous fluorescence spectra demonstrate that the microenvironments of Trp residue of human serum albumin are disturbed by most derivatives. Thermodynamic results showed that the 9H-pyrrolo[1,2-a]indol-9-ones are stronger quenchers and bind to human serum albumin with the higher affinity than isomeric indeno[2,1-b]pyrrol-8-ones. The influence of molecular structure on the binding aspects has been investigated. - Highlights: • The interactions between isomeric derivatives and HSA have been investigated. • Results reveal that 9H-pyrrolo[1,2-a]indol-9-ones are stronger quenchers for HSA. • Hydrogen bonds and van der Waals forces play major role in the binding process. • The influence of molecular structure on the binding aspects has been investigated. • The binding study was also modeled by molecular docking.

  13. Investigation of the interaction between isomeric derivatives and human serum albumin by fluorescence spectroscopy and molecular modeling

    International Nuclear Information System (INIS)

    Wang, Ruiyong; Dou, Huanjing; Yin, Yujing; Xie, Yuanzhe; Sun, Li; Liu, Chunmei; Dong, Jingjing; Huang, Gang; Zhu, Yanyan; Song, Chuanjun; Chang, Junbiao

    2014-01-01

    In this paper, we have synthesized 9H-pyrrolo[1,2-a]indol-9-ones and the isomeric indeno[2,1-b]pyrrol-8-ones. The interactions of human serum albumin with series of isomeric derivatives have been studied by spectrophotometric methods. Results show the intrinsic fluorescence is quenched by the derivatives with a static quenching procedure. The thermodynamics parameters indicate that van der Waals forces and hydrogen bonds play a major role in the interactions. The results of synchronous fluorescence spectra demonstrate that the microenvironments of Trp residue of human serum albumin are disturbed by most derivatives. Thermodynamic results showed that the 9H-pyrrolo[1,2-a]indol-9-ones are stronger quenchers and bind to human serum albumin with the higher affinity than isomeric indeno[2,1-b]pyrrol-8-ones. The influence of molecular structure on the binding aspects has been investigated. - Highlights: • The interactions between isomeric derivatives and HSA have been investigated. • Results reveal that 9H-pyrrolo[1,2-a]indol-9-ones are stronger quenchers for HSA. • Hydrogen bonds and van der Waals forces play major role in the binding process. • The influence of molecular structure on the binding aspects has been investigated. • The binding study was also modeled by molecular docking

  14. Structural consistency analysis of recombinant and wild-type human serum albumin

    Science.gov (United States)

    Cao, Hui-Ling; Sun, Li-Hua; Liu, Li; Li, Jian; Tang, Lin; Guo, Yun-Zhu; Mei, Qi-Bing; He, Jian-Hua; Yin, Da-Chuan

    2017-01-01

    Recombinant human serum albumin (rHSA) is potential alternatives for human serum albumin (HSA) which may ease severe shortage of HSA worldwide. In theory, rHSA and HSA are the same. Structure decides function. Therefore, the 3D structural consistency analysis of rHSA and HSA is outmost importance, which is the base of their function consistency. In this paper, the crystal structures of rHSA at resolution limit of 2.22 Å and HSA at 2.30 Å were determined by X-ray diffraction (XRD), which were deposited in the Protein Data Bank (PDB) with accession codes 4G03 (rHSA) and 4G04 (HSA). The differences between rHSA and HSA were systematically analyzed from the crystallization behavior, diffraction data and three-dimensional (3D) structure. The superimposed contrasted analysis indicated that rHSA and HSA achieved a structural similarity of 99% with an r.m.s. deviation of 0.397 Å for the corresponding overall Cα atoms. In addition, the number of α-helices in the rHSA or HSA molecule was verified to be 30. As a result, rHSA can potentially replace HSA. The study provides a theoretical and experimental basis for the clinical and additional applications of rHSA. Meanwhile, it is also a good example for applications of genetic engineering.

  15. A facile route to glycated albumin detection.

    Science.gov (United States)

    Bohli, Nadra; Meilhac, Olivier; Rondeau, Philippe; Gueffrache, Syrine; Mora, Laurence; Abdelghani, Adnane

    2018-07-01

    In this paper we propose an easy way to detect the glycated form of human serum albumin which is biomarker for several diseases such as diabetes and Alzheimer. The detection platform is a label free impedimetric immunosensor, in which we used a monoclonal human serum albumin antibody as a bioreceptor and electrochemical impedance as a transducing method. The antibody was deposited onto a gold surface by simple physisorption technique. Bovine serum albumin was used as a blocking agent for non-specific binding interactions. Cyclic voltammetry and electrochemical impedance spectroscopy were used for the characterization of each layer. Human serum albumin was glycated at different levels with several concentrations of glucose ranging from 0 mM to 500 mM representing physiological, pathological (diabetic albumin) and suprapathological concentration of glucose. Through the calibration curves, we could clearly distinguish between two different areas related to physiological and pathological albumin glycation levels. The immunosensor displayed a linear range from 7.49% to 15.79% of glycated albumin to total albumin with a good sensitivity. Surface plasmon resonance imaging was also used to characterize the developed immunosensor. Copyright © 2018 Elsevier B.V. All rights reserved.

  16. Extending the half-life of a fab fragment through generation of a humanized anti-human serum albumin Fv domain: An investigation into the correlation between affinity and serum half-life.

    Science.gov (United States)

    Adams, Ralph; Griffin, Laura; Compson, Joanne E; Jairaj, Mark; Baker, Terry; Ceska, Tom; West, Shauna; Zaccheo, Oliver; Davé, Emma; Lawson, Alastair Dg; Humphreys, David P; Heywood, Sam

    2016-10-01

    We generated an anti-albumin antibody, CA645, to link its Fv domain to an antigen-binding fragment (Fab), thereby extending the serum half-life of the Fab. CA645 was demonstrated to bind human, cynomolgus, and mouse serum albumin with similar affinity (1-7 nM), and to bind human serum albumin (HSA) when it is in complex with common known ligands. Importantly for half-life extension, CA645 binds HSA with similar affinity within the physiologically relevant range of pH 5.0 - pH 7.4, and does not have a deleterious effect on the binding of HSA to neonatal Fc receptor (FcRn). A crystal structure of humanized CA645 Fab in complex with HSA was solved and showed that CA645 Fab binds to domain II of HSA. Superimposition with the crystal structure of FcRn bound to HSA confirmed that CA645 does not block HSA binding to FcRn. In mice, the serum half-life of humanized CA645 Fab is 84.2 h. This is a significant extension in comparison with Fab variant. The Fab-HSA structure was used to design a series of mutants with reduced affinity to investigate the correlation between the affinity for albumin and serum half-life. Reduction in the affinity for MSA by 144-fold from 2.2 nM to 316 nM had no effect on serum half-life. Strikingly, despite a reduction in affinity to 62 µM, an extension in serum half-life of 26.4 h was still obtained. CA645 Fab and the CA645 Fab-HSA complex have been deposited in the Protein Data Bank (PDB) with accession codes, 5FUZ and 5FUO, respectively.

  17. Influence of starvation, triton WR-1339 and [131I]-human serum albumin on rat liver lysosomes

    International Nuclear Information System (INIS)

    Harikumar, P.; Ninjoor, V.

    1986-01-01

    The response of rat liver lysosomes to starvation and administration of lysosomotropic agents viz. Triton WR-1339 and [ 131 I]-human serum albumin, was assessed in terms of their distribution pattern after isopycnic sucrose density gradient centrifugation. Starvation induced changes in lysosomes appeared to be similar to that produced by the detergent uptake. Both the treatments caused a distinct decline in the equilibration densities of the organelles. On the other hand, injected labelled protein failed to comigrate with the lysosomal markers in starved as well as Triton treated rats and conspicuously remained in a region of high specific gravity in the gradient. These findings indicate retarded fusion between secondary lysosomes and [ 131 I]-human serum albumin containing phagosomes in the livers of rats subjected to starvation or detergent treatment. (author)

  18. Studies on interaction between flavonoids and bovine serum albumin by spectral methods

    International Nuclear Information System (INIS)

    Shi Xiaolei; Li Xuwen; Gui Mingyu; Zhou Hongyu; Yang Ruijie; Zhang Hanqi; Jin Yongri

    2010-01-01

    The interaction between three kinds of flavonoids and bovine serum albumin (BSA) was investigated by fluorescence and UV-vis absorption spectrometry. The results indicated that flavonoids have strong ability to quench the intrinsic fluorescence of BSA by forming complexes. The binding constants, number of binding sites, thermodynamic parameters and energy transfer mechanisms were also investigated. Conformation change of BSA was observed from synchronous, three-dimensional fluorescence and circular dichroism spectrum.

  19. Adsorption behavior of cation-exchange resin-mixed polyethersulfone-based fibrous adsorbents with bovine serum albumin

    NARCIS (Netherlands)

    Zhang, Y.; Zhang, Yuzhong; Borneman, Zandrie; Koops, G.H.; Wessling, Matthias

    2006-01-01

    The cation-exchange resin-mixed polyethersulfone (PES)-based fibrous adsorbents were developed to study their adsorption behavior with bovine serum albumin (BSA). A fibrous adsorbent with an open pore surface had much better adsorption behavior with a higher adsorbing rate. The adsorption capacity

  20. Effect of Human and Bovine Serum Albumin on kinetic Chemiluminescence of Mn (III-Tetrakis (4-Sulfonatophenyl Porphyrin-Luminol-Hydrogen Peroxide System

    Directory of Open Access Journals (Sweden)

    Sayed Yahya Kazemi

    2012-01-01

    Full Text Available The present work deals with an attempt to study the effect of human and bovine serum albumin on kinetic parameters of chemiluminescence of luminol-hydrogen peroxide system catalyzed by manganese tetrasulfonatophenyl porphyrin (MnTSPP. The investigated parameters involved pseudo-first-order rise and fall rate constant for the chemiluminescence burst, maximum level intensity, time to reach maximum intensity, total light yield, and values of the intensity at maximum CL which were evaluated by nonlinear least square program KINFIT. Because of interaction of metalloporphyrin with proteins, the CL parameters are drastically affected. The systems resulted in Stern-Volmer plots with values of 3.17×105 and 3.7×105M−1 in the quencher concentration range of 1.5×10−6 to 1.5×10−5 M for human serum albumin (HSA and bovine serum albumin (BSA, respectively.

  1. Determination of human albumin in serum and urine samples by constant-energy synchronous fluorescence method.

    Science.gov (United States)

    Madrakian, Tayyebeh; Bagheri, Habibollah; Afkhami, Abbas

    2015-08-01

    A sensitive spectrofluorimetric method using constant-energy synchronous fluorescence technique is proposed for the determination of human albumin without separation. In this method, no reagent was used for enhancement of the fluorescence signal of albumin in the solution. Effects of some parameters, such as energy difference between excitation and emission monochromators (ΔE), emission and excitation slit widths and scan rate of wavelength were studied and the optimum conditions were established. For this purpose factorial design and response surface method were employed for optimization of the effective parameters on the fluorescence signal. The results showed that the scan rate of the wavelength has no significant effect on the analytical signal. The calibration curve was linear in the range 0.1-220.0 µg mL(-1) of albumin with a detection limit of 7.0 × 10(-3)  µg mL(-1). The relative standard deviations (RSD) for six replicate measurements of albumin were calculated as 2.2%, 1.7% and 1.3% for 0.5, 10.0 and 100.0 µg mL(-1) albumin, respectively. Furthermore the proposed method has been employed for the determination of albumin in human serum and urine samples. Copyright © 2014 John Wiley & Sons, Ltd.

  2. Interactions between 4-(2-dimethylaminoethyloxy)-N-octadecyl-1,8-naphthalimide and serum albumins: Investigation by spectroscopic approach

    Energy Technology Data Exchange (ETDEWEB)

    Sun Yang; Wei Song [School of Chemical Engineering, Northwest University, No. 229 Taibai North Road, Xi' an, Shaanxi 710069 (China); Zhao Yingyong [Biomedicine Key Laboratory of Shaanxi Province, Northwest University, No. 229 Taibai North Road, Xi' an, Shaanxi 710069 (China); Hu Xiaoyun, E-mail: hxy3275@nwu.edu.cn [Department of Physics, Northwest University, No. 229 Taibai North Road, Xi' an, Shaanxi 710069 (China); Fan Jun, E-mail: fanjun@nwu.edu.cn [School of Chemical Engineering, Northwest University, No. 229 Taibai North Road, Xi' an, Shaanxi 710069 (China)

    2012-04-15

    A novel 4-(2-dimethylaminoethyloxy)-N-octadecyl-1,8-naphthalimide (DON) has been synthesized as a spectrofluorimetric probe for the determination of proteins. Photophysics of DON in different solvents has been delineated in this paper. Progressive redshift with polarity of solvents in emission and absorption spectra hints at intramolecular charge transfer. The interactions of DON with serum albumins (i.e., human serum albumin (HSA) and bovine serum albumin (BSA)) were studied by fluorescence and absorption spectroscopy. Fluorescence data revealed that the quenching of HSA/BSA by DON were static quenching and the DON-HSA/BSA complexes were formed. The binding constant (K{sub b}) for HSA and was found to be 8.44 Multiplication-Sign 10{sup -4} and 60.26 Multiplication-Sign 10{sup -4} M{sup -1} and the number of binding sites (n) were 1.00 and 1.40, respectively. The thermodynamic parameters, {Delta}H and {Delta}S, for the DON-HSA system was calculated to be -14.83 kJ mol{sup -1} and 23.61 J mol{sup -1} K{sup -1}, indicating the hydrogen bonds and hydrophobic interactions were the dominant intermolecular force. {Delta}H and {Delta}S for the binding of DON with BSA was -60.08 kJ mol{sup -1} and -90.7441 mol{sup -1} K{sup -1}, suggesting the hydrogen bonds and van der Waals force played the main role in the interaction. The results of displacement experiments showed that DON bound HSA/BSA occurred at the Trp-214 proximity, located in subdomain IIA of the serum albumin structure (the warfarin binding pocket). The effect of DON on the conformation of HSA was also analyzed by synchronous and three-dimensional fluorescence spectra. The fluorescence of DON could be quenched by HSA, based on which, a fluorometric method for the determination of microamount protein using DON in the medium of HCl-Tris buffer solution (pH=7.4) was developed. The linear range of the calibration curves was 0.1-10.0 {mu}M for HSA, 0.1-11.2 {mu}M for BSA and 0.2-9.7 {mu}M for egg albumin (EA). The

  3. Interactions between 4-(2-dimethylaminoethyloxy)-N-octadecyl-1,8-naphthalimide and serum albumins: Investigation by spectroscopic approach

    International Nuclear Information System (INIS)

    Sun Yang; Wei Song; Zhao Yingyong; Hu Xiaoyun; Fan Jun

    2012-01-01

    A novel 4-(2-dimethylaminoethyloxy)-N-octadecyl-1,8-naphthalimide (DON) has been synthesized as a spectrofluorimetric probe for the determination of proteins. Photophysics of DON in different solvents has been delineated in this paper. Progressive redshift with polarity of solvents in emission and absorption spectra hints at intramolecular charge transfer. The interactions of DON with serum albumins (i.e., human serum albumin (HSA) and bovine serum albumin (BSA)) were studied by fluorescence and absorption spectroscopy. Fluorescence data revealed that the quenching of HSA/BSA by DON were static quenching and the DON–HSA/BSA complexes were formed. The binding constant (K b ) for HSA and was found to be 8.44×10 −4 and 60.26×10 −4 M −1 and the number of binding sites (n) were 1.00 and 1.40, respectively. The thermodynamic parameters, ΔH and ΔS, for the DON–HSA system was calculated to be −14.83 kJ mol −1 and 23.61 J mol −1 K −1 , indicating the hydrogen bonds and hydrophobic interactions were the dominant intermolecular force. ΔH and ΔS for the binding of DON with BSA was −60.08 kJ mol −1 and −90.7441 mol −1 K −1 , suggesting the hydrogen bonds and van der Waals force played the main role in the interaction. The results of displacement experiments showed that DON bound HSA/BSA occurred at the Trp-214 proximity, located in subdomain IIA of the serum albumin structure (the warfarin binding pocket). The effect of DON on the conformation of HSA was also analyzed by synchronous and three-dimensional fluorescence spectra. The fluorescence of DON could be quenched by HSA, based on which, a fluorometric method for the determination of microamount protein using DON in the medium of HCl−Tris buffer solution (pH=7.4) was developed. The linear range of the calibration curves was 0.1–10.0 μM for HSA, 0.1–11.2 μM for BSA and 0.2–9.7 μM for egg albumin (EA). The detection limit (3σ) for HSA was 1.12×10 −10 M, for BSA it was 0.92×10

  4. Serum protein binding displacement: theoretical analysis using a hypothetical radiopharmaceutical and experimental analysis with 123I-N-isopropyl-p-iodoamphetamine

    International Nuclear Information System (INIS)

    Kawai, Keiichi; Nishii, Ryuichi; Shikano, Naoto; Makino, Nobuo; Kuga, Noriyuki; Yoshimoto, Mitsuyoshi; Jinnouchi, Seishi; Nagamachi, Shigeki; Tamura, Shozo; Takamura, Norito

    2009-01-01

    Introduction: The binding of radiopharmaceutical to serum proteins is thought to be an important factor that restricts its excretion and accumulation in tissue. We calculated the effect of inhibitors of serum protein binding using a hypothetical radiopharmaceutical. In vitro experiments and protein binding inhibitor-loaded monkey scintigraphy were then conducted using 123 I-N-isopropyl-p-iodoamphetamine (IMP) as the radiopharmaceutical. Methods: Free fraction ratios of radiopharmaceutical were calculated with one radiopharmaceutical, two serum proteins and two specific inhibitors in the steady state at various serum protein concentrations. In vitro protein binding inhibition studies using human, rat and monkey sera were performed with site-selective displacers of specific binding sites: 400 μM 6-methoxy-2-naphthylacetic acid (6MNA; a major nabumeton metabolite) as a serum albumin Site II inhibitor and 400 μM erythromycin (ETC) as an α 1 -acid glycoprotein (AGP) site inhibitor. Scintigraphy with or without 6MNA loading of monkeys was performed. Results: The theoretical findings roughly corresponded to the experimental results. Approximately 75% of IMP bound to serum albumin Site II and AGP in the species examined. The free fraction of IMP (25.0±0.6% for human, 22.8±0.4% for monkey, 23.7±0.3% for rat) increased with loading of specific protein binding inhibitors (6MNA: 28.0±0.3% for human, 24.5±0.7% for monkey, 24.3±0.2% for rat; ETC: 26.3±0.4% for human, 29.5±1.1% for monkey, 26.0±0.7% for rat) and was serum protein concentration dependant based on the results of calculations. Simultaneous administration of 6MNA and ETC produced a higher free fraction ratio of IMP (31.9±1.0% for human, 34.6±0.4% for monkey, 27.0±0.3% for rat) than summation of the single administrations of 6MNA and ETC (domino effect) in human, rat and monkey sera. Rapid cerebral accumulation was observed with 6MNA loading in monkey scintigraphy. Conclusions: 6MNA appears to change

  5. Crystal structure analysis of human serum albumin complexed with sodium 4-phenylbutyrate

    Directory of Open Access Journals (Sweden)

    Akito Kawai

    2018-03-01

    Full Text Available Sodium 4-phenylbutyrate (PB is an orphan drug for the treatment of urea cycle disorders. It also inhibits the development of endoplasmic reticulum stress, the action of histone deacetylases and as a regulator of the hepatocanalicular transporter. PB is generally considered to have the potential for use in the treatment of the diseases such as cancer, neurodegenerative diseases and metabolic diseases. In a previous study, we reported that PB is primarily bound to human serum albumin (HSA in plasma and its binding site is drug site 2. However, details of the binding mode of PB to HSA remain unknown. To address this issue, we examined the crystal structure of HSA with PB bound to it. The structure of the HSA–PB complex indicates that the binding mode of PB to HSA is quite similar to that for octanoate or drugs that bind to drug site 2, as opposed to that for other medium-chain length of fatty acids. These findings provide useful basic information related to drug–HSA interactions. Moreover, the information presented herein is valuable in terms of providing safe and efficient treatment and diagnosis in clinical settings. Keywords: Human serum albumin, X-ray crystallography, Sodium 4-phenylbutyrate, Drug interaction, Drug site 2

  6. Investigation of Non-Covalent Interactions of Aflatoxins (B1, B2, G1, G2, and M1 with Serum Albumin

    Directory of Open Access Journals (Sweden)

    Miklós Poór

    2017-10-01

    Full Text Available Aflatoxins are widely spread mycotoxins produced mainly by Aspergillus species. Consumption of aflatoxin-contaminated foods and drinks causes serious health risks for people worldwide. It is well-known that the reactive epoxide metabolite of aflatoxin B1 (AFB1 forms covalent adducts with serum albumin. However, non-covalent interactions of aflatoxins with human serum albumin (HSA are poorly characterized. Thus, in this study the complex formation of aflatoxins was examined with HSA applying spectroscopic and molecular modelling studies. Our results demonstrate that aflatoxins form stable complexes with HSA as reflected by binding constants between 2.1 × 104 and 4.5 × 104 dm3/mol. A binding free energy value of −26.90 kJ mol−1 suggests a spontaneous binding process between AFB1 and HSA at room-temperature, while the positive entropy change of 55.1 JK−1 mol−1 indicates a partial decomposition of the solvation shells of the interacting molecules. Modeling studies and investigations with site markers suggest that Sudlow’s Site I of subdomain IIA is the high affinity binding site of aflatoxins on HSA. Interaction of AFB1 with bovine, porcine, and rat serum albumins was also investigated. Similar stabilities of the examined AFB1-albumin complexes were observed suggesting the low species differences of the albumin-binding of aflatoxins.

  7. Thermometric enzyme linked immunosorbent assay in continuous flow system: optimization and evaluation using human serum albumin as a model system.

    Science.gov (United States)

    Borrebaeck, C; Börjeson, J; Mattiasson, B

    1978-06-15

    Thermometric enzyme-linked immunosorbent assay (TELISA) is described. After the procedure of optimization, human serum albumin was assayed using anti-human serum albumin bound to Sepharose CL 4-B in the enzyme thermistor unit and catalase as label on the free antigen. The model system was used for assays down to 10(-13)M and the preparation of immobilized antibodies was used repeatedly up to 100 times. Comparative studies of the TELISA technique with bromocresol green, immunoturbidimetric and rocket immunoelectrophoretic methods were carried out and showed that TELISA could be used as an alternative method.

  8. Neurokinin B and serum albumin limit copper binding to mammalian gonadotropin releasing hormone.

    Science.gov (United States)

    Gul, Ahmad Samir; Tran, Kevin K; Jones, Christopher E

    2018-02-26

    Gonadotropin releasing hormone (GnRH) triggers secretion of luteinizing hormone and follicle stimulating hormone from gonadotropic cells in the anterior pituitary gland. GnRH is able to bind copper, and both in vitro and in vivo studies have suggested that the copper-GnRH complex is more potent at triggering gonadotropin release than GnRH alone. However, it remains unclear whether copper-GnRH is the active species in vivo. To explore this we have estimated the GnRH-copper affinity and have examined whether GnRH remains copper-bound in the presence of serum albumin and the neuropeptide neurokinin B, both copper-binding proteins that GnRH will encounter in vivo. We show that GnRH has a copper dissociation constant of ∼0.9 × 10 -9  M, however serum albumin and neurokinin B can extract metal from the copper-GnRH complex. It is therefore unlikely that a copper-GnRH complex will survive transit through the pituitary portal circulation and that any effect of copper must occur outside the bloodstream in the absence of neurokinin B. Copyright © 2018 Elsevier Inc. All rights reserved.

  9. Serum albumin and total lymphocyte count as predictors of outcome in hip fractures.

    LENUS (Irish Health Repository)

    O'Daly, Brendan J

    2012-02-01

    BACKGROUND & AIMS: Hip fractures are a significant cause of mortality and morbidity in the elderly. Malnutrition is a significant contributor to this, however no consensus exists as to the detection or management of this condition. We hypothesise that results of admission serum albumin and total lymphocyte count (TLC), as markers of Protein Energy Malnutrition (PEM) can help predict clinical outcome in hip fracture patients aged over 60 years. METHODS: This retrospective study evaluated the nutritional status of patients with hip fractures using albumin and TLC assays and analysed their prognostic relevance. Clinical outcome parameters studied were delay to operation, duration of in-patient stay, re-admission and in-patient, 3- and 12-month mortality. RESULTS: Four hundred and fifteen hip fracture patients were evaluated. Survival data were available for 377 patients at 12 months. In-hospital mortality for PEM patients was 9.8%, compared with 0% for patients without. Patients with PEM had a higher 12-month mortality compared to patients who had normal values of both laboratory parameters (Odds Ratio 4.6; 95% CI: 1.0-21.3). Serum albumin (Hazard Ratio 0.932, 95% CI: 0.9-1.0) and age (Hazard Ratio 1.04, 95% CI: 1.0-1.1) were found to be significant independent prognostic factors of mortality by Cox regression analysis. CONCLUSIONS: These results highlight the relevance of assessing the nutritional status of patients with hip fractures at the time of admission and emphasises the correlation between PEM and outcome in these patients.

  10. Contribution to the study of plasmatic fibrinogen and serum albumin: effects of irradiation

    International Nuclear Information System (INIS)

    Suscillon, M.

    1967-01-01

    The author studies the modifications of properties and structure of serum albumin and fibrinogen solution when subjected to radiation of low energy (X rays). On the other hand, two original techniques are exposed: 1. Amperometric determination of fibrin stabilizing factor or factor XIII of hemostasis. 2. Spectrophotometric study of fibrin formation kinetics. Then showing off and quantitative determination of platelets fibrinogen is exposed. (author) [fr

  11. Forster resonance energy transfer in the system of human serum albumin-xanthene dyes

    Science.gov (United States)

    Kochubey, V. I.; Pravdin, A. B.; Melnikov, A. G.; Konstantinova, I.; Alonova, I. V.

    2016-04-01

    The processes of interaction of fluorescent probes: eosin and erythrosine with human serum albumin (HSA) were studied by the methods of absorption and fluorescence spectroscopy. Extinction coefficients of probes were determined. Critical transfer radius and the energy transfer efficiency were defined by fluorescence quenching of HSA. Analysis of the excitation spectra of HSA revealed that the energy transfer process is carried out mainly between tryptophanyl and probes.

  12. Albumin modification and fragmentation in renal disease.

    Science.gov (United States)

    Donadio, Carlo; Tognotti, Danika; Donadio, Elena

    2012-02-18

    Albumin is the most important antioxidant substance in plasma and performs many physiological functions. Furthermore, albumin is the major carrier of endogenous molecules and exogenous ligands. This paper reviews the importance of post-translational modifications of albumin and fragments thereof in patients with renal disease. First, current views and controversies on renal handling of proteins, mainly albumin, will be discussed. Post-translational modifications, namely the fragmentation of albumin found with proteomic techniques in nephrotic patients, diabetics, and ESRD patients will be presented and discussed. It is reasonable to hypothesize that proteolytic fragmentation of serum albumin is due to a higher susceptibility to proteases, induced by oxidative stress. The clinical relevance of the fragmentation of albumin has not yet been established. These modifications could affect some physiological functions of albumin and have a patho-physiological role in uremic syndrome. Proteomic analysis of serum allows the identification of over-expressed proteins and can detect post-translational modifications of serum proteins, hitherto hidden, using standard laboratory techniques. Copyright © 2011 Elsevier B.V. All rights reserved.

  13. Characterization of the complex between native and reduced bovine serum albumin with aquacobalamin and evidence of dual tetrapyrrole binding.

    Science.gov (United States)

    Dereven'kov, Ilia A; Hannibal, Luciana; Makarov, Sergei V; Makarova, Anna S; Molodtsov, Pavel A; Koifman, Oskar I

    2018-05-02

    Serum albumin binds to a variety of endogenous ligands and drugs. Human serum albumin (HSA) binds to heme via hydrophobic interactions and axial coordination of the iron center by protein residue Tyr161. Human serum albumin binds to another tetrapyrrole, cobalamin (Cbl), but the structural and functional properties of this complex are poorly understood. Herein, we investigate the reaction between aquacobalamin (H 2 OCbl) and bovine serum albumin (BSA, the bovine counterpart of HSA) using Ultraviolet-Visible and fluorescent spectroscopy, and electron paramagnetic resonance. The reaction between H 2 OCbl and BSA led to the formation of a BSA-Cbl(III) complex consistent with N-axial ligation (amino). Prior to the formation of this complex, the reactants participate in an additional binding event that has been examined by fluorescence spectroscopy. Binding of BSA to Cbl(III) reduced complex formation between the bound cobalamin and free cyanide to form cyanocobalamin (CNCbl), suggesting that the β-axial position of the cobalamin may be occupied by an amino acid residue from the protein. Reaction of BSA containing reduced disulfide bonds with H 2 OCbl produces cob(II)alamin and disulfide with intermediate formation of thiolate Cbl(III)-BSA complex and its decomposition. Finally, in vitro studies showed that cobalamin binds to BSA only in the presence of an excess of protein, which is in contrast to heme binding to BSA that involves a 1:1 stoichiometry. In vitro formation of BSA-Cbl(III) complex does not preclude subsequent heme binding, which occurs without displacement of H 2 OCbl bound to BSA. These data suggest that the two tetrapyrroles interact with BSA in different binding pockets.

  14. Effect of Garlic on Perfusion Scintigraphy of Rabbit's Lungs ...

    African Journals Online (AJOL)

    Purpose: To study of the effect of garlic on rabbit's lungs, with the aid of perfusion scintigraphy, after experimentally-induced pulmonary embolism. Methods: Twelve adult rabbits were anesthetized. Prepared macroaggregated albumin- technetium 99m (99mTc-MAA) radiopharmaceutical was injected into the ear vein at a ...

  15. Albumin Redhill (-1 Arg, 320 Ala → Thr): A glycoprotein variant of human serum albumin whose precursor has an aberrant signal peptidase cleavage site

    International Nuclear Information System (INIS)

    Brennan, S.O.; Myles, T.; Peach, R.J.; George, P.M.; Donaldson, D.

    1990-01-01

    Albumin Redhill is an electrophoretically slow genetic variant of human serum albumin that does not bind 63 Ni 2+ and has a molecular mass 2.5 kDa higher than normal albumin. Its inability to bind Ni 2+ was explained by the finding of an additional residue of Arg at position -1. This did not explain the molecular basis of the genetic variation or the increase in apparent molecular mass. Fractionation of tryptic digests on concanavalin A-Sepharose followed by peptide mapping of the bound and unbound fractions and sequence analysis of the glycopeptides identified a mutation of 320 Ala → Thr. This introduces as Asn-Tyr-Thr oligosaccharide attachment sequence centered on Asn-318 and explains the increase in molecular mass. This, however, did not satisfactorily explain the presence of the additional Arg residue at position -1. DNA sequencing of polymerase chain reaction-amplified genomic DNA encoding the prepro sequence of albumin indicated an additional mutation of -2 Arg → Cys. The authors propose that the new Phe-Cys-Arg sequence in the propeptide is an aberrant signal peptidase cleavage site and that the signal peptidase cleaves the propeptide of albumin Redhill in the lumen of the endoplasmic reticulum before it reaches the Golgi vesicles, the site of the diarginyl-specific proalbumin convertase

  16. [Binding interaction of harpagoside and bovine serum albumin: spectroscopic methodologies and molecular docking].

    Science.gov (United States)

    Cao, Tuan-Wu; Huang, Wen-Bing; Shi, Jian-Wei; He, Wei

    2018-03-01

    Scrophularia ningpoensis has exhibited a variety of biological activities and been used as a pharmaceutical product for the treatment of inflammatory ailment, rheumatoid arthritis, osteoarthritis and so on. Harpagoside (HAR) is considerer as a main bioactive compound in this plant. Serum albumin has important physiological roles in transportation, distribution and metabolism of many endogenous and exogenous substances in body. It is of great significance to study the interaction mechanism between HAR and bovine serum albumin (BSA). The mechanism of interaction between HAR and BSA was investigated using 2D and 3D fluorescence, synchronous florescence, ultraviolet spectroscopy and molecular docking. According to the analysis of fluorescence spectra, HAR could strongly quench the fluorescence of BSA, and the static quenching process indicated that the decrease in the quenching constant was observed with the increase in temperature. The magnitude of binding constants (KA) was more than 1×10⁵ L·mol⁻¹, and the number of binding sites(n) was approximate to 1. The thermodynamic parameters were calculated through analysis of fluorescence data with Stern-Volmer and Van't Hoff equation. The calculated enthalpy change (ΔH) and entropy change (ΔS) implied that the main interaction forces of HAR with BSA were the bonding interaction between van der Waals forces and hydrogen. The negative values of energy (ΔG) demonstrated that the binding of HAR with BSA was a spontaneous and exothermic process. The binding distance(r) between HAR and BSA was calculated to be about 2.80 nm based on the theory of Frster's non-radiation energy transfer, which indicated that energy is likely to be transfer from BSA to HAR. Both synchronous and 3D florescence spectroscopy clearly revealed that the microenvironment and conformation of BSA changed during the binding interaction between HAR and BSA. The molecular docking analysis revealed HAR is more inclined to BSA and human serum albumin

  17. Differential sensing using proteins: exploiting the cross-reactivity of serum albumin to pattern individual terpenes and terpenes in perfume.

    Science.gov (United States)

    Adams, Michelle M; Anslyn, Eric V

    2009-12-02

    There has been a growing interest in the use of differential sensing for analyte classification. In an effort to mimic the mammalian senses of taste and smell, which utilize protein-based receptors, we have introduced serum albumins as nonselective receptors for recognition of small hydrophobic molecules. Herein, we employ a sensing ensemble consisting of serum albumins, a hydrophobic fluorescent indicator (PRODAN), and a hydrophobic additive (deoxycholate) to detect terpenes. With the aid of linear discriminant analysis, we successfully applied our system to differentiate five terpenes. We then extended our terpene analysis and utilized our sensing ensemble for terpene discrimination within the complex mixtures found in perfume.

  18. Lung inhalation scintigraphy with radioactive aerosols in several pulmonary diseases

    International Nuclear Information System (INIS)

    Martins, L.R.; Marioni Filho, H.; Romaldini, H.; Uehara, C.; Alonso, G.

    1983-01-01

    The pulmonary ventilation scintigraphy with 99m Tc diethylene-triamine-pentaacetate (99mTc-DTPA) delivered through a new nebulizer system when analyzed together with the classic lung perfusion scintigraphy with 99mTc-labeled albumin macroaggregates (99mTcMAA) is a very important diagnostic tool in several pulmonary diseases. Several aspects of the lung ventilation-perfusion scintigraphy are studied in 15 people with no lung disease, smokers and nonsmokers. The findings with the lung ventilation-perfusion scintigraphy are also discussed in 34 patients with several pulmonary diseases: lung cancer, chronic obstructive lung disease, policystic pulmonary disease, and pulmonary embolims. The authors concluded that the procedure is a valuable diagnostic tool in several pulmonary diseases, especially because good lung images are obtained, no side effects were detected, the technique is ease and low cost, and it brings new informations, not available with other diagnostic methods. (author)

  19. A model based on spectrofluorimetry to study the interaction between glyphosate and serum albumin of Salminus brasiliensis

    Science.gov (United States)

    Escobar, Marta Araujo Cyrino; Cortez, Celia Martins; Silva, Dilson; Neto, Jayme da Cunha Bastos

    2017-11-01

    The aim of this work is to initiate an investigation on the albumin of Salminus brasiliensis (gold fish) as a biomarker of environmental actions of glyphosate. We started using a mathematical-computational model based on spectrofluorimetric measurements to study the interaction of glyphosate with gold fish albumin and human serum albumin. Salminus brasiliensis is a migratory freshwater fish species found in southern and central-western Brazil, mainly in the Prata river basin, where most of soybean plantations are set. Glyphosate is a very used herbicide in this type of crop. Differently from the organophosphorate methyl parathion, glyphosate does not form complex with HSA, and the quenching constants estimated for its binding with gold fish albumin at 20 °C and 25 °C is 1.3(± 0.3) × 104 / M e 2.5 (± 0.3) × 104 / M, respectively.

  20. Synthesis and characterisation of 8-hydroxyquinoline-bovine serum albumin conjugates as metal ion chelating proteins

    International Nuclear Information System (INIS)

    Giraudi, G.; Baggiani, C.; Giovannoli, C.; Marletto, C.; Vanni, A.

    1999-01-01

    A derivative of 8-hydroxyquinoline (8-quinolinol, oxine) with a linking bridge containing a carboxylic group was covalently coupled to bovine serum albumin by the N-hydroxysuccinimide method to obtain stable monomeric conjugates with oxine to protein mole ratios up to 37. These conjugates were characterised spectrophotometrically and their complexation properties were confirmed by spectral analysis with and without the addition of Al(III), Cd(II), Co(II), Cu(II), Hg(II), Mn(II), Ni(II), Pb(II), V(IV), U(VI) and Zn(II) ions added. The maximum number of ions bound by these chelating proteins was determined spectrophotometrically by titration with metal ions at pH 6.0. The conjugates with a substitution ratio (moles of 8-hydroxyquinoline bound/mole of albumin) less than about 8 showed 1:1 binding with metal ions, while conjugates with higher substitution ratios were able to complex with 2:1 ratio of 8-hydroxyquinoline to metal ion. Association and dissociation kinetics of complexation with copper(II) ions showed a complex mechanism. The spectral and binding properties of these metal ion-binding proteins confirm that the coupling of the 8-hydroxyquinoline derivative to bovine serum albumin gives stable, water soluble, macromolecular chelating agents that retain the complexing ability of the original ligand. (Copyright (c) 1999 Elsevier Science B.V., Amsterdam. All rights reserved.)

  1. Carbonate radical anion-induced electron transfer in bovine serum albumin

    Energy Technology Data Exchange (ETDEWEB)

    Joshi, Ravi [Chemistry Group, Bhabha Atomic Research Centre, Mumbai 400 085 (India)]. E-mail: rjudrin@yahoo.com; Mukherjee, T. [Chemistry Group, Bhabha Atomic Research Centre, Mumbai 400 085 (India)

    2006-07-15

    Reaction of native and thermally denatured bovine serum albumin (BSA) with carbonate radical anion (CO{sub 3}{sup -} radical) has been studied using pulse radiolysis technique. Scavenging of CO{sub 3}{sup -} radical by native BSA and consequent electron transfer from tyrosine to tryptophan radical has been observed to occur with almost same rate constant (k{approx}1.7x10{sup 8} dm{sup 3} mol{sup -1} s{sup -1}) at pH 8.8. Effect of structural changes, due to thermal denaturation, on scavenging of CO{sub 3}{sup -} radical and the electron transfer process have been studied and discussed in this paper.

  2. Correlation of serum prostate specific antigen levels and Tc-99m mdp bone scintigraphy in newly diagnosed patients with prostrate cancer (abstract)

    International Nuclear Information System (INIS)

    Rauf, M.; Khan, S.M.; Khan, A.A.; Ahmad, S.; Knob, G.; Shah, S.; Khan, A.A.

    1998-01-01

    The aim of the study was to evaluate the correlation between serum prostate specific antigen (PSA) level and bone scintigraphy in newly diagnosed untreated prostate cancer patients. The probability of a positive bone scan for metastases was analyzed for different threshold values of prostate specific antigen (PSA), acid phosphastase and alkaline phosphates. Fifty four newly diagnosed untreated prostate cancer patients (mean age, 67 years range, 41 to 94) were included in this study. In each case serum PSA, acid phosphatase and alkaline phosphatase measurements were performed followed by whole body Technetium-99m MDP bone scan. The positive predictive value of serum PSA level for bone metastases at the threshold of 10 ng/ml was 70% whereas the same threshold level of PSA gave a negative predictive value of 100%. We used receiver operating characteristics (ROC) analysis to examine the power of predictive value of each serum test, in predicting the results of the bone scan. We also applied regression analysis for the assessment of correlation between the levels of tumor markers and the extent of bone pathology. It was concluded that bone scintigraphy seems to be unnecessary in evaluation of newly diagnosed untreated prostate cancer in patients with no clinical signs of bone pathology and serum PSA levels of equal to or less than 10 ng/ml. (author)

  3. Interactions of nanobubbles with bovine serum albumin and papain films on gold surfaces

    Czech Academy of Sciences Publication Activity Database

    Kolivoška, Viliam; Gál, Miroslav; Hromadová, Magdaléna; Lachmanová, Štěpánka; Pospíšil, Lubomír

    2011-01-01

    Roč. 6, č. 4 (2011), s. 164-170 ISSN 1559-4106 R&D Projects: GA ČR GP203/09/P502; GA ČR GA203/09/0705; GA ČR GA203/08/1157; GA AV ČR IAA400400802 Institutional research plan: CEZ:AV0Z40400503 Keywords : nanobubbles * bovine serum albumin * gold surfaces Subject RIV: CG - Electrochemistry Impact factor: 3.118, year: 2010

  4. Application of silver films with different roughness parameter for septic human serum albumin detection by Surface Enhanced Raman Spectroscopy

    Science.gov (United States)

    Zyubin, A. Y.; Konstantinova, E. I.; Matveeva, K. I.; Slezhkin, V. A.; Samusev, I. G.; Demin, M. V.; Bryukhanov, V. V.

    2018-01-01

    In this paper, the rough silver films parameters investigation, used as media for surface enhancement Raman spectroscopy for health and septic human serum albumin (HSA) study results have been presented. The detection of small concentrations of HSA isolated from blood serum and it main vibrational groups identification has been done.

  5. Study on the conformal variations of bovine and human serum albumin in solution using small angle X-ray scattering

    International Nuclear Information System (INIS)

    Olivieri, Johnny Rizzieri.

    1992-01-01

    It is reported a Small Angle X-Ray Scattering (SAXS) study of BSA (Bovine Serum Albumin) and HSA (Human Serum Albumin) on pH between 2.5 and 7.0. The measured scattering intensities, normalized in relation to incident beam, exposition time and scattering due to solvent and capillary, and corrected due to concentration and beam shape effects, have shown a strong dependence of the protein shape with pH for both albumins. It was found that the radius of gyration varies between 26.7 and 35 A, and the analyses of the distance distribution function. P(r), indicated that these proteins undergoes conformational changes with pH. Different theoretical shapes have been proposed and analysed comparing the computed P(r) function generated from the models with the experimental P(r). A large variety of shapes were found in both proteins, indicating that BSA and HSA are very flexibility macromolecules. (author). 60 refs., 49 figs., 7 tabs

  6. Amino acid substitutions in genetic variants of human serum albumin and in sequences inferred from molecular cloning

    International Nuclear Information System (INIS)

    Takahashi, N.; Takahashi, Y.; Blumberg, B.S.; Putnam, F.W.

    1987-01-01

    The structural changes in four genetic variants of human serum albumin were analyzed by tandem high-pressure liquid chromatography (HPLC) of the tryptic peptides, HPLC mapping and isoelectric focusing of the CNBr fragments, and amino acid sequence analysis of the purified peptides. Lysine-372 of normal (common) albumin A was changed to glutamic acid both in albumin Naskapi, a widespread polymorphic variant of North American Indians, and in albumin Mersin found in Eti Turks. The two variants also exhibited anomalous migration in NaDodSO 4 /PAGE, which is attributed to a conformational change. The identity of albumins Naskapi and Mersin may have originated through descent from a common mid-Asiatic founder of the two migrating ethnic groups, or it may represent identical but independent mutations of the albumin gene. In albumin Adana, from Eti Turks, the substitution site was not identified but was localized to the region from positions 447 through 548. The substitution of aspartic acid-550 by glycine was found in albumin Mexico-2 from four individuals of the Pima tribe. Although only single-point substitutions have been found in these and in certain other genetic variants of human albumin, five differences exist in the amino acid sequences inferred from cDNA sequences by workers in three other laboratories. However, our results on albumin A and on 14 different genetic variants accord with the amino acid sequence of albumin deduced from the genomic sequence. The apparent amino acid substitutions inferred from comparison of individual cDNA sequences probably reflect artifacts in cloning or in cDNA sequence analysis rather than polymorphism of the coding sections of the albumin gene

  7. Comparison of serum prostate specific antigen levels and bone scintigraphy in patients with prostate carcinoma

    International Nuclear Information System (INIS)

    Bielickaite, J.; Zadeikaite, R.; Jurkiene, N. and others

    2003-01-01

    The aim of this study was to analyze the levels of serum prostate specific antigen in patients with and without bone metastases detected by means of bone scintigraphy and to determine the highest prostate specific antigen level in patients without bone metastases. The 50 patients consecutively diagnosed of prostate cancer between 1999 and 2001 in our institution made up the study population. Prostate specific antigen plasmatic levels were determined and bone scintigraphy was performed (whole body study after 99mTc-methyl-diphosphonate administration) in all the patients. In patients with positive bone scans (n=23), the mean prostate specific antigen level was 71.4±35.2 ng/ml and was significantly (p<0.00005) higher than in 14 patients with negative bone scans (mean prostate specific antigen level was 10.1±10.5 ng/ml). Suspicious lesions were found in 13 patients and their mean prostate specific antigen level was 8.5±7.7 ng/ml. Regarding prostate specific antigen levels, no statistically significant differences were found between patients with suspicious lessons and normal bone scans. The highest determined prostate specific antigen level in patients without bone metastases was 18 ng/ml. The bone scintigraphy should be performed in all patients with prostate specific antigen level above 18 ng/ml, but it is of limited value in patients with prostate specific antigen level below 18 ng/ml. (author)

  8. Hepatic Arterial Perfusion Scintigraphy with '99mTc-Macroaggregated Albumin in Hepatocellular Carcinoma

    International Nuclear Information System (INIS)

    Kim, Gang Deuk; Sohn, Kwang Joon; Min, Kyung Yoon; Kwon, Young Mi; Kim, Chang Guhn; Noh, Byung Suk; Won, Jong Jin

    1994-01-01

    Hepatic arterial perfusion scintigraphy with '9 9m Tc macroggregated albumin (HAPS) study was carried out in 16 patients with hepatocellular carcinoma (HCC) and in six patients without liver tumor to evaluate HAPS findings of hepatocellular carcinoma and use fullness of HAPS. HAPS with planar and SPECT study were performed in 22 patients after conventional hepatic or celiac arteriography. For HAPS study, 4 5 mCi of MAA mixed with 2 ml of saline was injected into proper hepatic artery or its distal branches at the rate of approximately 1 ml/sec. We analysed 21 HCCs over 2 cm in diameter(average diameter: 6.4 cm) and 17 of 21 HCCs were over 4 cm in diameter. CT, sonography and angiography were performed within two week in all 16 patients and liver scan was performed in 12 patients. Three different pattern of tumor perfusion were observed in 16 patients with HCC. 1) diffuse increased perfusion in 16 of 21(76%) 2) increased peripheral perfusion in 4 of 21(19%) 3) diffuse decreased perfusion in 1 of 21 (5%) Arteriovenous shunt indicated by lung uptake of MAA were observed in 9 of 16 (56% ). In contrast, angiography demonstrates arteriovenous shunt in 2 of 16 (13%). There was no accumulation of radioactivity on RRC blood pool scan in all six patients with HCC examined. HAPS is useful study in evaluation of perfusion pattern or vascularity of HCC and in detection of arteriovenous shunt.

  9. Application of photoactivation in the preparation of radiopharmaceuticals. Pt. 3. Human serum albumin labelled with technetium (99mTc)

    International Nuclear Information System (INIS)

    Komarek, P.; Kleisner, I.; Konopkova, M.; Komarkova, I.

    1997-01-01

    Human serum albumin was photoactivated with UV light at 254 nm and labelled with technetium ( 99m Tc) by reducing pertechnetate ( 99m Tc) with stannous chloride. Radiochemical purity was determined by using paper chromatography, columns and electrophoresis. The biodistribution of labelled albumin in rats was assessed by activity counting in isolated organs 15 and 60 minutes after administration. Photoactivation increases the number of free SH groups, which affect favourably the labelling efficiency. Irradiated albumin exhibits a higher labelling efficiency (99%) than non-irradiated albumin (96%). The structural changes depend on the UV radiation dose, concentration of irradiated substances, and metal ion content (Sn 2+ ). The results obtained suggest that the elimination from blood of albumin whose structure has been altered by photoactivation can be accelerated, thereby creating favourable conditions for its application in the diagnosis of inflammatory diseases. (author)

  10. Subnanosecond fluorescence spectroscopy of human serum albumin as a method to estimate the efficiency of the depression therapy

    Science.gov (United States)

    Syrejshchikova, T. I.; Gryzunov, Yu. A.; Smolina, N. V.; Komar, A. A.; Uzbekov, M. G.; Misionzhnik, E. J.; Maksimova, N. M.

    2010-05-01

    The efficiency of the therapy of psychiatric diseases is estimated using the fluorescence measurements of the conformational changes of human serum albumin in the course of medical treatment. The fluorescence decay curves of the CAPIDAN probe (N-carboxyphenylimide of the dimethylaminonaphthalic acid) in the blood serum are measured. The probe is specifically bound to the albumin drug binding sites and exhibits fluorescence as a reporter ligand. A variation in the conformation of the albumin molecule substantially affects the CAPIDAN fluorescence decay curve on the subnanosecond time scale. A subnanosecond pulsed laser or a Pico-Quant LED excitation source and a fast photon detector with a time resolution of about 50 ps are used for the kinetic measurements. The blood sera of ten patients suffering from depression and treated at the Institute of Psychiatry were preliminary clinically tested. Blood for analysis was taken from each patient prior to the treatment and on the third week of treatment. For ten patients, the analysis of the fluorescence decay curves of the probe in the blood serum using the three-exponential fitting shows that the difference between the amplitudes of the decay function corresponding to the long-lived (9 ns) fluorescence of the probe prior to and after the therapeutic procedure reliably differs from zero at a significance level of 1% ( p < 0.01).

  11. Interaction of tea polyphenols with serum albumins: A fluorescence spectroscopic analysis

    Energy Technology Data Exchange (ETDEWEB)

    Bose, Adity, E-mail: adityc17j@gmail.com

    2016-01-15

    Interactions of some tea polyphenols, namely (−) Catechin (C), (−)-epicatechin (EC), (–) epicatechin-3-gallate (ECG), (−)-epigallocatechin (EGC) and (−)-epigallocatechin-3-gallate (EGCG) are outlined with the serum albumin proteins. These interactions had all resulted in binding with the proteins with a concomitant static quenching of the protein fluorescence. A fluorescence technique has been considered as the tool to comprehend the polyphenol–protein interactions mainly and simultaneously other spectroscopic techniques used to verify the results have been discussed. In this mini review the different types of equations usually employed to calculate the binding constant values have been outlined, namely, modified Stern Volmer plot, Scatchard plot and Lineweaver Burk equation, with their corresponding results. The n values (number of binding sites) had always been close to unity suggesting a 1:1 complexation with the polyphenols and the protein. A structural change in the polyphenols has been found to alter the binding constant value and the galloyl moiety attached to the C ring of the polyphenols have been found to play a crucial role in this regard. It has been found that an increase in galloyl moiety increases binding of the catechins with proteins. - Highlights: • Review on interactions of some tea polyphenols with the serum albumin proteins. • Tea polyphenols include Catechin, epigallocatechin-3-gallate, epigallocatechin, epicatechin-3-gallate and epicatechin. • Fluorescence spectroscopic technique is mainly outlined. • Binding constant studies have been given importance. • Galloyl moiety in the C ring is crucial in increasing binding constant.

  12. Human serum albumin crystals and method of preparation

    Science.gov (United States)

    Carter, Daniel C. (Inventor)

    1989-01-01

    Human serum albumin (HSA) crystals are provided in the form of tetragonal plates having the space groups P42(sub 1)2, the crystals being grown to sizes in excess of 0.5 mm in two dimensions and a thickness of 0.1 mm. Growth of the crystals is carried out by a hanging drop method wherein a precipitant solution containing polyethylene glycol (PEG) and a phosphate buffer is mixed with an HSA solution, and a droplet of mixed solution is suspended over a well of precipitant solution. Crystals grow to the desired size in 3 to 7 days. Concentration of reagents, pH and other parameters are controlled within prescribed limits. The resulting crystals exhibit a size and quality such as to allow performance of x ray diffraction studies and enable the conduct of drug binding studies as well as genetic engineering studies.

  13. Verifying the competition between haloperidol and biperiden in serum albumin through a model based on spectrofluorimetry

    Science.gov (United States)

    Muniz da Silva Fragoso, Viviane; Patrícia de Morais e Coura, Carla; Paulino, Erica Tex; Valdez, Ethel Celene Narvaez; Silva, Dilson; Cortez, Celia Martins

    2017-11-01

    The aim of this work was to apply mathematical-computational modeling to study the interactions of haloperidol (HLP) and biperiden (BPD) with human (HSA) and bovine (BSA) serum albumin in order to verify the competition of these drugs for binding sites in HSA, using intrinsic tryptophan fluorescence quenching data. The association constants estimated for HPD-HSA was 2.17(±0.05) × 107 M-1, BPD-HSA was 2.01(±0.03) × 108 M-1 at 37 °C. Results have shown that drugs do not compete for the same binding sites in albumin.

  14. Zn2+ chelation by serum albumin improves hexameric Zn2+-insulin dissociation into monomers after exocytosis.

    Directory of Open Access Journals (Sweden)

    José A G Pertusa

    Full Text Available β-cells release hexameric Zn2+-insulin into the extracellular space, but monomeric Zn2+-free insulin appears to be the only biologically active form. The mechanisms implicated in dissociation of the hexamer remain unclear, but they seem to be Zn2+ concentration-dependent. In this study, we investigate the influence of albumin binding to Zn2+ on Zn2+-insulin dissociation into Zn2+-free insulin and its physiological, methodological and therapeutic relevance. Glucose and K+-induced insulin release were analyzed in isolated mouse islets by static incubation and perifusion experiments in the presence and absence of albumin and Zn2+ chelators. Insulin tolerance tests were performed in rats using different insulin solutions with and without Zn2+ and/or albumin. Albumin-free buffer does not alter quantification by RIA of Zn2+-free insulin but strongly affects RIA measurements of Zn2+-insulin. In contrast, accurate determination of Zn2+-insulin was obtained only when bovine serum albumin or Zn2+ chelators were present in the assay buffer solution. Albumin and Zn2+ chelators do not modify insulin release but do affect insulin determination. Preincubation with albumin or Zn2+ chelators promotes the conversion of "slow" Zn2+-insulin into "fast" insulin. Consequently, insulin diffusion from large islets is ameliorated in the presence of Zn2+ chelators. These observations support the notion that the Zn2+-binding properties of albumin improve the dissociation of Zn2+-insulin into subunits after exocytosis, which may be useful in insulin determination, insulin pharmacokinetic assays and islet transplantation.

  15. Study of Interaction between Cadmium and Bovine Serum Albumin with UV-Vis Spectrocopy Approach

    Science.gov (United States)

    Suhartono, E.; Thalib, I.; Aflanie, I.; Noor, Z.; Idroes, R.

    2018-05-01

    This study aims to explain the interaction of cadmium (Cd) with serum albumin through visible light (UV-Vis) spectroscopy approach. This study is an in vitro experimental study using Cd with several concentrations and Bovine Serum Albumin (BSA). Each solution was then incubated for 10 min at 37°C, and measured the absorbance at 220-300 nm. The absorbance data is then presented in graphical form. From the graph, a linear equation will appear to calculate the value of metal binding constants (K) to proteins. Also, in this present study we analsyed the ratio between A220 and A220 to identify changes in the protein region especially tyrosine and peptide bonds. The results show that the addition of Cd in different concentrations could increase the absorbance with a constant value (K) = 1.634. Based on the result, it seems the addition of Cd in different concentrations will lead the reaction to form BSA-Cd. Also, the result shows that the ration of A220/A280 were decreased with the increasing of Cd concentration. In conclusion, the addition of Cd could interact and changes the protein structure in BSA.

  16. The effect of paracetamol on 5 fluorouracil and bovine serum albumin interaction: A biophysical study

    Science.gov (United States)

    Dahiya, Vandana; Pal, Samanwita

    2018-05-01

    Serum Albumin is a major carrier protein and its binding with drugs is important to examine the change in pharmacokinetic properties due to interaction amongst drugs. In the present study we have attempted to understand the relevant drug-drug interaction (DDI) between two common drugs viz, paracetamol, an anti-inflammatory and fluorouracil, an anti-cancer drug. In-vitro spectroscopic methods viz., fluorescence quenching and UV-vis absorption have been employed for the drug-bovine serum albumin (BSA) complexes studies. The binding parameters and quenching constants have been determined for BSA-Paracetamol and BSA-5Fluorouracil complex according to literature models. It is also predicted from the quenching studies that BSA-5Fluorouracil is a stronger complex than BSA-Paracetamol. On the other hand paracetamol can alter binding affinity of 5Fluorouracil towards BSA. Hence it becomes clear that although the drugs could be administered simultaneously but they influence each other's binding with protein in a concentration dependent fashion. Further these results also indicate that availability of free 5Fluorouracil in blood may increase in presence of paracetamol.

  17. Clinical evaluation of hepatic scintigraphy using 99mTc-GSA

    International Nuclear Information System (INIS)

    Ishii, Katsumi; Nishiyama, Shogo; Nishimaki, Hiroshi; Tadokoro, Katsumi; Ikeda, Toshiaki; Matsubayashi, Takashi; Ishii, Kodo

    1992-01-01

    Functional hepatic imaging was performed using 99m Tc-DTPA-galactosyl human serum albumin ( 99m Tc-GSA), a radiolabeled ligand that reacts specifically to the asialoglycoprotein receptor that resides at the plasma membrane of hepatocytes, in 21 patients: five with chronic active hepatitis (CAH), 14 with compensative liver cirrhosis (LC), one with chronic inactive hepatitis and one with acute hepatitis. The former two diseases were mainly investigated. Serial liver images were acquired at the rates of 10 sec/frame for 0-5 min and 2 min/frame for 6-30 min after the injection of 99m Tc-GSA, and the images were compared with 99m Tc-phytase images in 2 patients with CAH and 11 with LC, and those with portal scintigrams using 123 I-iodoamphetamine (IMP) in 3 patients with LC. The images using 99m Tc-GSA were in better agreement with hepatic function than those using 99m Tc-phytase, and with the findings of portal scintigraphy using 123 I-IMP. LHL15 (liver/liver and heart radioactivities at 15 min after injection of 99m Tc-GSA) correlated with the hepaplastin test (r=0.978 in CAH, and r=0.544 in LC), indicators of hepatic reserve. These results suggest that liver scintigraphy using 99m Tc-GSA might be a useful method for evaluating liver function. (author)

  18. Layer-by-layer films from tartrazine dye with bovine serum albumin

    Science.gov (United States)

    de Souza, Nara C.; Flores, Júlio C. Johner; Silva, Josmary R.

    2009-12-01

    We report on the preparation and study of the adsorption process of layer-by-layer films of tartrazine alternated with bovine serum albumin. UV-Vis spectroscopy indicated that the films form J-aggregates of tartrazine. Adsorption kinetics was fitted by the Johnson-Mehl-Avrami equation and surface morphological analyses by atomic force microscopy suggested that the J-aggregates were column-shaped, which was attributed to the column-like symmetry of the tartrazine molecules. The columnar structures that formed probably arose from the juxtaposition of smaller aggregates that were already present at the beginning of film growth.

  19. A low-protein diet restricts albumin synthesis in nephrotic rats.

    OpenAIRE

    Kaysen, G A; Jones, H; Martin, V; Hutchison, F N

    1989-01-01

    High-protein diets increase albumin synthesis in rats with Heymann nephritis but albuminuria increases also, causing serum albumin concentration to be suppressed further than in nephrotic animals eating a low-protein diet. Experiments were designed to determine whether dietary protein augmentation directly stimulates albumin synthesis, or whether instead increased albumin synthesis is triggered by the decrease in serum albumin concentration. Evidence is presented that dietary protein augmenta...

  20. 21 CFR 862.1035 - Albumin test system.

    Science.gov (United States)

    2010-04-01

    ... 21 Food and Drugs 8 2010-04-01 2010-04-01 false Albumin test system. 862.1035 Section 862.1035....1035 Albumin test system. (a) Identification. An albumin test system is a device intended to measure the albumin concentration in serum and plasma. Albumin measurements are used in the diagnosis and...

  1. Radioaerosol inhalation lung scintigraphy in bronchial asthma

    International Nuclear Information System (INIS)

    Chiba, Takashi

    1993-01-01

    A study on obstructive changes in airways and mucociliary clearance in children and youth with bronchial asthma was performed. Radioaerosol inhalation lung scintigraphies using 99T c-human serum albumin (HSA) were applied to 50 children and youth with bronchial asthma. The deposition patterns of the radioaerosol and aerosol clearance curves were evaluated. Abnormal deposition patterns, which consisted of non-homogeneous distribution and/or hot spot formation, were likely to be seen in patients with asthmatic attacks at the time of measurements. However, a few asymptomatic patients also revealed abnormal deposition patterns. The deposition patterns were related to FEV 1.0 %, MMF, V 50 and V 25 , but especially to FEV 1.0 %. As an index of mucociliary clearance, β, the rate constant of the 99m Tc-HSA aerosol clearance curve, was introduced. β was significantly lower in patients with abnormal aerosol deposition patterns than in normal persons. β was also significantly lower in patients undergoing asthmatic attack at the time of the measurements than in asymptomatic patients. β correlated negatively with FEV 1.0 %, MMF, V 50 and V 25 , but especially with FEV 1.0 %. Although patients with long term affection or moderate-to-severe asthma tended to reveal abnormal deposition patterns and had low β values, these differences were not statistically significant. Radioaerosol inhalation lung scintigraphy with 99m Tc-HSA is useful for evaluating not only obstructive changes in the airways but also for evaluating mucociliary clearance in children with bronchial asthma. (author)

  2. A note on the electrolytic preparation of sup(99m)Tc human serum albumin

    International Nuclear Information System (INIS)

    Ligny, C.L. de; Dekker, B.G.

    1978-01-01

    A note to the simple electrolytic preparations of Tc-99m human serum albumin using tin electrodes, elaborated by Narasimhan and Mani, is described. Narasimhan and Mani's procedure yields mainly hydrolysed reduced Tc. Gil et al described a modification of Narasimhan and Mani's procedure wherein about 60% Tc-HSA chelate can be obtained. Purity analysis was performed by paper chromatography with 85% methanol as eluent. (T.I.)

  3. Fatty acid and drug binding to a low-affinity component of human serum albumin, purified by affinity chromatography

    DEFF Research Database (Denmark)

    Vorum, H; Pedersen, A O; Honoré, B

    1992-01-01

    Binding equilibria for decanoate to a defatted, commercially available human serum albumin preparation were investigated by dialysis exchange rate determinations. The binding isotherm could not be fitted by the general binding equation. It was necessary to assume that the preparation was a mixture...... of two albumin components about 40% of the albumin having high affinity and about 60% having low affinity. By affinity chromatography we succeeded in purifying the low-affinity component from the mixture. The high-affinity component, however, could not be isolated. We further analyzed the fatty acid...... and drug binding abilities of the low-affinity component. The fatty acids decanoate, laurate, myristate and palmitate were bound with higher affinity to the mixture than to the low-affinity component. Diazepam was bound with nearly the same affinity to the low-affinity component as to the albumin mixture...

  4. A modified procedure for the labelling of human serum albumin microspheres with 99m Tc for lung scanning

    International Nuclear Information System (INIS)

    El-Kolaly, M.T.; Amin, A.; Raieh, M.; El-Mohty, A.

    1996-01-01

    A modified procedure is reported for the labelling of human serum albumin microspheres (HSAM) with 99m Tc. Albumin microspheres were first soaked in Sn-methylene diphosphonate (Sn-MDP) solution, then heated in a boiling water both for 10-15 minutes. The Sn-MDP coated HSAM were washed twice with saline containing poly sorbate-80 to remove the excess Sn-MDP solution. The coated albumin microspheres were then labelled with 99m Tc. More than 95% labelling yield are achieved by using the following quantities: 10 mg dry albumin microspheres, 5 mg MDP, 0.05 mg Sn Cl 2 .2 H 2 O, 0.1 mg ascorbic acid. The biological distribution of the labelled microspheres in mice has been studied and more than 85% lung uptake is achieved after 10 min of injection and the lung/liver ratio was 62. 8 tabs

  5. Brain Tumour Scintigraphy with {sup 99m}Tc-Pertechnetate, {sup 99m}Tc-Fe(II) Complex and {sup 131}I-Labelled Macroaggregated Albumin - Comparison of Results; La Scintigraphie des Tumeurs Cerebrales a l'Aide de Pertechnetate Marque au {sup 99m}Tc, de Complexe {sup 99m}Tc-Fe-II et de Macroagregats d'Albumine Marques au {sup 131}I. Comparaison des Resultats

    Energy Technology Data Exchange (ETDEWEB)

    Haas, J. P.; Dietz, H.; Schmidt, K. J.; Doerr, F.; Brod, K. H.; Wolf, R. [Institut de Radiologie Clinique et Clinique de Neurochirurgie, Universite de Mayence, Federal Republic of Germany (Germany)

    1969-05-15

    {sup 99m}Tc, in the form of pertechnetate, has now gained its place in brain scintigraphy. The present authors and many others have found its diagnostic value equal to that of substances labelled with mercury or iodine. Using {sup 99m}Tc-pertechnetate as the basis of their work, the authors attempted to extend isotopic diagnosis by two methods, namely: intra-arterial introduction of macroaggregated albumin; and intravenous injection of a new substance, the {sup 99m}Tc-Fe(II) complex. Following their publication in 1966 of the results obtained with the first method, the authors now present an account of their experiments carried out on over 100 patients with brain tumours. Compared with scintigraphy involving intravenous injection of {sup 99m}Tc-pertechnetate, this new method gives supplementary information which is often of considerable help in clinical neuroradiological diagnosis of these patients. The findings in a majority of cases were confirmed by operation or by autopsy. The method made it possible for the first time to use scintigraphy to visualize the arterial network of the brain. In view of the ease with which brain scintigraphy can be performed after intravenous injection, and also of our experience with the {sup 99m}Tc-Fe(II) complex in kidney scintigraphy and the evidence of a brief report in the United States literature, the authors decided to try out this substance in the detection of brain tumours. Their first results showed it to be incontestably superior to all others previously applied intravenously. It has the indubitable advantages of {sup 99m}Tc as regards the irradiation dose to the patient and gives an exceptionally precise delineation of the invasive cerebral processes due to a rapid fall in blood concentration. A combination of these two new scintigraphic methods would thus seem to open up new possibilities and greatly enhance the field of application of radioisotopes in the clinical study of brain diseases. The paper contains material

  6. Physicochemical Properties of Bovine Serum Albumin-Glucose and Bovine Serum Albumin-Mannose Conjugates Prepared by Pulsed Electric Fields Treatment

    Directory of Open Access Journals (Sweden)

    Wenjie Jian

    2018-03-01

    Full Text Available The pulsed electric fields (PEF treatment is a novel method for obtaining glycated proteins by way of a Maillard reaction between proteins and polysaccharides but its effect on the preparation of protein–monosaccharide conjugate has not been explored. This study aimed to prepare bovine serum albumin (BSA–glucose and BSA–mannose conjugates using PEF in pH 10.0 at an intensity of 10 or 20 kV/cm, frequency of 1 kHz, pulse width of 20 μs and 73.5 pulses. The conjugates were evaluated for physicochemical properties. The results indicated that PEF not only promoted Maillard reaction between BSA and glucose or mannose but also alleviated the undesirable browning. PEF treatment favored the increased surface hydrophobicity and emulsifying activity in BSA but reduced surface hydrophobicity and foaming stability and improved foaming capacity in BSA–glucose and BSA–mannose conjugates. These findings provided useful considerations in the application of PEF treatment as a potential method to prepare BSA–monosaccharide conjugates by Maillard reaction.

  7. Native and denatured bovine serum albumin. D.c. polarography, stripping voltammetry and constant current chronopotentiometry

    Czech Academy of Sciences Publication Activity Database

    Ostatná, Veronika; Uslu, B.; Dogan, B.; Ozkan, S.; Paleček, Emil

    2006-01-01

    Roč. 593, č. 1-2 (2006), s. 172-178 ISSN 0022-0728 R&D Projects: GA AV ČR(CZ) IAA500040513; GA MŠk(CZ) LC06035 Institutional research plan: CEZ:AV0Z50040507 Keywords : protein electrochemistry * bovine serum albumin * native and denatured proteins Subject RIV: BO - Biophysics Impact factor: 2.339, year: 2006

  8. Surface imprinted beads for the recognition of human serum albumin.

    Science.gov (United States)

    Bonini, Francesca; Piletsky, Sergey; Turner, Anthony P F; Speghini, Adolfo; Bossi, Alessandra

    2007-04-15

    The synthesis of poly-aminophenylboronic acid (ABPA) imprinted beads for the recognition of the protein human serum albumin (HSA) is reported. In order to create homogeneous recognition sites, covalent immobilisation of the template HSA was exploited. The resulting imprinted beads were selective for HSA. The indirect imprinting factor (IF) calculated from supernatant was 1.6 and the direct IF, evaluated from the protein recovered from the beads, was 1.9. The binding capacity was 1.4 mg/g, which is comparable to commercially available affinity materials. The specificity of the HSA recognition was evaluated with competitive experiments, indicating a molar ratio 4.5/1 of competitor was necessary to displace half of the bound HSA. The recognition and binding of the imprinted beads was also tested with a complex sample, human serum and targeted removal of HSA without a loss of the other protein components was demonstrated. The easy preparation protocol of derivatised beads and a good protein recognition properties make the approach an attractive solution to analytical and bio-analytical problems in the field of biotechnology.

  9. Data set for mass spectrometric analysis of recombinant human serum albumin from various expression systems

    Directory of Open Access Journals (Sweden)

    Daryl G.S. Smith

    2015-09-01

    Full Text Available Human serum albumin (HSA is a versatile and important protein for the pharmaceutical industry (Fanali et al., Mol. Aspects Med. 33(3 (2012 209–290. Due to the potential transmission of pathogens from plasma sourced albumin, numerous expression systems have been developed to produce recombinant HSA (rHSA (Chen et al., Biochim. Biophys. Acta (BBA—Gen. Subj. 1830(12 (2013 5515–5525; Kobayashi, Biologicals 34(1 (2006 55–59. Based on our previous study showing increased glycation of rHSA expressed in Asian rice (Frahm et al., J. Phys. Chem. B 116(15 (2012 4661–4670, both supplier-to-supplier and lot-to-lot variability of rHSAs from a number of expression systems were evaluated using reversed phase liquid chromatography linked with MS and MS/MS analyses. The data are associated with the research article ‘Determination of Supplier-to-Supplier and Lot-to-Lot Variability in Glycation of Recombinant Human Serum Albumin Expressed in Oryza sativa’ where further analysis of rHSA samples with additional biophysical methods can be found (Frahm et al., PLoS ONE 10(9 (2014 e109893. We determined that all rHSA samples expressed in rice showed elevated levels of arginine and lysine hexose glycation compared to rHSA expressed in yeast, suggesting that the extensive glycation of the recombinant proteins is a by-product of either the expression system or purification process and not a random occurrence.

  10. Identification and mapping of linear antibody epitopes in human serum albumin using high-density Peptide arrays.

    Directory of Open Access Journals (Sweden)

    Lajla Bruntse Hansen

    Full Text Available We have recently developed a high-density photolithographic, peptide array technology with a theoretical upper limit of 2 million different peptides per array of 2 cm(2. Here, we have used this to perform complete and exhaustive analyses of linear B cell epitopes of a medium sized protein target using human serum albumin (HSA as an example. All possible overlapping 15-mers from HSA were synthesized and probed with a commercially available polyclonal rabbit anti-HSA antibody preparation. To allow for identification of even the weakest epitopes and at the same time perform a detailed characterization of key residues involved in antibody binding, the array also included complete single substitution scans (i.e. including each of the 20 common amino acids at each position of each 15-mer peptide. As specificity controls, all possible 15-mer peptides from bovine serum albumin (BSA and from rabbit serum albumin (RSA were included as well. The resulting layout contained more than 200.000 peptide fields and could be synthesized in a single array on a microscope slide. More than 20 linear epitope candidates were identified and characterized at high resolution i.e. identifying which amino acids in which positions were needed, or not needed, for antibody interaction. As expected, moderate cross-reaction with some peptides in BSA was identified whereas no cross-reaction was observed with peptides from RSA. We conclude that high-density peptide microarrays are a very powerful methodology to identify and characterize linear antibody epitopes, and should advance detailed description of individual specificities at the single antibody level as well as serologic analysis at the proteome-wide level.

  11. Identification and mapping of linear antibody epitopes in human serum albumin using high-density Peptide arrays.

    Science.gov (United States)

    Hansen, Lajla Bruntse; Buus, Soren; Schafer-Nielsen, Claus

    2013-01-01

    We have recently developed a high-density photolithographic, peptide array technology with a theoretical upper limit of 2 million different peptides per array of 2 cm(2). Here, we have used this to perform complete and exhaustive analyses of linear B cell epitopes of a medium sized protein target using human serum albumin (HSA) as an example. All possible overlapping 15-mers from HSA were synthesized and probed with a commercially available polyclonal rabbit anti-HSA antibody preparation. To allow for identification of even the weakest epitopes and at the same time perform a detailed characterization of key residues involved in antibody binding, the array also included complete single substitution scans (i.e. including each of the 20 common amino acids) at each position of each 15-mer peptide. As specificity controls, all possible 15-mer peptides from bovine serum albumin (BSA) and from rabbit serum albumin (RSA) were included as well. The resulting layout contained more than 200.000 peptide fields and could be synthesized in a single array on a microscope slide. More than 20 linear epitope candidates were identified and characterized at high resolution i.e. identifying which amino acids in which positions were needed, or not needed, for antibody interaction. As expected, moderate cross-reaction with some peptides in BSA was identified whereas no cross-reaction was observed with peptides from RSA. We conclude that high-density peptide microarrays are a very powerful methodology to identify and characterize linear antibody epitopes, and should advance detailed description of individual specificities at the single antibody level as well as serologic analysis at the proteome-wide level.

  12. Fetuin-A/albumin-mineral complexes resembling serum calcium granules and putative nanobacteria: demonstration of a dual inhibition-seeding concept.

    Directory of Open Access Journals (Sweden)

    Cheng-Yeu Wu

    2009-11-01

    Full Text Available Serum-derived granulations and purported nanobacteria (NB are pleomorphic apatite structures shown to resemble calcium granules widely distributed in nature. They appear to be assembled through a dual inhibitory-seeding mechanism involving proteinaceous factors, as determined by protease (trypsin and chymotrypsin and heat inactivation studies. When inoculated into cell culture medium, the purified proteins fetuin-A and albumin fail to induce mineralization, but they will readily combine with exogenously added calcium and phosphate, even in submillimolar amounts, to form complexes that will undergo morphological transitions from nanoparticles to spindles, films, and aggregates. As a mineralization inhibitor, fetuin-A is much more potent than albumin, and it will only seed particles at higher mineral-to-protein concentrations. Both proteins display a bell-shaped, dose-dependent relationship, indicative of the same dual inhibitory-seeding mechanism seen with whole serum. As ascertained by both seeding experiments and gel electrophoresis, fetuin-A is not only more dominant but it appears to compete avidly for nanoparticle binding at the expense of albumin. The nanoparticles formed in the presence of fetuin-A are smaller than their albumin counterparts, and they have a greater tendency to display a multi-layered ring morphology. In comparison, the particles seeded by albumin appear mostly incomplete, with single walls. Chemically, spectroscopically, and morphologically, the protein-mineral particles resemble closely serum granules and NB. These particles are thus seen to undergo an amorphous to crystalline transformation, the kinetics and completeness of which depend on the protein-to-mineral ratios, with low ratios favoring faster conversion to crystals. Our results point to a dual inhibitory-seeding, de-repression model for the assembly of particles in supersaturated solutions like serum. The presence of proteins and other inhibitory factors tend

  13. Isolation of human anti-serum albumin Fab antibodies with an extended serum-half life.

    Science.gov (United States)

    Kang, Hyeon-Ju; Kim, Hye-Jin; Cha, Sang-Hoon

    2016-01-01

    The serum albumin (SA) has been exploited to generate long-acting biotherapeutics by taking advantage of the FcRn-mediated recycling mechanism in a direct or an indirect way. Since Fab fragments have been proven to be clinically safe for human usage, we assumed that human anti-SA Fab antibodies could have a great potential as a carrier molecule to extend the serum half-life of therapeutic proteins. We, herein, had attempted to isolate anti-SA Fab antibodies from HuDVFab-8L antibody library via a phage display technology, and identified eight discrete human Fab antibodies. One of the Fab antibodies, SL335, showed the strongest binding reactivity to human SA with nM range of affinity at both pH 6 and pH 7.4, and cross-reacted to SAs from various species including rat, mouse, canine and monkey. The in vivo pharmacokinetic assay using a rat model indicated that SL335 has approximately 10 fold longer serum half-life and 26 to 44-fold increase in AUC0 → ∞ compared to the negative control Fab molecule in both intravenous and subcutaneous administrations. Knowing that Fabs have proven to be safe in clinics for a long time, SL335 seems to have a great potential in generating long-acting protein drugs by tagging effector molecules with either chemical conjugation or genetic fusion. Copyright © 2015 Elsevier B.V. All rights reserved.

  14. Quantitation of species differences in albumin–ligand interactions for bovine, human and rat serum albumins using fluorescence spectroscopy: A test case with some Sudlow's site I ligands

    International Nuclear Information System (INIS)

    Poór, Miklós; Li, Yin; Matisz, Gergely; Kiss, László; Kunsági-Máté, Sándor; Kőszegi, Tamás

    2014-01-01

    Albumin, the most abundant plasma protein is an approximately 67 kDa sized water-soluble macromolecule. Since several drugs and xenobiotics circulate in the blood at least partially in albumin-bound form, albumin plays a key role in the pharmacokinetics/toxicokinetics of these chemicals. Most of the drugs and xenobiotics are Sudlow's site I ligands. In numerous studies, bovine serum albumin (BSA) is used for modeling albumin–ligand interactions and the results are extrapolated to human serum albumin (HSA). Furthermore, only limited information is available related to albumin–ligand interactions of different albumin species. Therefore, in our study, we have focused on the quantification of differences between bovine, human and rat serum albumin (RSA) using four Sudlow's site I ligands (luteolin, ochratoxin A, phenylbutazone and warfarin). Interactions were analyzed by fluorescence spectroscopy. Stability constants as well as competing capacities of the ligands were determined, and thermodynamic study was also performed. Our results highlight that there could be major differences between BSA, HSA and RSA in their ligand binding properties. Based on our observations we emphasize that in molecular aspects BSA behaves considerably differently from HSA or from albumins of other species therefore, it is strongly recommended to apply at least some confirmatory measurements when data obtained from other species are attempted to be extrapolated to HSA. -- Highlights: • Albumin–ligand interactions of human, bovine and rat albumins were studied. • Four Sudlow's site I ligands were tested by fluorescence spectroscopy. • Substantial differences were found in stability constants among albumin complexes. • Competing capacity of ligands showed major differences in the studied species. • Data obtained for BSA cannot be directly extrapolated to human albumin

  15. Binding of several anti-tumor drugs to bovine serum albumin: Fluorescence study

    Energy Technology Data Exchange (ETDEWEB)

    Bi Shuyun [College of Chemistry, Changchun Normal University, Changchun 130032 (China)], E-mail: sy_bi@sina.com; Sun Yantao [College of Chemistry, Jilin University, Changchun 130023 (China); College of Chemistry, Jilin Normal University, Siping 136000 (China); Qiao Chunyu; Zhang Hanqi [College of Chemistry, Jilin University, Changchun 130023 (China); Liu Chunming [College of Chemistry, Changchun Normal University, Changchun 130032 (China)

    2009-05-15

    The interactions of mitomycin C (MMC), fluorouracil (FU), mercaptopurine (MP) and doxorubicin hydrochloride (DXR) with bovine serum albumin (BSA) were studied by spectroscopic method. Quenching of fluorescence of serum albumin by these drugs was found to be a static quenching process. The binding constants (K{sub A}) were 9.66x10{sup 3}, 2.08x10{sup 3}, 8.20x10{sup 2} and 7.50x10{sup 3} L mol{sup -1} for MMC-, FU-, MP- and DXR-BSA, respectively, at pH 7.4 Britton-Robinson buffer at 28 deg. C. The thermodynamic functions such as enthalpy change ({delta}H), entropy change ({delta}S) and Gibbs free-energy change ({delta}G) for the reactions were also calculated according to the thermodynamic equations. The main forces in the interactions of these drugs with BSA were evaluated. It was found that the interactions of MMC and FU with BSA were exothermic processes and those of MP and DXR with BSA were endothermic. In addition, the binding sites on BSA for the four drugs were probed by the changes of binding properties of these drugs with BSA in the presence of two important site markers such as ibuprofen and indomethacin. Based on the Foester theory of non-radiation energy transfer, the binding distances between the drugs and tryptophane were calculated and they were 3.00, 1.14, 2.85, and 2.79 nm for MMC, FU, MP and DXR, respectively.

  16. Interaction studies of resistomycin from Streptomyces aurantiacus AAA5 with calf thymus DNA and bovine serum albumin

    Science.gov (United States)

    Vijayabharathi, R.; Sathyadevi, P.; Krishnamoorthy, P.; Senthilraja, D.; Brunthadevi, P.; Sathyabama, S.; Priyadarisini, V. Brindha

    2012-04-01

    Resistomycin, a secondary metabolite produced by Streptomyces aurantiacus AAA5. The binding interaction of resistomycin with calf thymus DNA (CT DNA) and bovine serum albumin (BSA) was investigated by spectrophotometry, spectrofluorimetry, circular dichroism (CD) and synchronous fluorescence techniques under physiological conditions in vitro. Absorption spectral studies along with the fluorescence competition with ethidium bromide measurements and circular dichroism clearly suggest that the resistomycin bind with CT DNA relatively strong via groove binding. BSA interaction results revealed that the drug was found to quench the fluorescence intensity of the protein through a static quenching mechanism. The number of binding sites 'n' and apparent binding constant 'K' calculated according to the Scatchard equation exhibit a good binding property to bovine serum albumin protein. In addition, the results observed from synchronous fluorescence measurements clearly demonstrate the occurrence of conformational changes of BSA upon addition of the test compound.

  17. Constrained Photophysics of 5,7-dimethoxy-2,3,4,9-tetrahydro-1H-carbazol-1-one in the Bioenvironment of Serum Albumins: A Spectroscopic Endeavour Supported by Molecular Docking Analysis.

    Science.gov (United States)

    Mitra, Amrit Krishna; Sau, Abhishek; Pal, Uttam; Saha, Chandan; Basu, Samita

    2017-07-01

    This paper vividly indicates that steady state as well as time-resolved fluorescence techniques can serve as highly sensitive monitors to explore the interactions of 5,7-dimethoxy-2,3,4,9-tetrahydro-1H-carbazol-1-one with model transport proteins, bovine serum albumin (BSA) and human serum albumin (HSA). Besides these, we have used fluorescence anisotropy study to assess the degree of restrictions imparted by the micro-environments of serum albumins. Again, to speculate the triplet excited state interaction between such fluorophore and albumin proteins (BSA& HSA), laser flash-photolysis experiments have been carried out. Molecular docking experiments have also been performed to support the conclusions obtained from steady state experiments.

  18. THE EFFECTS OF GLYCATION ON THE BINDING OF HUMAN SERUM ALBUMIN TO WARFARIN AND L-TRYPTOPHAN

    OpenAIRE

    Joseph, K.S.; Hage, David S.

    2010-01-01

    Diabetes leads to elevated levels of glucose in blood which, in turn, can lead to the non-enzymatic glycation of serum proteins such as human serum albumin (HSA). It has been suggested that this increase in glycation can alter the ability of HSA to bind to drugs and other small solutes. This study used high-performance affinity chromatography (HPAC) to see if there is any significant change related to glycation in the binding of HSA to warfarin and L-tryptophan, which are often used as probe ...

  19. Characterization of 6-mercaptopurine binding to bovine serum albumin and its displacement from the binding sites by quercetin and rutin

    Energy Technology Data Exchange (ETDEWEB)

    Ehteshami, Mehdi [Nutrition Research Center, School of Health and Nutrition, Tabriz University of Medical Sciences, Tabriz 51644-14766 (Iran, Islamic Republic of); Rasoulzadeh, Farzaneh [Drug Applied Research Center, Tabriz University of Medical Sciences, Tabriz 51644-14766 (Iran, Islamic Republic of); Mahboob, Soltanali [Nutrition Research Center, School of Health and Nutrition, Tabriz University of Medical Sciences, Tabriz 51644-14766 (Iran, Islamic Republic of); Rashidi, Mohammad-Reza, E-mail: rashidi@tbzmed.ac.ir [Research Center for Pharmaceutical Nanotechnology, Tabriz University of Medical Sciences, Tabriz 51644-14766 (Iran, Islamic Republic of)

    2013-03-15

    Binding of a drug to the serum albumins as major serum transport proteins can be influenced by other ligands leading to alteration of its pharmacological properties. In the present study, binding characteristics of 6-mercaptopurine (6-MP) with bovine serum albumin (BSA) together with its displacement from its binding site by quercetin and rutin have been investigated by the spectroscopic method. According to the binding parameters, a static quenching component in overall dynamic quenching process is operative in the interaction between 6-MP and BSA. The binding of 6-MP to BSA occurred spontaneously due to entropy-driven hydrophobic interactions. The synchronous fluorescence spectroscopy study revealed that the secondary structure of BSA is changed in the presence of 6-MP and both Tyr and Trp residues participate in the interaction between 6-MP and BSA with the later one being more dominant. The binding constant value of 6-MP-BSA in the presence of quercetin and rutin increased. 6-MP was displaced by ibuprofen indicating that the binding site of 6-MP on albumin is site II. Therefore, the change of the pharmacokinetic and pharmacodynamic properties of 6-MP by quercetin and rutin through alteration of binding capacity of 6-MP to the serum albumin cannot be ruled out. In addition, the displacement study showed that 6-MP is located in site II of BSA. - Highlights: Black-Right-Pointing-Pointer Participation of both Tyr and particularly Trp residues in the interaction between 6-MP and BSA. Black-Right-Pointing-Pointer Involvement of a static quenching component in an overall dynamic quenching process. Black-Right-Pointing-Pointer Ability of quercetin and rutin to change the binding constants of 6-MP-BSA complex. Black-Right-Pointing-Pointer Binding of 6-MP to BSA through entropy-driven hydrophobic interactions.

  20. Fluorescent analysis of interaction of flavonols with hemoglobin and bovine serum albumin

    Science.gov (United States)

    Sentchouk, V. V.; Bondaryuk, E. V.

    2007-09-01

    We have studied the fluorescent properties of flavonols (quercetin, fisetin, morin, rutin) with the aim of studying possible interaction with hemoglobin and bovine serum albumin (BSA). We observed an increase in the intensity of intrinsic fluorescence for all the flavonols except rutin in the presence of BSA. From the changes in the fluorescence spectra, we concluded that tautomeric forms are formed on interaction with hemoglobin. We determined the interconnection between the structure of related flavonols and their fluorescent properties on interaction with proteins, and we determined the binding constants for binding with BSA and hemoglobin.

  1. Cabazitaxel-loaded human serum albumin nanoparticles as a therapeutic agent against prostate cancer

    Directory of Open Access Journals (Sweden)

    Qu N

    2016-07-01

    Full Text Available Na Qu,1 Robert J Lee,1,2 Yating Sun,1 Guangsheng Cai,1 Junyang Wang,1 Mengqiao Wang,1 Jiahui Lu,1 Qingfan Meng,1 Lirong Teng,1 Di Wang,1 Lesheng Teng1,3 1School of Life Sciences, Jilin University, Changchun, People’s Republic of China; 2Division of Pharmaceutics, College of Pharmacy, The Ohio State University, Columbus, OH, USA; 3State Key Laboratory of Long-acting and Targeting Drug Delivery System, Yantai, People’s Republic of China Abstract: Cabazitaxel-loaded human serum albumin nanoparticles (Cbz-NPs were synthesized to overcome vehicle-related toxicity of current clinical formulation of the drug based on Tween-80 (Cbz-Tween. A salting-out method was used for NP synthesis that avoids the use of chlorinated organic solvent and is simpler compared to the methods based on emulsion-solvent evaporation. Cbz-NPs had a narrow particle size distribution, suitable drug loading content (4.9%, and superior blood biocompatibility based on in vitro hemolysis assay. Blood circulation, tumor uptake, and antitumor activity of Cbz-NPs were assessed in prostatic cancer xenograft-bearing nude mice. Cbz-NPs exhibited prolonged blood circulation and greater accumulation of Cbz in tumors along with reduced toxicity compared to Cbz-Tween. Moreover, hematoxylin and eosin histopathological staining of organs revealed consistent results. The levels of blood urea nitrogen and serum creatinine in drug-treated mice showed that Cbz-NPs were less toxic than Cbz-Tween to the kidneys. In conclusion, Cbz-NPs provide a promising therapeutic for prostate cancer. Keywords: cabazitaxel, human serum albumin, nanoparticle, drug delivery, toxicity, pros­tate cancer

  2. Association of malnutrition-inflammation score, dialysis-malnutrition score and serum albumin with novel risk factors for cardiovascular diseases in hemodialysis patients.

    Science.gov (United States)

    As'habi, Atefeh; Tabibi, Hadi; Hedayati, Mehdi; Mahdavi-Mazdeh, Mitra; Nozary-Heshmati, Behnaz

    2015-02-01

    This study was designed to investigate the associations between malnutrition-inflammation score (MIS), dialysis-malnutrition score (DMS) and serum albumin with novel risk factors for cardiovascular diseases (CVD) in hemodialysis (HD) patients. In this cross-sectional study, 291 HD patients were randomly selected from among 2302 adult HD patients in Tehran HD centers. The MIS and DMS were determined during one of the dialysis sessions in these patients. In addition, 4 mL blood was obtained before dialysis and analyzed for serum albumin and novel risk factors for CVD, including C-reactive protein (CRP), soluble intercellular adhesion molecule type 1 (sICAM-1), soluble vascular cell adhesion molecule type 1 (sVCAM-1), sE-selectin, malondialdehyde (MDA), nitric oxide (NO), endothelin-1 and lipoprotein (a) [Lp (a)]. MIS and DMS were significantly positively correlated with serum CRP (p protein-energy wasting indicators in HD patients are associated with serum CRP and sICAM-1, as two CVD risk factors.

  3. Competitive binding of Chlorin p6 and Dansyl-L-Proline to Sudlow's site II of human serum albumin

    Science.gov (United States)

    Patel, Sunita; Sharma, Kaushal Kishor; Datta, Anindya

    2015-03-01

    The binding of chlorin p6, a model photosensitizer for photodynamic therapy (PDT), to the Sudlow's site II of Human Serum Albumin (HSA) has been monitored by different spectroscopic methods. Displacement of Dansyl-L-Proline (DP) from its conjugate with HSA is manifested in the spectral shift and decrease in its fluorescence intensity as well as the emergence of component with lifetime of 2-3 ns, which is characteristic of free DP. As DP is known to bind specifically to the Sudlow's site II of human serum albumin, its displacement by chlorin p6 indicates the residence of the photosensitizer in the same site, in addition to Sudlow's site I. The binding constants for Sudlow's site II, determined by the stopped-flow technique, are found to be two orders of magnitude smaller than that for Sudlow's site I.

  4. Investigations into the oxygen effect during the radiolysis of serum albumin with the help of SDS-polyacrylamide gel electrophoresis

    International Nuclear Information System (INIS)

    Schilling, K.B.G.

    1984-01-01

    In this work the radiation induced structural changes of serum albumin were researched with the help of SDS-polyacrylamide gel electrophoresis. Cow serum albumin (bSA) at a concentration of 1 mg/ml was dissolved in a solution of 10 -2 M sodium phosphate buffer and in an air saturated solution with and without formiate (10 -1 M) and irradiated with 200 kV X-rays up to doses of 1500 Gy in a nitrogen atmosphere. The irradiation products were separated, with and without reduction, to 7.5 and 10% polyacrylamide gel, their molecular weights measured and the quantitative decrease of the monomeric serum albumin with increasing dose estimated using staining methods. With increasing dose in an air atmosphere the amount of bSA decreases, after reduction even more so, and at least 14 different protein fragments whose molecular weights were determined result from this. In the formiate-containing solution a bSA decrease of up to 20% was observed, but only in the reduced solutions. The nitrogen atmosphere during the irradiation resulted in protein aggregate formation (2, 3 and 4 times the molecular weight of the monomeric bSA). Changes in the protein size, structure, and net charge as reasons for the electrophoretic behavior are discussed as well as the importance of the primary radicals during the radiation chemical reactions. (orig./RB) [de

  5. Porphyrin mediated photo-modification of the structure and function of human serum albumin

    Science.gov (United States)

    Rozinek, Sarah C.

    Photosensitization reactions involve irradiating (with visible light) molecules with a high efficiency for either electron transfer or entering an excited triplet state (photosensitizer). Such reactions are applied to photodynamic cancer therapy, many medical laser-treatments, and a potential array of disinfection and pest elimination techniques. To understand the biophysical mechanisms of how these applications are effective at the protein level, the group of Dr. Brancaleon (UTSA) has investigated the irradiation of several dye-protein combinations, and discovered effects on protein structure and function. To further that work, we have investigated irradiation of the protein, human serum albumin (HSA), photosensitized by either protoporphyrin IX (PPIX) or meso-tetrakis(4-sulfonatophenyl)porphyrin (TSPP). HSA is the most abundant plasma protein, making it a likely substrate in PDT, and it possesses a specific binding pocket for iron-PPIX (heme) and possibly other porphyrin derivatives. The results of our research are summarized as follows. First, a thorough characterization of the binding of each photosensitizer to albumin was completed, elucidating a probable binding location for TSPP. Next, fluorescence lifetime emission of the single tryptophan residue, alongside circular dichroism, found tertiary structural changes around tryptophan and an overall 20% decrease in protein secondary structure after irradiation with TSPP bound. Finally, to determine if protein function was lost after photosensitization, size exclusion chromatography found modified albumin still recognizable by its receptor-protein, and comparative ex vivo up-take studies revealed that modified albumin is not processed the same way as native albumin in live tapeworm larva (Mesocestoides corti). Thus we found that visible light can induce partial unfolding of a protein by using a photo-activated ligand. These small structural modifications were sufficient to affect the protein's biological function.

  6. Probing the interaction of a new synthesized CdTe quantum dots with human serum albumin and bovine serum albumin by spectroscopic methods

    Energy Technology Data Exchange (ETDEWEB)

    Bardajee, Ghasem Rezanejade, E-mail: rezanejad@pnu.ac.ir; Hooshyar, Zari

    2016-05-01

    A novel CdTe quantum dots (QDs) were prepared in aqueous phase via a facile method. At first, poly (acrylic amide) grafted onto sodium alginate (PAAm-g-SA) were successfully synthesized and then TGA capped CdTe QDs (CdTe-TGA QDs) were embed into it. The prepared CdTe-PAAm-g-SA QDs were optimized and characterized by transmission electron microscopy (TEM), thermo-gravimetric (TG) analysis, Fourier transform infrared (FT-IR), UV–vis and fluorescence spectroscopy. The characterization results indicated that CdTe-TGA QDs, with particles size of 2.90 nm, were uniformly dispersed on the chains of PAAm-g-SA biopolymer. CdTe-PAAm-g-SA QDs also exhibited excellent UV–vis absorption and high fluorescence intensity. To explore biological behavior of CdTe-PAAm-g-SA QDs, the interactions between CdTe-PAAm-g-SA QDs and human serum albumin (HSA) (or bovine serum albumin (BSA)) were investigated by cyclic voltammetry, FT-IR, UV–vis, and fluorescence spectroscopic. The results confirmed the formation of CdTe-PAAm-g-SA QDs-HSA (or BSA) complex with high binding affinities. The thermodynamic parameters (ΔG < 0, ΔH < 0 and ΔS < 0) were indicated that binding reaction was spontaneous and van der Waals interactions and hydrogen-bond interactions played a major role in stabilizing the CdTe-PAAm-g-SA QDs-HSA (or BSA) complexes. The binding distance between CdTe-PAAm-g-SA QDs and HSA (or BSA)) was calculated about 1.37 nm and 1.27 nm, respectively, according to Forster non-radiative energy transfer theory (FRET). Analyzing FT-IR spectra showed that the formation of QDs-HSA and QDs-BSA complexes led to conformational changes of the HSA and BSA proteins. All these experimental results clarified the effective transportation and elimination of CdTe-PAAm-g-SA QDs in the body by binding to HSA and BSA, which could be a useful guideline for the estimation of QDs as a drug carrier. - Highlights: • The CdTe quantum dots coated with polyacrylamide grafted onto sodium alginate. • The

  7. Low serum albumin and total lymphocyte count as predictors of 30 day hospital readmission in patients 65 years of age or older

    Directory of Open Access Journals (Sweden)

    Robert Robinson

    2015-08-01

    Full Text Available Introduction. Hospital readmission within 30 days of discharge is a target for health care cost savings through the medicare Value Based Purchasing initiative. Because of this focus, hospitals and health systems are investing considerable resources into the identification of patients at risk of hospital readmission and designing interventions to reduce the rate of hospital readmission. Malnutrition is a known risk factor for hospital readmission.Materials and Methods. All medical patients 65 years of age or older discharged from Memorial Medical Center from January 1, 2012 to March 31, 2012 who had a determination of serum albumin level and total lymphocyte count on hospital admission were studied retrospectively. Admission serum albumin levels and total lymphocyte counts were used to classify the nutritional status of all patients in the study. Patients with a serum albumin less than 3.5 grams/dL and/or a TLC less than 1,500 cells per mm3 were classified as having protein energy malnutrition. The primary outcome investigated in this study was hospital readmission for any reason within 30 days of discharge.Results. The study population included 1,683 hospital discharges with an average age of 79 years. The majority of the patients were female (55.9% and had a DRG weight of 1.22 (0.68. 219 patients (13% were readmitted within 30 days of hospital discharge. Protein energy malnutrition was common in this population. Low albumin was found in 973 (58% patients and a low TLC was found in 1,152 (68% patients. Low albumin and low TLC was found in 709 (42% of patients. Kaplan–Meier analysis shows any laboratory evidence of PEM is a significant (p < 0.001 predictor of hospital readmission. Low serum albumin (p < 0.001 and TLC (p = 0.018 show similar trends. Cox proportional-hazards regression analysis showed low serum albumin (Hazard Ratio 3.27, 95% CI [2.30–4.63] and higher DRG weight (Hazard Ratio 1.19, 95% CI [1.03–1.38] to be significant

  8. 3-hydroxyflavone-bovine serum albumin interaction in Dextran medium

    Directory of Open Access Journals (Sweden)

    Voicescu Mariana

    2015-01-01

    Full Text Available Spectroscopic analysis of a bioactive flavonol, 3-Hydroxyflavone (3-HF, in systems based on Dextran 70 (Dx70 (an important bio-relevant polysacharide and Bovine Serum Albumin (BSA (a carrier protein, have been studied by fluorescence and circular dichroism. Changes produced by different concentrations of Dx70 on the fluorescent characteristics of 3-HF, and on the excited - state intramolecular proton transfer (ESIPT process were studied. The influence of 3-HF binding and of Dx70 on the secondary structure of BSA were investigated by circular dichroism spectroscopy. The influence of temperature (30-80°C range on the intrinsic Tryptophan fluorescence in 3-HF/BSA/Dx70 systems, was investigated. The results are discussed with relevance to 3-HF as a sensitive fluorescence probe for exploring flavone-protein interaction in plasma expander media and also for its biological evaluation.

  9. Structural studies on serum albumins under green light irradiation.

    Science.gov (United States)

    Comorosan, Sorin; Polosan, Silviu; Popescu, Irinel; Ionescu, Elena; Mitrica, Radu; Cristache, Ligia; State, Alina Elena

    2010-10-01

    This paper presents two new experimental results: the protective effect of green light (GL) on ultraviolet (UV) denaturation of proteins, and the effect of GL on protein macromolecular structures. The protective effect of GL was revealed on two serum albumins, bovine (BSA) and human (HSA), and recorded by electrophoresis, absorption, and circular dichroism spectra. The effect of GL irradiation on protein structure was recorded by using fluorescence spectroscopy and electrophoresis. These new effects were modeled by quantum-chemistry computation using Gaussian 03 W, leading to good fit between theoretical and experimental absorption and circular dichroism spectra. A mechanism for these phenomena is suggested, based on a double-photon absorption process. This nonlinear effect may lead to generation of long-lived Rydberg macromolecular systems, capable of long-range interactions. These newly suggested systems, with macroscopic quantum coherence behaviors, may block the UV denaturation processes.

  10. Evaluation of use of human albumin in critically ill dogs: 73 cases (2003-2006).

    Science.gov (United States)

    Trow, Amy V; Rozanski, Elizabeth A; Delaforcade, Armelle M; Chan, Daniel L

    2008-08-15

    To evaluate the use of human albumin in critically ill dogs. Design-Retrospective case series. 73 client-owned hospitalized dogs. Medical records of dogs that received human albumin were reviewed to assess effects of the use of human albumin on serum albumin concentration, colloid osmotic pressure, and total protein concentration; determine the relationships between these variables and outcome; and assess its safety. Data for signalment, diagnoses, physiologic variables, dosage, amount of crystalloid fluid administered prior to human albumin administration, complications, and outcome were reviewed. Additionally, pre- and postadministration values for serum albumin, colloid osmotic pressure, and total protein were recorded. Administration of human albumin resulted in significant changes in serum albumin, colloid osmotic pressure, and total protein. The serum albumin, total protein, degree of improvement in serum albumin, colloid osmotic pressure, and dosage of human albumin were significantly greater in survivors. Seventeen of 73 (23%) dogs had at least 1 complication that could be potentially associated with the administration of human albumin that occurred during or immediately following administration of human albumin. Three of 73 (4%) dogs had severe delayed complications. Administration of human albumin significantly increased serum albumin, and total protein concentrations and colloid osmotic pressure, especially in survivors. Because of the high mortality rate of the study population and other confounding factors, it was uncertain whether complications were associated with the underlying disease or with human albumin administration. Acute and delayed complications may have been under-recognized.

  11. Interactions of Poly(amidoamine) Dendrimers with Human Serum Albumin: Binding Constants and Mechanisms

    OpenAIRE

    Giri, Jyotsnendu; Diallo, Mamadou S.; Simpson, André J.; Liu, Yi; Goddard, William A., III; Kumar, Rajeev; Woods, Gwen C.

    2011-01-01

    The interactions of nanomaterials with plasma proteins have a significant impact on their in vivo transport and fate in biological fluids. This article discusses the binding of human serum albumin (HSA) to poly(amidoamine) [PAMAM] dendrimers. We use protein-coated silica particles to measure the HSA binding constants (K_b) of a homologous series of 19 PAMAM dendrimers in aqueous solutions at physiological pH (7.4) as a function of dendrimer generation, terminal group, and core chemistry. To g...

  12. β-Lactam antibiotics epitope mapping with STD NMR spectroscopy: a study of drug-human serum albumin interaction

    International Nuclear Information System (INIS)

    Milagre, Cintia D. F.; Cabeca, Luis F.; Almeida, Wanda P.; Marsaioli, Anita J.

    2012-01-01

    Molecular recognition events are key issues in many biological processes. STD NMR (saturation transfer difference nuclear magnetic resonance spectroscopy) is one of the techniques used to understand such biological interactions. Herein, we have investigated the interactions of four β-lactam antibiotics belonging to two classes (cephalosporins and penicillins) with human serum albumin (HSA) by 1 H STD NMR revealing that the interaction between the aromatic moiety and HSA is responsible for the binding efficiency. Thus, the structural differences from the five to six-membered thio ring in penicillins and cephalosporins do not seem to influence antibiotic albumin interactions. (author)

  13. Stereoselective Binding of Flurbiprofen Enantiomers and their Methyl Esters to Human Serum Albumin Studied by Time-Resolved Phosphorescence

    NARCIS (Netherlands)

    mr. Lammers, I.; Lhiaubet-Vallet, V.; Jimenez, M.C.; Ariese, F.; Miranda, M.A.; Gooijer, C.

    2012-01-01

    The interaction of the nonsteroidal anti-inflammatory drug flurbiprofen (FBP) with human serum albumin (HSA) hardly influences the fluorescence of the protein's single tryptophan (Trp). Therefore, in addition to fluorescence, heavy atom-induced room-temperature phosphorescence is used to study the

  14. Synthetic nanoparticles of bovine serum albumin with entrapped salicylic acid

    Directory of Open Access Journals (Sweden)

    Bronze-Uhle ES

    2016-12-01

    Full Text Available ES Bronze-Uhle,1 BC Costa,1 VF Ximenes,2 PN Lisboa-Filho1 1Department of Physics, São Paulo State University (Unesp, School of Sciences, Bauru, São Paulo, Brazil; 2Department of Chemistry, São Paulo State University (Unesp, School of Sciences, Bauru, São Paulo, Brazil Abstract: Bovine serum albumin (BSA is highly water soluble and binds drugs or inorganic substances noncovalently for their effective delivery to various affected areas of the body. Due to the well-defined structure of the protein, containing charged amino acids, albumin nanoparticles (NPs may allow electrostatic adsorption of negatively or positively charged molecules, such that substantial amounts of drug can be incorporated within the particle, due to different albumin-binding sites. During the synthesis procedure, pH changes significantly. This variation modifies the net charge on the surface of the protein, varying the size and behavior of NPs as the drug delivery system. In this study, the synthesis of BSA NPs, by a desolvation process, was studied with salicylic acid (SA as the active agent. SA and salicylates are components of various plants and have been used for medication with anti-inflammatory, antibacterial, and antifungal properties. However, when administered orally to adults (usual dose provided by the manufacturer, there is 50% decomposition of salicylates. Thus, there has been a search for some time to develop new systems to improve the bioavailability of SA and salicylates in the human body. Taking this into account, during synthesis, the pH was varied (5.4, 7.4, and 9 to evaluate its influence on the size and release of SA of the formed NPs. The samples were analyzed using field-emission scanning electron microscopy, transmission electron microscopy, Fourier transform infrared, zeta potential, and dynamic light scattering. Through fluorescence, it was possible to analyze the release of SA in vitro in phosphate-buffered saline solution. The results of

  15. Chiral recognition of naproxen enantiomers based on fluorescence quenching of bovine serum albumin-stabilized gold nanoclusters

    Science.gov (United States)

    Jafari, Marzieh; Tashkhourian, Javad; Absalan, Ghodratollah

    2017-10-01

    A simple, fast and green method for chiral recognition of S- and R-naproxen has been introduced. The method was based on quenching of the fluorescence intensity of bovine serum albumin-stabilized gold nanoclusters in the presence of naproxen enantiomers. The quenching intensity in the presence of S-naproxen was higher than R-naproxen when phosphate buffer solution at pH 7.0 was used. The chiral recognition occurred due to steric effect between bovine serum albumin conformation and naproxen enantiomers. Two linear determination range were established as 7.4 × 10-7-9.1 × 10-6 and 9.1 × 10-6-3.1 × 10-5 mol L-1 for both enantiomers and detection limits of 7.4 × 10-8 mol L- 1 and 9.5 × 10-8 mol L-1 were obtained for S- and R-naproxen, respectively. The developed method showed good repeatability and reproducibility for the analysis of a synthetic sample. To make the procedure applicable to biological samples, the removal of heavy metals from the sample is suggested before any analytical attempt.

  16. 99mTc-albumin can replace 125I-albumin to determine plasma volume repeatedly

    DEFF Research Database (Denmark)

    Bonfils, Peter K; Damgaard, Morten; Stokholm, Knud H

    2012-01-01

    OBJECTIVE: Plasma volume assessment may be of importance in several disorders. The purpose of the present study was to compare the reliability of plasma volume measurements by technetium-labeled human serum albumin ((99m)Tc-HSA) with a simultaneously performed plasma volume determination...... with iodine-labeled human serum albumin ((125)I-HSA). MATERIALS AND METHODS: In 15 healthy volunteers, simultaneous plasma volume measurements with (99m)Tc-HSA and (125)I-HSA were performed after ½ hour in the supine position. Blood samples were obtained 10, 15, 20, and 30 minutes after the injection...... for accurate retropolation from the plasma counts to time zero to correct for leakage of the isotopes from the circulation. RESULTS: The mean difference (bias) between plasma volume measured with (125)I-albumin and (99m)Tc-albumin was 8 ml (0.1 ml/kg) with limits of agreement (bias ±1.96 SD) ranging from -181...

  17. Human serum albumin binding of certain antimalarials

    Science.gov (United States)

    Marković, Olivera S.; Cvijetić, Ilija N.; Zlatović, Mario V.; Opsenica, Igor M.; Konstantinović, Jelena M.; Terzić Jovanović, Nataša V.; Šolaja, Bogdan A.; Verbić, Tatjana Ž.

    2018-03-01

    Interactions between eight in-house synthesized aminoquinolines, along with well-known chloroquine, and human serum albumin (HSA) have been studied by fluorescence spectroscopy. The synthesized aminoquinolines, despite being structurally diverse, were found to be very potent antimalarials. Fluorescence measurements indicate that three compounds having additional thiophene or benzothiophene substructure bind more strongly to HSA than other studied compounds. Competitive binding experiments indicate that these three compounds bind significantly stronger to warfarin compared to diazepam binding site. Fluorescence quenching at three temperatures (20, 25, and 37 °C) was analyzed using classical Stern-Volmer equation, and a static quenching mechanism was proposed. The enthalpy and entropy changes upon sulphur-containing compound-HSA interactions were calculated using Van't Hoff equation. Positive values of enthalpy and entropy changes indicate that non-specific, hydrophobic interactions are the main contributors to HSA-compound interaction. Molecular docking and calculated lipophilicity descriptors indicate the same, pointing out that the increased lipophilicity of sulphur-containing compounds might be a reason for their better binding to HSA. Obtained results might contribute to design of novel derivatives with improved pharmacokinetic properties and drug efficacy.

  18. Thermodynamic studies on the interaction of folic acid with bovine serum albumin

    International Nuclear Information System (INIS)

    Jha, Niki S.; Kishore, Nand

    2011-01-01

    Research highlights: → Thermodynamics of binding of folic acid with bovine serum albumin studied. → Effect of co-solutes on binding permitted detailed analysis of interactions. → Electrostatic interactions dominate with contribution from hydrogen bonding. → No significant conformational change in protein observed upon drug binding. - Abstract: Binding of the vitamin folic acid with bovine serum albumin (BSA) has been studied using isothermal titration calorimetry (ITC) in combination with fluorescence and circular dichroism spectroscopies. The thermodynamic parameters of binding have been evaluated as a function of temperature, ionic strength, in the presence of nonionic surfactants triton X-100, tetrabutylammonium bromide, and sucrose. The values of the van't Hoff enthalpy calculated from the temperature dependence of the binding constant agree with the calorimetric enthalpies indicating that the binding of folic acid to the BSA is a two state process without involving intermediates. These observations are supported by the intrinsic fluorescence and circular dichroism spectroscopic measurements. With increase in the ionic strength, reduction in the binding affinity of folic acid to BSA is observed suggesting predominance of electrostatic interactions in the binding. The contribution of hydrophobic interactions in the binding is also demonstrated by decrease in the binding affinity in the presence of tetrabutylammonium bromide (TBAB). The value of binding affinity in the presence of sucrose indicates that hydrogen bonding also plays a significant contribution in the complexation process. The calorimetric and spectroscopic results provide quantitative information on the binding of folic acid to BSA and suggest that the binding is dominated by electrostatic interactions with contribution from hydrogen bonding.

  19. Thermodynamic Study of the Interaction of Bovine Serum Albumin and Amino Acids with Cellulose Nanocrystals

    OpenAIRE

    Lombardo, Salvatore; Eyley, Sam; Schütz, Christina; Van Gorp, Hans; Rosenfeldt, Sabine; Van den Mooter, Guy; Thielemans, Wim

    2017-01-01

    The interaction of bovine serum albumin (BSA) with sulfated, carboxylated, and pyridinium-grafted cellulose nanocrystals (CNCs) was studied as a function of the degree of substitution by determining the adsorption isotherm and by directly measuring the thermodynamics of interaction. The adsorption of BSA onto positively charged pyridinium-grafted cellulose nanocrystals followed Langmuirian adsorption with the maximum amount of adsorbed protein increasing linearly with increasing degree of sub...

  20. [Study of Reaction Dynamics between Bovine Serum Albumin and Folic Acid by Stopped-Flow/Fluorescence].

    Science.gov (United States)

    Ye, San-xian; Luo, Yun-jing; Qiao, Shu-liang; Li, Li; Liu, Cai-hong; Shi, Jian-long; An, Xue-jing

    2016-01-01

    As a kind of coenzyme of one-carbon enzymes in vivo, folic acid belongs to B vitamins, which can interact with other vitamins and has great significance for converting among amino acids, dividing growth of cells and protein synthesis reactions. Half-life, concentration and reaction rate constant of drugs are important parameters in pharmacokinetic study. In this paper, by utilizing fluorescence spectrophotometer and stopped-flow spectrum analyzer, reaction kinetic parameters between bovine serum albumin(BSA) and folic acid in a bionic system have been investigated, which provide references for parameters of drug metabolism related to folic acid. By using Stern-Volmer equation dealing with fluorescence quenching experiments data, we concluded that under 25, 30, and 37 degrees C, the static quenching constants of folic acid to intrinsic fluorescence from bovine serum albumin were 2.455 x 10(10), 4.900 x 10(10) and 6.427 x 10(10) L x mol(-1) x s(-1) respectively; The results of kinetic reaction rate have shown that the reaction rate of BSA and folic acid are greater than 100 mol x L(-1) x s(-1) at different temperatures, pH and buffering media, illustrating that the quenching mechanism between BSA and folic acid is to form composite static quenching process. Reaction concentration of bovine serum albumin and its initial concentration were equal to the secondary reaction formula, and the correlation coefficient was 0.998 7, while the half-life (t1/2) was 0.059 s at physiological temperature. With the increase of folic acid concentration, the apparent rate constant of this reaction had a linear increasing trend, the BSA fluorescence quenching rate constant catalyzed by folic acid was 3.174 x 10(5) mol x L(-1) x s(-1). Furthermore, with different buffer, the apparent rate constant and reaction rate constant of BSA interacting with folic acid were detected to explore the influence on the reaction under physiological medium, which is of great significance to determine the

  1. Insights into the ninhydrin chemiluminescent reaction and its potential for micromolar determination of human serum albumin

    Energy Technology Data Exchange (ETDEWEB)

    Alvarez, M. Rodriguez [Department of Physical and Analytical Chemistry, Faculty of Chemistry, University of Oviedo, Av. Julian Claveria, 8 33006 Oviedo (Spain); Laino, R. Badia [Department of Physical and Analytical Chemistry, Faculty of Chemistry, University of Oviedo, Av. Julian Claveria, 8 33006 Oviedo (Spain); Diaz-Garcia, M.E. [Department of Physical and Analytical Chemistry, Faculty of Chemistry, University of Oviedo, Av. Julian Claveria, 8 33006 Oviedo (Spain)]. E-mail: medg@uniovi.es

    2006-06-15

    The N-terminal region of human serum albumin (HSA) has an inherent affinity for Co(II) ions. On this basis a new continuous flow method for detection of HSA has been developed taking advantage of the strong quenching effect of the albumin in the ninhydrin-H{sub 2}O{sub 2}-Co(II) chemiluminescent system. The analytical potential of the system is compared with other conventional chemiluminescent reagents. The method gives linear responses from the detection limit (0.30 {mu}M HSA) up to 6.8 {mu}M. The repeatability of the method is good (RSD=7%), it is cheap and rapid to apply and does not require the use of insoluble or expensive reagents nor sophisticated equipment.

  2. Albumin and pre-albumin levels do not reflect the nutritional status of female adolescents with restrictive eating disorders.

    Science.gov (United States)

    Huysentruyt, Koen; De Schepper, Jean; Vanbesien, Jesse; Vandenplas, Yvan

    2016-04-01

    Albumin and pre-albumin are frequently used as nutritional markers in clinical practice. We examined whether serum albumin and pre-albumin were predicted by body mass index (BMI), hydration and/or inflammation in female adolescents with a recently diagnosed restrictive eating disorder (RED). This was a retrospective study of female adolescents with RED from 2002 to 2011. Low albumin and pre-albumin levels were defined as nutritional status in adolescents with RED. ©2015 Foundation Acta Paediatrica. Published by John Wiley & Sons Ltd.

  3. Serum albumin levels in burn people are associated to the total body surface burned and the length of hospital stay but not to the initiation of the oral/enteral nutrition.

    Science.gov (United States)

    Pérez-Guisado, Joaquín; de Haro-Padilla, Jesús M; Rioja, Luis F; Derosier, Leo C; de la Torre, Jorge I

    2013-01-01

    Serum albumin levels have been used to evaluate the severity of the burns and the nutrition protein status in burn people, specifically in the response of the burn patient to the nutrition. Although it hasn't been proven if all these associations are fully funded. The aim of this retrospective study was to determine the relationship of serum albumin levels at 3-7 days after the burn injury, with the total body surface area burned (TBSA), the length of hospital stay (LHS) and the initiation of the oral/enteral nutrition (IOEN). It was carried out with the health records of patients that accomplished the inclusion criteria and were admitted to the burn units at the University Hospital of Reina Sofia (Córdoba, Spain) and UAB Hospital at Birmingham (Alabama, USA) over a 10 years period, between January 2000 and December 2009. We studied the statistical association of serum albumin levels with the TBSA, LHS and IOEN by ANOVA one way test. The confidence interval chosen for statistical differences was 95%. Duncan's test was used to determine the number of statistically significantly groups. Were expressed as mean±standard deviation. We found serum albumin levels association with TBSA and LHS, with greater to lesser serum albumin levels found associated to lesser to greater TBSA and LHS. We didn't find statistical association with IOEN. We conclude that serum albumin levels aren't a nutritional marker in burn people although they could be used as a simple clinical tool to identify the severity of the burn wounds represented by the total body surface area burned and the lenght of hospital stay.

  4. [Study on the interaction of doxycycline with human serum albumin].

    Science.gov (United States)

    Hu, Tao-Ying; Chen, Lin; Liu, Ying

    2014-05-01

    The present study was designed to investigate the interaction of doxycycline (DC) with human serum albumin (HSA) by the inner filter effects, displacement experiments and molecular docking methods, based on classic multi-spectroscopy. With fluorescence quenching method at 298 and 310 K, the binding constants Ka, were determined to be 2. 73 X 10(5) and 0. 74X 10(5) L mol-1, respectively, and there was one binding site between DC and HSA, indicating that the binding of DC to HSA was strong, and the quenching mechanism was a static quenching. The thermodynamic parameters (enthalpy change, AH and enthropy change, delta S) were calculated to be -83. 55 kJ mol-1 and -176. 31 J mol-1 K-1 via the Vant' Hoff equation, which indicated that the interaction of DC with HSA was driven mainly by hydrogen bonding and van der Waals forces. Based on the Föster's theory of non-radiation energy transfer, the specific binding distance between Trp-214 (acceptor) and DC (donor) was 4. 98 nm, which was similar to the result confirmed by molecular docking. Through displacement experiments, sub-domain IIA of HSA was assigned to possess the high-affinity binding site of DC. Three-dimensional fluorescence spectra indicated that the binding of DC to HSA induced the conformation change of HSA and increased the disclosure of some part of hydrophobic regions that had been buried before. The results of FTIR spectroscopy showed that DC bound to HSA led to the slight unfolding of the polypeptide chain of HSA. Furthermore, the binding details between DC and HSA were further confirmed by molecular docking methods, which revealed that DC was bound at sub-domain IIA through multiple interactions, such as hydrophobic effect, polar forces and pi-pi interactions. The experimental results provide theoretical basis and reliable data for the study of the interaction between small drug molecule and human serum albumin

  5. Spectroscopic studies on the interaction between ZnSe nanoparticles with bovine serum albumin

    International Nuclear Information System (INIS)

    Chen, Zhi; Wu, Dudu

    2012-01-01

    The interaction between ZnSe nanoparticles (NPs) and bovine serum albumin (BSA) was studied by UV–vis, fluorescence spectroscopic techniques. The results showed that the fluorescence of BSA was strongly quenched by ZnSe NPs and the quenching mechanism was discussed to be a static quenching procedure, which was proved by quenching constant (K q ). The recorded UV–vis data and the fluorescence data quenching by the ZnSe NPs showed that the interaction between them leads to the formation of ZnSe–BSA complex. Based on the synchronous fluorescence spectra, it was established that the conformational change of BSA was induced by the interaction of ZnSe with the tyrosine micro-region of the BSA molecules. Furthermore, the temperature effects on the structural and spectroscopic properties of individual ZnSe NPs and protein and their bioconjugates (ZnSe–BSA) were also researched. It was found that, compared to the monotonic decrease of the individual ZnSe NPs fluorescence intensity, the temperature dependence of the ZnSe–BSA emission had a much more complex behavior, which was highly sensitive to the conformational changes of the protein. - Highlights: ►Interaction between bovine serum albumin (BSA) and ZnSe nanoparticles was studied. ► UV–vis data and fluorescence data demonstrated the formation of ZnSe–BSA complex. ► Temperature dependence of ZnSe–BSA emission was sensitive to the conformational changes of protein.

  6. Polymerized serum albumin beads for use as slow-release adjuvants

    International Nuclear Information System (INIS)

    Martin, M.E.D.

    1987-02-01

    Experimental vaccines have been made by covalently bonding virus particles into polymerized rabbit serum albumin beads. Using Nodamura virus as a model antigen, these model vaccines induced specific humoral antibody production, comparable with that achieved using Freund's adjuvants. Virus specific antibodies were also induced when Nodamura virus was covalently attached to the bead surface using different crosslinkers. However, when poliovirus type 2 (Sabin strain) was polymerized into beads, the levels of neutralizing antibodies were insignificant compared with control aqueous vaccines. The synthetic immunostimulator, muramyl dipeptide, was included with bead vaccines in an attempt to potentiate the immune response. Immunostimulation is achieved by a slow release of antigen coinciding with the gradual breakdown of bead structure. Methods used include radio-iodination and radioimmunoassay. 65 figs., 6 tabs., 173 refs

  7. Intestinal absorption of dinitrophenyl-lysine and effect of immunization with dinitrophenylated bovine serum albumin

    International Nuclear Information System (INIS)

    Shimura, Fumio; Shimura, Junko; Shimazaki, Shigeki; Hosoya, Norimasa

    1983-01-01

    The intestinal absorption of dinitrophenyl-lysine (DNP-lys) was studied with a special interest on the role of the immune system in the absorption of small molecules which are recognized as nonself. [ 3 H]-DNP- lys was rapidly absorbed by ligated intestinal loops in situ via a saturable and unique route. When [ 3 H]-DNP-lys was preincubated with the immume serum obtained from rats immunized with dinitrophenylated bovine serum albumin (DNP-BSA), the [ 3 H]-DNP-lys absorption was depressed. The absorption of [ 3 H]-DNP-lys in DNP-BSA-immunized rats was depressed compared to the control. The results obtained suggest that the immune system play a role in avoiding the absorption of small molecules with antigenicity. (author)

  8. The influence of salt type on the retention of bovine serum albumin in ion-exchange chromatography

    DEFF Research Database (Denmark)

    Al-Jibbouri, Sattar

    2007-01-01

    In this paper, an analysis of the influence of the salt types, NaCl, NaCH"3COO, Na"2SO"4 and Na"3C"6H"5O"7, on the isocratic retention behaviour of bovine serum albumin (BSA) on two anion-exchangers media (Source 30Q and TSK Gel Super Q 5 PW) has been presented. The retention data demonstrated...

  9. Effective binding of perhalogenated closo-borates to serum albumins revealed by spectroscopic and ITC studies

    Science.gov (United States)

    Kuperman, Marina V.; Losytskyy, Mykhaylo Yu.; Bykov, Alexander Yu.; Yarmoluk, Sergiy M.; Zhizhin, Konstantin Yu.; Kuznetsov, Nikolay T.; Varzatskii, Oleg A.; Gumienna-Kontecka, Elzbieta; Kovalska, Vladyslava B.

    2017-08-01

    The interactions of boron cluster compounds closo-borates with biomolecules are widely studied due to their efficiency as agents for boron neutron capture therapy of cancer. In present work the binding abilities of anionic halogen closo-borates [B10Hal10]2- (Hal = Cl, Br, I) and [B12Hal12]2- (Hal = Cl, I) towards bovine and human serum albumins were investigated by spectroscopic and isothermal titration calorimetry (ITC) methods. The protein fluorescence quenching method and ITC studies confirmed the complex formation. The degree of protein fluorescence quenching increased from chlorine to iodine boron derivatives that is attributed to external heavy atom effect. The ITC data point on the existence in the protein structure of two types of binding sites: with higher and lower affinity to closo-borates. Albumin-closo-borate complex binding ratio, n (4-5 anions per protein molecule) is higher than for the parent hydrogen closo-borates (2 anions per protein molecule). Binding constants estimated by fluorescent and ITC methods indicate higher affinity of halogen closo-borates to albumins (K in the range of 104-106 M-1) comparing to that of the hydrogen closo-borate (K about 103 M-1). Due to their high affinity and high binding ratio to albumins halogen closo-borates are proposed for further studies as agents for boron neutron capture therapy.

  10. Recombinant albumin monolayers on latex particles.

    Science.gov (United States)

    Sofińska, Kamila; Adamczyk, Zbigniew; Kujda, Marta; Nattich-Rak, Małgorzata

    2014-01-14

    The adsorption of recombinant human serum albumin (rHSA) on negatively charged polystyrene latex micro-particles was studied at pH 3.5 and the NaCl concentration range of 10(-3) to 0.15 M. The electrophoretic mobility of latex monotonically increased with the albumin concentration in the suspension. The coverage of adsorbed albumin was quantitatively determined using the depletion method, where the residual protein concentration was determined by electrokinetic measurements and AFM imaging. It was shown that albumin adsorption was irreversible. Its maximum coverage on latex varied between 0.7 mg m(-2) for 10(-3) M NaCl to 1.3 mg m(-2) for 0.15 M NaCl. The latter value matches the maximum coverage previously determined for human serum albumin on mica using the streaming potential method. The increase in the maximum coverage was interpreted in terms of reduced electrostatic repulsion among adsorbed molecules. These facts confirm that albumin adsorption at pH 3.5 is governed by electrostatic interactions and proceeds analogously to colloid particle deposition. The stability of albumin monolayers was measured in additional experiments where changes in the latex electrophoretic mobility and the concentration of free albumin in solutions were monitored over prolonged time periods. Based on these experimental data, a robust procedure of preparing albumin monolayers on latex particles of well-controlled coverage and molecule distribution was proposed.

  11. Biomimetic synthesis of calcium carbonate with different morphologies and polymorphs in the presence of bovine serum albumin and soluble starch.

    Science.gov (United States)

    Liu, Yuxi; Chen, Yuping; Huang, Xuechen; Wu, Gang

    2017-10-01

    Calcium carbonate has been synthesized by the reaction of Na 2 CO 3 and CaCl 2 in the presence of bovine serum albumin (BSA) and soluble starch. Effects of various bovine serum albumin (BSA) and soluble starch on the polymorph and morphology of CaCO 3 crystals were investigated. Crystallization of vaterite is favored in the presence of BSA and soluble starch, respectively, while calcite is favored in the presence of a mixture of BSA and soluble starch. The morphologies of CaCO 3 particles in the presence of mixture of BSA and soluble starch are mainly rod-like, suggesting that the BSA, soluble and their assemblies play key roles in stabilizing and directing the CaCO 3 crystal growth. Copyright © 2017. Published by Elsevier B.V.

  12. Presence of albumin mRNA precursors in nuclei of analbuminemic rat liver lacking cytoplasmic albumin mRNA.

    OpenAIRE

    Esumi, H; Takahashi, Y; Sekiya, T; Sato, S; Nagase, S; Sugimura, T

    1982-01-01

    Analbuminemic rats, which lack serum albumin, were previously found to have no albumin mRNA in the cytoplasm of the liver. In the present study, the existence of nuclear albumin mRNA precursors in the liver of analbuminemic rats was examined by RNA X cDNA hybridization kinetics. Albumin mRNA precursors were present in the nuclei of analbuminemic rat liver at almost normal levels, despite the absence of albumin mRNA from the cytoplasm. Nuclear RNA of analbuminemic rat liver was subjected to el...

  13. HPMA-based drug delivery system and its interactions of human serum albumin: SAXS, ITC, and NMR study

    Czech Academy of Sciences Publication Activity Database

    Filippov, Sergey K.; Kaberov, Leonid; Zhang, X.; Niebuur, B.-J.; Chytil, Petr; Etrych, Tomáš; Wieland, F.; Velychkivska, Nadiia; Starovoytova, Larisa; Svergun, D.; Papadakis, C.

    2017-01-01

    Roč. 254, 20 August (2017), s. 455 ISSN 0065-7727. [ACS National Meeting & Exposition /254./. 20.08.2017-24.08.2017, Washington] R&D Projects: GA ČR(CZ) GC15-10527J Institutional support: RVO:61389013 Keywords : HPMA * human serum albumin * SAXS Subject RIV: CF - Physical ; Theoretical Chemistry OBOR OECD: Physical chemistry

  14. Quantitation of species differences in albumin–ligand interactions for bovine, human and rat serum albumins using fluorescence spectroscopy: A test case with some Sudlow's site I ligands

    Energy Technology Data Exchange (ETDEWEB)

    Poór, Miklós [Institute of Laboratory Medicine, University of Pécs, Ifjúság u. 13, Pécs H-7624 (Hungary); Li, Yin; Matisz, Gergely [Department of General and Physical Chemistry, University of Pécs, Pécs H-7624 (Hungary); János Szentágothai Research Center, Pécs H-7624 (Hungary); Kiss, László [Department of General and Physical Chemistry, University of Pécs, Pécs H-7624 (Hungary); Kunsági-Máté, Sándor [Department of General and Physical Chemistry, University of Pécs, Pécs H-7624 (Hungary); János Szentágothai Research Center, Pécs H-7624 (Hungary); Kőszegi, Tamás, E-mail: koszegit@freemail.hu [Institute of Laboratory Medicine, University of Pécs, Ifjúság u. 13, Pécs H-7624 (Hungary)

    2014-01-15

    Albumin, the most abundant plasma protein is an approximately 67 kDa sized water-soluble macromolecule. Since several drugs and xenobiotics circulate in the blood at least partially in albumin-bound form, albumin plays a key role in the pharmacokinetics/toxicokinetics of these chemicals. Most of the drugs and xenobiotics are Sudlow's site I ligands. In numerous studies, bovine serum albumin (BSA) is used for modeling albumin–ligand interactions and the results are extrapolated to human serum albumin (HSA). Furthermore, only limited information is available related to albumin–ligand interactions of different albumin species. Therefore, in our study, we have focused on the quantification of differences between bovine, human and rat serum albumin (RSA) using four Sudlow's site I ligands (luteolin, ochratoxin A, phenylbutazone and warfarin). Interactions were analyzed by fluorescence spectroscopy. Stability constants as well as competing capacities of the ligands were determined, and thermodynamic study was also performed. Our results highlight that there could be major differences between BSA, HSA and RSA in their ligand binding properties. Based on our observations we emphasize that in molecular aspects BSA behaves considerably differently from HSA or from albumins of other species therefore, it is strongly recommended to apply at least some confirmatory measurements when data obtained from other species are attempted to be extrapolated to HSA. -- Highlights: • Albumin–ligand interactions of human, bovine and rat albumins were studied. • Four Sudlow's site I ligands were tested by fluorescence spectroscopy. • Substantial differences were found in stability constants among albumin complexes. • Competing capacity of ligands showed major differences in the studied species. • Data obtained for BSA cannot be directly extrapolated to human albumin.

  15. Bacillus anthracis Co-Opts Nitric Oxide and Host Serum Albumin for Pathogenicity in Hypoxic Conditions

    Directory of Open Access Journals (Sweden)

    Stephen eSt John

    2013-05-01

    Full Text Available Bacillus anthracis is a dangerous pathogen of humans and many animal species. Its virulence has been mainly attributed to the production of Lethal and Edema toxins as well as the antiphagocytic capsule. Recent data indicate that the nitric oxide (NO synthase (baNOS plays an important pathogenic role at the early stage of disease by protecting bacteria from the host reactive species and S-nytrosylating the mitochondrial proteins in macrophages. In this study we for the first time present evidence that bacteria-derived NO participates in the generation of highly reactive oxidizing species which could be abolished by the NOS inhibitor L-NAME, free thiols, and superoxide dismutase but not catalase. The formation of toxicants is likely a result of the simultaneous formation of NO and superoxide leading to a labile peroxynitrite and its stable decomposition product, nitrogen dioxide. The toxicity of bacteria could be potentiated in the presence of bovine serum albumin. This effect is consistent with the property of serum albumin to serves as a trap of a volatile NO accelerating its reactions. Our data suggest that during infection in the hypoxic environment of pre-mortal host the accumulated NO is expected to have a broad toxic impact on host cell functions.

  16. Renal targeted delivery of triptolide by conjugation to the fragment peptide of human serum albumin.

    Science.gov (United States)

    Yuan, Zhi-xiang; Wu, Xiao-juan; Mo, Jingxin; Wang, Yan-li; Xu, Chao-qun; Lim, Lee Yong

    2015-08-01

    We have previously demonstrated that peptide fragments (PFs) of the human serum albumin could be developed as potential renal targeting carriers, in particular, the peptide fragment, PF-A299-585 (A299-585 representing the amino acid sequence of the human serum albumin). In this paper, we conjugated triptolide (TP), the anti-inflammatory Chinese traditional medicine, to PF-A299-585 via a succinic acid spacer to give TPS-PF-A299-585 (TP loading 2.2% w/w). Compared with the free TP, TPS-PF-A299-585 exhibited comparable anti-inflammatory activity in the lipopolysaccharide stimulated MDCK cells, but was significantly less cytotoxic than the free drug. Accumulation of TPS-PF-A299-585 in the MDCK cells in vitro and in rodent kidneys in vivo was demonstrated using FITC-labeled TPS-PF-A299-585. Renal targeting was confirmed in vivo in a membranous nephropathic (MN) rodent model, where optical imaging and analyses of biochemical markers were combined to show that TPS-PF-A299-585 was capable of alleviating the characteristic symptoms of MN. The collective data affirm PF-A299-585 to be a useful carrier for targeting TP to the kidney. Copyright © 2015 Elsevier B.V. All rights reserved.

  17. Composition comprising radioactive labeled-fibrinogen and albumin

    International Nuclear Information System (INIS)

    Charlton, J.C.; Gravett, D.L.

    1976-01-01

    The stability of fibrinogen is improved by mixing it with albumin, preferably at least 5 parts by weight of albumin per part by weight of fibrinogen. By this invention, iodinated ( 125 I) human fibrinogen can be stabilized with human serum albumin for use in the diagnosis of thrombi

  18. Multiple binding modes of ibuprofen in human serum albumin identified by absolute binding free energy calculations

    KAUST Repository

    Evoli, Stefania

    2016-11-10

    Human serum albumin possesses multiple binding sites and transports a wide range of ligands that include the anti-inflammatory drug ibuprofen. A complete map of the binding sites of ibuprofen in albumin is difficult to obtain in traditional experiments, because of the structural adaptability of this protein in accommodating small ligands. In this work, we provide a set of predictions covering the geometry, affinity of binding and protonation state for the pharmaceutically most active form (S-isomer) of ibuprofen to albumin, by using absolute binding free energy calculations in combination with classical molecular dynamics (MD) simulations and molecular docking. The most favorable binding modes correctly reproduce several experimentally identified binding locations, which include the two Sudlow\\'s drug sites (DS2 and DS1) and the fatty acid binding sites 6 and 2 (FA6 and FA2). Previously unknown details of the binding conformations were revealed for some of them, and formerly undetected binding modes were found in other protein sites. The calculated binding affinities exhibit trends which seem to agree with the available experimental data, and drastically degrade when the ligand is modeled in a protonated (neutral) state, indicating that ibuprofen associates with albumin preferentially in its charged form. These findings provide a detailed description of the binding of ibuprofen, help to explain a wide range of results reported in the literature in the last decades, and demonstrate the possibility of using simulation methods to predict ligand binding to albumin.

  19. Study of albumin from beef blood serum in D{sub 2}O solutions; Badanie roztworow albuminy z surowicy wolowej w D{sub 2}O

    Energy Technology Data Exchange (ETDEWEB)

    Lewandowska, D. [Inst. of Experimental Physics, Gdansk Univ. (Poland); Podoski, T. [Wyzsza Szkola Morska, Gdynia (Poland)

    1994-12-31

    Molecular dynamics of albumin obtained from beef blood serum have been investigated in heavy water solutions by means of NMR spectra. The chemical shifts as well as spin-lattice relaxation times have been measured. The number of water protons interacting with albumin molecule have been estimated. 9 refs, 2 figs, 3 tabs.

  20. Conjugation of nano and quantum materials with bovine serum albumin (BSA) to study their biological potential

    Energy Technology Data Exchange (ETDEWEB)

    Singh, Suman, E-mail: sumansingh01@gmail.com [Central Scientific Instruments Organisation (CSIR-CSIO), Chandigarh (India); Kaur, Rajnish; Chahal, Jitender; Devi, P. [Central Scientific Instruments Organisation (CSIR-CSIO), Chandigarh (India); Jain, D.V.S. [Panjab University, Chandigarh (India); Singla, M.L., E-mail: singla_min@yahoo.co.in [Central Scientific Instruments Organisation (CSIR-CSIO), Chandigarh (India)

    2013-09-15

    Conjugates of gold nanoparticles (AuNPs) and semiconductor quantum dots (CdS/T) have been synthesized with bovine serum albumin (BSA) using wet chemistry. The optical properties of nano and quantum materials and their BSA conjugate have been studied using UV–Visible and Fluorescence spectroscopy. UV–Visible spectrum of pure BSA showed an absorption maximum at 278 nm, which showed blue shift after its conjugation with nano and quantum materials. Increased concentration of AuNPs during conjugation resulted in broadening of BSA peak (278 nm), which can be related to the formation of ground state complex formation, caused by the partial adsorption of BSA on the surface of NPs. However, increased concentrations of BSA resulted in decrease in SPR intensity of gold nanoparticles (528 nm) and absorbance peak of BSA started diminishing. AuNPs acted as quencher for BSA fluorescence intensity, when excited at 280 nm. The binding constant (K) and the number of binding sites (n) between AuNPs and BSA have been found to be 1.97×10{sup 2} LM{sup −1} and 0.6 respectively. With quantum dots, conjugation resulted in enhancement of fluorescence emission of quantum dots when excited at 300 nm, which might be due to the stabilizing effect of BSA on QDs or due to energy transfer from tryptophan moieties of albumin to quantum dots. -- Highlights: • Synthesis of nanoparticles (AuNPs) and quantum dots (CdS). • Conjugation of these materials with bovine serum albumin. • Optical behavioral studies.

  1. Bovine serum albumin adsorption on passivated porous silicon layers

    Science.gov (United States)

    Lockwood, David; Boukherroub, Rabah

    2005-03-01

    Hydrogen-terminated porous silicon (pSi) films were fabricated through electrochemical anodization of crystalline Si in HF-based solutions. The pSi-H surface was chemically functionalized by thermal reaction with undecylenic acid to produce an organic monolayer covalently attached to the silicon surface through Si-C bonds and bearing an acid terminal group. Bovine serum albumin (BSA) was then adsorbed onto the modified surface. SEM showed that the porous films were damaged and partially lifted off the Si substrate after a prolonged BSA adsorption. Ellipsometry revealed that the BSA had penetrated ˜ 1.3 micrometers into the porous structure. The film damage results from BSA anchoring itself tightly through strong electrostatic interactions to the acid-covered Si sidewalls. A change in surface tension during BSA film formation then causes the pSi layer to buckle and lift-off the underlying Si substrate. FTIR results from the modified pSi surfaces showed the presence of strong characteristic Amide I, II and III vibrational bands after BSA adsorption.

  2. Binding of anandamide to bovine serum albumin

    DEFF Research Database (Denmark)

    Bojesen, I.N.; Hansen, Harald S.

    2003-01-01

    The endocannabinoid anandamide is of lipid nature and may thus bind to albumin in the vascular system, as do fatty acids. The knowledge of the free water-phase concentration of anandamide is essential for the investigations of its transfer from the binding protein to cellular membranes, because...... a water-phase shuttle of monomers mediates such transfers. We have used our method based upon the use of albumin-filled red cell ghosts as a dispersed biological "reference binder" to measure the water-phase concentrations of anandamide. These concentrations were measured in buffer (pH 7.3) in equilibrium...... that BSA has one high-affinity binding site for anandamide at all four temperatures. The free energy of anandamide binding (¿G) is calculated to -43.05 kJ mol with a large enthalpy (¿H ) contribution of -42.09 kJ mol. Anandamide has vasodilator activity, and the binding to albumin may mediate its transport...

  3. Reinforcement of calcium phosphate cement with multi-walled carbon nanotubes and bovine serum albumin for injectable bone substitute applications

    NARCIS (Netherlands)

    Chew, K.K.; Low, K.L.; Zein, S.H.S.; McPhail, D.; Gerhardt, L.C.; Roether, J.A.; Boccaccini, A.R.

    2011-01-01

    This paper presents the development of novel alternative injectable calcium phosphate cement (CPC) composites for orthopaedic applications. The new CPC composites comprise ß-tri-calcium phosphate (ß-TCP) and di-calcium phosphate anhydrous (DCPA) mixed with bovine serum albumin (BSA) and incorporated

  4. Alpha-fetoprotein (AFP) modulates the effect of serum albumin on brain development by restraining the neurotrophic effect of oleic acid.

    Science.gov (United States)

    García-García, Alejandro G; Polo-Hernández, Erica; Tabernero, Arantxa; Medina, José M

    2015-10-22

    We have previously shown that serum albumin controls perinatal rat brain development through the regulation of oleic acid synthesis by astrocytes. In fact, oleic acid synthesized and released by astrocytes promoted neurite growth, neuron migration and the arrangement of prospective synapses. In this work we show that alpha-fetoprotein (AFP) is also present in the brain during embryonic development, its concentrations peaking at E15.5 and at E19.5. However, after E19.5 AFP concentrations plummeted concurrently with a sharp increase in serum albumin concentrations. At E15.5, AFP is present in caudal regions of the brain, particularly in brain areas undergoing differentiation during this period, such as the thalamic reticular nucleus of the thalamus, the hypothalamus, the amygdala and the hippocampus. Albumin was not detected in the brain at E15.5 but stained brain cells substantially on day E19.5, showing a very similar distribution to that of AFP under the same circumstances. The concentrations of free oleic acid in the brain were inversely correlated with those of AFP, suggesting that the signals elicited by AFP and oleic acid can be inversely associated. GAP-43, a marker of axonal growth that is highly expressed by the presence of oleic acid, was not co-localized with AFP except in the marginal zone and areas delimiting the subplate. AFP prevented the increase in GAP-43 expression caused by the presence of oleic acid in neurons in primary culture in vitro and in organotypic cultures of embryonic rat brain ex vivo, suggesting that AFP may modulate the effect of serum albumin on brain development. Copyright © 2015 The Authors. Published by Elsevier B.V. All rights reserved.

  5. Patterns of the adsorption of bovine serum albumin on carboxymethyl dextran and carboxymethyl cellulose films

    Science.gov (United States)

    Paribok, I. V.; Solomyanskii, A. E.; Zhavnerko, G. K.

    2016-02-01

    Patterns of the adsorption of bovine serum albumin on carboxymethyl dextran and carboxymethyl cellulose films are studied by means of microcontact printing, atomic force microscopy, and quartz crystal microbalance. It is shown that both the charge of polysaccharide macromolecules and the technique for deposition of their films onto the surface (via adsorption from a solution or covalent cross-linking) are factors that determine the degree of nonspecific adsorption of the protein on such films.

  6. The kinetics of the phospholipase A2-catalyzed hydrolysis of Egg phosphatidylcholine in unilamellar vesicles. Product inhibition and its relief by serum albumin.

    Science.gov (United States)

    Kupferberg, J P; Yokoyama, S; Kézdy, F J

    1981-06-25

    Only the lecithin in the outer leaflet (representing 70% of the total) of egg lecithin unilamellar vesicles is hydrolyzed by Crotalus atrox phospholipase A2. Hydrolyzed vesicles remain intact and impermeable to ionic solutes. The fatty acids produced in the hydrolysis remain on the vesicle and are only partially ionized at neutral pH due to electrostatic repulsions. About 40% of the lysolecithin product is desorbed from the vesicle. In the presence of a large excess of bovine serum albumin, the reaction is first order with respect to both the enzyme and the substrate. At 21 degrees C, pH 7.2, I = 0.16 M, and [Ca2+] = 7 mM, the second order rate constant is kex(2) = 1.5 X 10(6) M-1 s-1. In the absence of albumin, the reaction is inhibited competitively by both the monomeric (KIm = 4.5 X 10(-8) M) and micellar (nKIa = 3.7 X 10(-7) M) forms of lysolecithin ([critical micelle concentration] = 4.3 X 10(-6) M). Bovine serum albumin complexes two molecules of lysolecithin with a dissociation constant, Kb = 5 X 10(-8) M. With substoichiometric albumin, the reaction is biphasic, and, when the albumin is saturated with lysolecithin, the kinetics become similar to those observed in the absence of albumin. The action of phospholipase A2 shows that in unilamellar vesicles there is only one major lecithin conformation in the outer leaflet, or that all conformations are rapidly interconvertible.

  7. Serum albumin-adjusted glycated albumin is an adequate indicator of glycemic control in patients with Cushing's syndrome.

    Science.gov (United States)

    Kitamura, Tetsuhiro; Otsuki, Michio; Tamada, Daisuke; Tabuchi, Yukiko; Mukai, Kosuke; Morita, Shinya; Kasayama, Soji; Bando, Yukihiro; Shimomura, Iichiro; Koga, Masafumi

    2014-12-01

    We recently reported that glycated albumin (GA) in patients with Cushing's syndrome is low. In the present study, we examined whether serum albumin (SA)-adjusted GA (SAaGA) is an adequate indicator of glycemic control in patients with Cushing's syndrome. We studied 26 patients with Cushing's syndrome (13 patients without diabetes and 13 patients with diabetes). Twenty six non-diabetic subjects and 26 patients with type 2 diabetes mellitus matched for age, sex and BMI were used as the controls. SAaGA was calculated using the regression formula between SA and GA in non-diabetic patients with Cushing's syndrome and non-diabetic subjects. SA showed a significant correlation with GA in non-diabetic patients with Cushing's syndrome and non-diabetic subjects. GA, but not SAaGA, in non-diabetic patients with Cushing's syndrome was significantly lower than that in the non-diabetic controls. Furthermore, the GA/HbA1c ratio, but not the SAaGA/HbA1c ratio, in diabetic patients with Cushing's syndrome was significantly lower than that in the diabetic controls. The measured GA in the patients with Cushing's syndrome was significantly lower than the estimated GA, but there was no difference between SAaGA and the estimated GA. The present findings suggest that SAaGA is an adequate indicator of the glycemic control in patients with Cushing's syndrome. Copyright © 2014 The Canadian Society of Clinical Chemists. Published by Elsevier Inc. All rights reserved.

  8. Preparation and characterization of microspheres of albumin-heparin conjugates

    NARCIS (Netherlands)

    Kwon, Glen S.; Bae, You Han; Kim, Sung Wan; Cremers, Harry; Cremers, H.F.M.; Feijen, Jan

    1991-01-01

    Albumin-heparin microspheres have been prepared as a new drug carrier. A soluble albumin-heparin conjugate was synthesized by forming amide bonds between human serum albumin and heparin. After purification the albumin-heparin conjugate was crosslinked in a water-in-oil emulsion to form

  9. Synthesis and anti-angiogenic effect of conjugates between serum albumin and non-steroidal anti-inflammatory drugs

    DEFF Research Database (Denmark)

    Kjær, Birgitte; Struve, Casper; Friis, Tina

    2010-01-01

    Non-steroidal anti-inflammatory drugs (NSAIDs) inhibit tumor growth and angiogenesis. Covalent linkage of naproxen to human serum albumin (HSA) has been shown to target it efficiently to the liver and this may potentially be exploited for liver-selective inhibition of angiogenesis. With the aim...... effect on endothelial cells at or above the level of the non-conjugated NSAIDs in an in vitro angiogenesis assay....

  10. Comparison of bone scintigraphy with serum tumor markers of CA 15-3 and carcinoembryonic antigen in patients with breast carcinoma

    International Nuclear Information System (INIS)

    Gedik, G. K.; Kiratli, P.O.; Aras, T.; Tascioglu, B.

    2006-01-01

    To compare the bone scintigraphy findings with a carcinoembryonic antigen (CEA) and cancer antigen 15-3 (CA 15-3) levels in breast carcinoma patients. We also investigated the relationship between anatomical bone type and its effect on tumor marker levels. The study was consisted of retrospective evaluation of 120 bone scans of patients with breast carcinoma admitted to the Nuclear Medicine Department, Medical Faculty, Hacettepe University, Ankara, Turkey between January 2003 and December 2004. The mean age of the patients was 54.7 years. We grouped the results of the bone scans into 3 as normal, equivocal and metastatic. Carcinoembryonic antigen and CA 15-3 levels were recorded from the files of the patients. Upper cut levels of 4.8 U/ml for CEA and 38 U/ml for CA 15-3 was accepted. Metastatic bone areas were distributed according to their anatomical location as long, short, flat, irregular and sesamoid and effect of bone type on tumor marker was investigated. In 16 of the patients, bone scintigraphy revealed metastases. Sixty-one patients had normal scans and in 47 patients metastases could not be ruled out. In patients with metastases, CA 15-3 was elevated in 8 and CEA was higher than the upper limit in 6. For CEA and CA 15-3, the anatomical type of bone has no any effect on serum tumor marker concentration between patients with normal and elevated levels of tumor markers in metastatic patients. Tumor markers are not solely enough in predicting bone metastases. Bone scintigraphy and tumor markers should be both used in management of patients with breast carcinoma. The anatomical type of bone has no any effect on elevation of serum tumor marker concentration. (author)

  11. Clinical evaluation of hepatic scintigraphy using sup 99m Tc-GSA

    Energy Technology Data Exchange (ETDEWEB)

    Ishii, Katsumi; Nishiyama, Shogo; Nishimaki, Hiroshi; Tadokoro, Katsumi; Ikeda, Toshiaki; Matsubayashi, Takashi; Ishii, Kodo (Kitasato Univ., Sagamihara, Kanagawa (Japan). School of Medicine)

    1992-06-01

    Functional hepatic imaging was performed using {sup 99m}Tc-DTPA-galactosyl human serum albumin ({sup 99m}Tc-GSA), a radiolabeled ligand that reacts specifically to the asialoglycoprotein receptor that resides at the plasma membrane of hepatocytes, in 21 patients: five with chronic active hepatitis (CAH), 14 with compensative liver cirrhosis (LC), one with chronic inactive hepatitis and one with acute hepatitis. The former two diseases were mainly investigated. Serial liver images were acquired at the rates of 10 sec/frame for 0-5 min and 2 min/frame for 6-30 min after the injection of {sup 99m}Tc-GSA, and the images were compared with {sup 99m}Tc-phytase images in 2 patients with CAH and 11 with LC, and those with portal scintigrams using {sup 123}I-iodoamphetamine (IMP) in 3 patients with LC. The images using {sup 99m}Tc-GSA were in better agreement with hepatic function than those using {sup 99m}Tc-phytase, and with the findings of portal scintigraphy using {sup 123}I-IMP. LHL15 (liver/liver and heart radioactivities at 15 min after injection of {sup 99m}Tc-GSA) correlated with the hepaplastin test (r=0.978 in CAH, and r=0.544 in LC), indicators of hepatic reserve. These results suggest that liver scintigraphy using {sup 99m}Tc-GSA might be a useful method for evaluating liver function. (author).

  12. Biophysical influence of coumarin 35 on bovine serum albumin: Spectroscopic study

    Science.gov (United States)

    Bayraktutan, Tuğba; Onganer, Yavuz

    2017-01-01

    The binding mechanism and protein-fluorescence probe interactions between bovine serum albumin (BSA) and coumarin 35 (C35) was investigated by using UV-Vis absorption and fluorescence spectroscopies since they remain major research topics in biophysics. The spectroscopic data indicated that a fluorescence quenching process for BSA-C35 system was occurred. The fluorescence quenching processes were analyzed using Stern-Volmer method. In this regard, Stern-Volmer quenching constants (KSV) and binding constants were calculated at different temperatures. The distance r between BSA (donor) and C35 (acceptor) was determined by exploiting fluorescence resonance energy transfer (FRET) method. Synchronous fluorescence spectra were also studied to observe information about conformational changes. Moreover, thermodynamics parameters were calculated for better understanding of interactions and conformational changes of the system.

  13. Characterization of the binding of 2-mercaptobenzimidazole to bovine serum albumin.

    Science.gov (United States)

    Teng, Yue; Zou, Luyi; Huang, Ming; Zong, Wansong

    2015-04-01

    2-Mercaptobenzimidazole (MBI) is widely utilized as a corrosion inhibitor, copper-plating brightener and rubber accelerator. The residue of MBI in the environment is potentially harmful to human health. In this article, the interaction of MBI with bovine serum albumin (BSA) was explored using spectroscopic and molecular docking methods under physiological conditions. The positively charged MBI can spontaneously bind with the negatively charged BSA through electrostatic forces with one binding site. The site marker competition experiments and the molecular docking study revealed that MBI bound into site II (subdomain IIIA) of BSA, which further led to some secondary structure and microenvironmental changes of BSA. This work provides useful information on understanding the toxicological actions of MBI at the molecular level. Copyright © 2015 John Wiley & Sons, Ltd.

  14. FTIR study of secondary structure of bovine serum albumin and ovalbumin

    International Nuclear Information System (INIS)

    Abrosimova, K V; Shulenina, O V; Paston, S V

    2016-01-01

    Proteins structure is the critical factor for their functioning. Fourier transform infrared spectroscopy provides a possibility to obtain information about secondary structure of proteins in different states and also in a whole biological samples. Infrared spectra of egg white from the untreated and hard-boiled hen's egg, and also of chicken ovalbumin and bovine serum albumin in lyophilic form and in aqueous solution were studied. Lyophilization of investigated globular proteins is accompanied by the decrease of a-helix structures and the increase in amount of intermolecular β-sheets. Analysis of infrared spectrum of egg white allowed to make an estimation of OVA secondary structure and to observe α-to-β structural transformation as a result of the heat denaturation. (paper)

  15. Improved anticancer effects of albumin-bound paclitaxel nanoparticle via augmentation of EPR effect and albumin-protein interactions using S-nitrosated human serum albumin dimer.

    Science.gov (United States)

    Kinoshita, Ryo; Ishima, Yu; Chuang, Victor T G; Nakamura, Hideaki; Fang, Jun; Watanabe, Hiroshi; Shimizu, Taro; Okuhira, Keiichiro; Ishida, Tatsuhiro; Maeda, Hiroshi; Otagiri, Masaki; Maruyama, Toru

    2017-09-01

    In the latest trend of anticancer chemotherapy research, there were many macromolecular anticancer drugs developed based on enhanced permeability and retention (EPR) effect, such as albumin bound paclitaxel nanoparticle (nab- PTX, also called Abraxane ® ). However, cancers with low vascular permeability posed a challenge for these EPR based therapeutic systems. Augmenting the intrinsic EPR effect with an intrinsic vascular modulator such as nitric oxide (NO) could be a promising strategy. S-nitrosated human serum albumin dimer (SNO-HSA Dimer) shown promising activity previously was evaluated for the synergistic effect when used as a pretreatment agent in nab-PTX therapy against various tumor models. In the high vascular permeability C26 murine colon cancer subcutaneous inoculation model, SNO-HSA Dimer enhanced tumor selectivity of nab-PTX, and attenuated myelosuppression. SNO-HSA Dimer also augmented the tumor growth inhibition of nab-PTX in low vascular permeability B16 murine melanoma subcutaneous inoculation model. Furthermore, nab-PTX therapy combined with SNO-HSA Dimer showed higher antitumor activity and improved survival rate of SUIT2 human pancreatic cancer orthotopic model. In conclusion, SNO-HSA Dimer could enhance the therapeutic effect of nab-PTX even in low vascular permeability or intractable pancreatic cancers. The possible underlying mechanisms of action of SNO-HSA Dimer were discussed. Copyright © 2017 Elsevier Ltd. All rights reserved.

  16. Displacement of Drugs from Human Serum Albumin: From Molecular Interactions to Clinical Significance.

    Science.gov (United States)

    Rimac, Hrvoje; Debeljak, Željko; Bojić, Mirza; Miller, Larisa

    2017-01-01

    Human serum albumin (HSA) is the most abundant protein in human serum. It has numerous functions, one of which is transport of small hydrophobic molecules, including drugs, toxins, nutrients, hormones and metabolites. HSA has the ability to interact with a wide variety of structurally different compounds. This promiscuous, nonspecific affinity can lead to sudden changes in concentrations caused by displacement, when two or more compounds compete for binding to the same molecular site. It is important to consider drug combinations and their binding to HSA when defining dosing regimens, as this can directly influence drug's free, active concentration in blood. In present paper we review drug interactions with potential for displacement from HSA, situations in which they are likely to occur and their clinical significance. We also offer guidelines in designing drugs with decreased binding to HSA. Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.org.

  17. Detection of human spermatozoal peptides after conjugation to 125I-labelled human serum albumin

    International Nuclear Information System (INIS)

    Metler, L.; Skrabei, H.; Czuppon, A.B.

    1981-01-01

    Human spermatozoal peptides, liberated during autolysis of the cells, were fractionated by gel-filtration chromatography and thin-layer chromatography. After conjugation to 125 I-labelled human serum albumin, all fractions were assayed with rabbit antihuman spermatozoa antiserum. In earlier publications, human sperm-immobilizing and sperm-agglutinating sera were used for the detection of solubilized spermatozoal antigen. The low sensitivity of these tests necessitated a more sensitive test. The purpose of this work is to describe a solid-phase radioimmunoassay for the detection of antigenic peptides

  18. Restriction of the anti-bovine serum albumin response in rabbits immunized with Micrococcus lysodeikticus.

    Science.gov (United States)

    De Baetselier, P; Hamers-Casterman, C; Van der Loo, W; Hamers, R

    1977-01-01

    Rabbits capable of producing antibodies of restricted heterogeneity in response to Micrococcus lysodeikticus are equally capable of producing antibodies of restricted heterogeneity to bovine serum albumin. These antibodies are produced when animals are simultaneously injected with micrococcus and BSA and their specificity is restricted to a small number of epitopes. These results suggest that micrococcal vaccines can induce the restriction of heterogeneity in antibodies raised against totally unrelated antigens. Images Figure 4 Figure 5 Figure 2 Figure 6 Figure 7 Figure 8 PMID:71263

  19. Small-angle X-ray scattering studies on the X-ray induced aggregation of ribonnuclease, lactate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase and serum albumin. A comparison with malate synthase

    International Nuclear Information System (INIS)

    Zipper, P.; Gatterer, H.G.; Schutz, J.; Durchschlag, H.

    1980-01-01

    The X-ray induced aggregation of ribonuclease, lactate dehydrogenase (LDH), glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and serum albumin in aqueous solution was monitored in situ by means of small-angle X-ray scattering. Measurements carried out with ribonuclease, LDH and serum albumin in the absence of dithiothreitol (DTT) and with GAPDH in the presence of 0.2mM DTT established the following series for the rates of aggregation of the proteins under these conditions: ribonuclease >LDH> >GAPDH> serum albumin. Within six hours from the beginning of irradiation (i.e. about the time required for the exposure of one complete scattering curve under the conditions of our experiments) the following increases of R tilde resulted: ribonuclease 9%, LDH 7%, GAPDH 4%, serum albumin <1%. Changes of R tilde exceeding 1% are, of course, too high to be tolerated in conventional scattering experiments. Measurements carried out with LDH and GAPDH in the presence of 2mM DTT established a strong protective effect of DTT against the X-ray induced aggregation of these enzymes. The initial increase of R tilde upon irradiation of LDH and GAPDH in the presence of 2mM DTT was found to be even lower than the increase of R tilde observed when serum albumin was irradiated in the absence of DTT. However, the observed decrease of anti x of LDH and GAPDH at the early stages of irradiation suggested the occurrence of fragmentation of the enzymes as another consequence of radiation damage. This finding is discussed in context with the results from previous scattering experiments and electrophoretic studies on malate synthase. (author)

  20. Interaction of Palmitic Acid with Metoprolol Succinate at the Binding Sites of Bovine Serum Albumin

    Directory of Open Access Journals (Sweden)

    Mashiur Rahman

    2014-12-01

    Full Text Available Purpose: The aim of this study was to characterize the binding profile as well as to notify the interaction of palmitic acid with metoprolol succinate at its binding site on albumin. Methods: The binding of metoprolol succinate to bovine serum albumin (BSA was studied by equilibrium dialysis method (ED at 27°C and pH 7.4, in order to have an insight in the binding chemistry of the drug to BSA in presence and absence of palmitic acid. The study was carried out using ranitidine as site-1 and diazepam as site-2 specific probe. Results: Different analysis of binding of metoprolol succinate to bovine serum albumin suggested two sets of association constants: high affinity association constant (k1 = 11.0 x 105 M-1 with low capacity (n1 = 2 and low affinity association (k2 = 4.0×105 M-1 constant with high capacity (n2 = 8 at pH 7.4 and 27°C. During concurrent administration of palmitic acid and metoprolol succinate in presence or absence of ranitidine or diazepam, it was found that palmitic acid displaced metoprolol succinate from its binding site on BSA resulting reduced binding of metoprolol succinate to BSA. The increment in free fraction of metoprolol succinate was from 26.27% to 55.08% upon the addition of increased concentration of palmitic acid at a concentration of 0×10-5 M to 16×10-5 M. In presence of ranitidine and diazepam, palmitic acid further increases the free fraction of metoprolol succinate from 33.05% to 66.95% and 40.68% to 72.88%, respectively. Conclusion: This data provided the evidence of interaction at higher concentration of palmitic acid at the binding sites on BSA, which might change the pharmacokinetic properties of metoprolol succinate.

  1. Impedimetric immunosensor for human serum albumin detection on a direct aldehyde-functionalized silicon nitride surface

    Energy Technology Data Exchange (ETDEWEB)

    Caballero, David, E-mail: caballero@unistra.fr [Nanobioengineering group-IBEC, Barcelona Science Park, C/ Baldiri Reixach 10-12, 08028 Barcelona (Spain); University of Barcelona, Department of Electronics, C/ Marti i Franques 1, 08028 Barcelona (Spain); Centro de Investigacion Biomedica en Red en Bioingenieria, Biomateriales y Nanomedicina (CIBER-BBN), 50018 Zaragoza (Spain); Martinez, Elena [Nanobioengineering group-IBEC, Barcelona Science Park, C/ Baldiri Reixach 10-12, 08028 Barcelona (Spain); Centro de Investigacion Biomedica en Red en Bioingenieria, Biomateriales y Nanomedicina (CIBER-BBN), 50018 Zaragoza (Spain); Bausells, Joan [Centre Nacional de Microelectronica (CNM-IMB), CSIC, Campus UAB, 08193 Bellaterra (Spain); Errachid, Abdelhamid, E-mail: abdelhamid.errachid-el-salhi@univ-lyon1.fr [Nanobioengineering group-IBEC, Barcelona Science Park, C/ Baldiri Reixach 10-12, 08028 Barcelona (Spain); Universite Claude Bernard - Lyon 1, LSA - UMR 5180, 43 Bd du 11 novembre 1918, 69622 Villeurbanne Cedex (France); Samitier, Josep [Nanobioengineering group-IBEC, Barcelona Science Park, C/ Baldiri Reixach 10-12, 08028 Barcelona (Spain); University of Barcelona, Department of Electronics, C/ Marti i Franques 1, 08028 Barcelona (Spain); Centro de Investigacion Biomedica en Red en Bioingenieria, Biomateriales y Nanomedicina (CIBER-BBN), 50018 Zaragoza (Spain)

    2012-03-30

    Highlights: Black-Right-Pointing-Pointer An impedimetric label-free immunosensor was developed for the specific detection of human serum albumin proteins. Black-Right-Pointing-Pointer Anti-HSA antibodies were covalently immobilized on silicon nitride surfaces using a direct functionalization methodology. Black-Right-Pointing-Pointer Silicon nitride offers multiple advantages compared to other common materials. Black-Right-Pointing-Pointer The proposed sensor has high sensitivity and good selectivity for the detection of HSA proteins. - Abstract: In this work we report the fabrication and characterization of a label-free impedimetric immunosensor based on a silicon nitride (Si{sub 3}N{sub 4}) surface for the specific detection of human serum albumin (HSA) proteins. Silicon nitride provides several advantages compared with other materials commonly used, such as gold, and in particular in solid-state physics for electronic-based biosensors. However, few Si{sub 3}N{sub 4}-based biosensors have been developed; the lack of an efficient and direct protocol for the integration of biological elements with silicon-based substrates is still one of its the main drawbacks. Here, we use a direct functionalization method for the direct covalent binding of monoclonal anti-HSA antibodies on an aldehyde-functionalized Si-p/SiO{sub 2}/Si{sub 3}N{sub 4} structure. This methodology, in contrast with most of the protocols reported in literature, requires less chemical reagents, it is less time-consuming and it does not need any chemical activation. The detection capability of the immunosensor was tested by performing non-faradaic electrochemical impedance spectroscopy (EIS) measurements for the specific detection of HSA proteins. Protein concentrations within the linear range of 10{sup -13}-10{sup -7} M were detected, showing a sensitivity of 0.128 {Omega} {mu}M{sup -1} and a limit of detection of 10{sup -14} M. The specificity of the sensor was also addressed by studying the

  2. Impedimetric immunosensor for human serum albumin detection on a direct aldehyde-functionalized silicon nitride surface

    International Nuclear Information System (INIS)

    Caballero, David; Martinez, Elena; Bausells, Joan; Errachid, Abdelhamid; Samitier, Josep

    2012-01-01

    Highlights: ► An impedimetric label-free immunosensor was developed for the specific detection of human serum albumin proteins. ► Anti-HSA antibodies were covalently immobilized on silicon nitride surfaces using a direct functionalization methodology. ► Silicon nitride offers multiple advantages compared to other common materials. ► The proposed sensor has high sensitivity and good selectivity for the detection of HSA proteins. - Abstract: In this work we report the fabrication and characterization of a label-free impedimetric immunosensor based on a silicon nitride (Si 3 N 4 ) surface for the specific detection of human serum albumin (HSA) proteins. Silicon nitride provides several advantages compared with other materials commonly used, such as gold, and in particular in solid-state physics for electronic-based biosensors. However, few Si 3 N 4 -based biosensors have been developed; the lack of an efficient and direct protocol for the integration of biological elements with silicon-based substrates is still one of its the main drawbacks. Here, we use a direct functionalization method for the direct covalent binding of monoclonal anti-HSA antibodies on an aldehyde-functionalized Si-p/SiO 2 /Si 3 N 4 structure. This methodology, in contrast with most of the protocols reported in literature, requires less chemical reagents, it is less time-consuming and it does not need any chemical activation. The detection capability of the immunosensor was tested by performing non-faradaic electrochemical impedance spectroscopy (EIS) measurements for the specific detection of HSA proteins. Protein concentrations within the linear range of 10 −13 –10 −7 M were detected, showing a sensitivity of 0.128 Ω μM −1 and a limit of detection of 10 −14 M. The specificity of the sensor was also addressed by studying the interferences with a similar protein, bovine serum albumin. The results obtained show that the antibodies were efficiently immobilized and the proteins

  3. Interaction of norfloxacin with bovine serum albumin studied by different spectrometric methods; displacement studies, molecular modeling and chemometrics approaches

    Energy Technology Data Exchange (ETDEWEB)

    Naseri, Abdolhossein, E-mail: a_naseri@tabrizu.ac.ir [Departments of Analytical Chemistry, Faculty of Chemistry, University of Tabriz, Tabriz 51666-16471 (Iran, Islamic Republic of); Hosseini, Soheila [Departments of Analytical Chemistry, Faculty of Chemistry, University of Tabriz, Tabriz 51666-16471 (Iran, Islamic Republic of); Rasoulzadeh, Farzaneh [Drug Applied Research Center, Tabriz University of Medical Sciences, Tabriz 51644-14766 (Iran, Islamic Republic of); Rashidi, Mohammad-Reza [Research Center for Pharmaceutical Nanotechnology, Tabriz University of Medical Sciences, Tabriz 51644-14766 (Iran, Islamic Republic of); Zakery, Maryam; Khayamian, Taghi [Department of Chemistry, College of Chemistry, Isfahan University of Technology, Isfahan 84154 (Iran, Islamic Republic of)

    2015-01-15

    Serum albumins as major target proteins can bind to other ligands leading to alteration of their pharmacological properties. The mechanism of interaction between norfloxacin (NFLX) with bovine serum albumin (BSA) was investigated. Fuorescence quenching of serum albumin by this drug was found to be a static quenching process. The binding sites number, n, apparent binding constant, K, and thermodynamic parameters were calculated at different temperatures. The distance, r, between donor, BSA, and acceptor, NFLX, was calculated according to the Forster theory of non-radiation energy transfer. Also binding characteristics of NFLX with BSA together with its displacement from its binding site by kanamycin and effect of common metal ions on binding constant were investigated by the spectroscopic methods. The conformational change in the secondary structure of BSA upon interaction with NFLX was investigated qualitatively from synchronous fluorescence spectra, Fourier Transform Infrared (FTIR) and circular dichroism (CD) spectrometric methods. Molecular docking studies were performed to obtain information on the possible residues involved in the interaction process and changes in accessible surface area of the interacting residues. The results showed that the conformation of BSA changed in the presence of NFLX. For the first time, displacement studies were used for this interaction; displacement studies showed that NFLX was displaced by phenylbutazon and ketoprofen but was not displaced by ibuprofen indicating that the binding site of NFLX on albumin was site I. In addition a powerful chemometrics method, multivariate curve resolution-alternating least square, was used for resolution of spectroscopic augmented data obtained in two different titration modes in order to extract spectral information regardless of spectral overlapping of components. - Highlights: • Interaction between norfloxacin and BSA is studied by spectral methods. • Chemometrics methods are used to

  4. Application of fluorescent and vibration spectroscopy for septic serum human albumin structure deformation during pathology

    Science.gov (United States)

    Zyubin, A.; Konstantinova, E.; Slezhkin, V.; Matveeva, K.; Samusev, I.; Bryukhanov, V.

    2017-12-01

    In this paper we perform results of conformational analysis of septic human serum albumin (HSA) carried out by Raman spectroscopy (RS), infrared (IR) spectroscopy and fluorescent spectroscopy. The main vibrational groups were identified and analyzed for septic HSA and its health control. Comparison between Raman and IR results were done. Fluorescent spectral changes of Trp-214 group were analyzed. Application of Raman, IR spectroscopy, fluorescent spectroscopy for conformational changes study of HSA during pathology were shown.

  5. Synthesis and characterization of imprinted sorbent for separation of gramine from bovine serum albumin

    International Nuclear Information System (INIS)

    Luliński, Piotr; Klejn, Dorota; Maciejewska, Dorota

    2016-01-01

    The aim of this study was to develop an efficient sorbent for separation of N,N-dimethyl-3-aminomethylindole (gramine) from bovine serum albumin. An imprinting technology was involved in the synthesis of polymers from nine different functional monomers in the presence of ethylene glycol dimethacrylate as a cross-linker. The analysis of binding capacities showed that the highest specificity towards gramine was achieved when 4-vinylbenzoic acid was used as the functional monomer in methanol to form the bulk imprinted polymer, MIP1 (imprinting factor equal to 21.3). The Scatchard analysis of MIP1 showed two classes of binding sites with the dissociation constants K_d equal to 0.105 and 6.52 μmol L"−"1. The composition and morphology of polymers were defined by "1"3C CP/MAS NMR, BET and SEM-EDS analyses. The recognition mechanism of MIP1 was tested using the structurally related bioanalytes, and the dominant role of indole moiety and ethylamine side chain was revealed. A new MISPE protocol was optimized for separation of gramine. The total recoveries on MIP1 were equal to 94 ± 12 % from standard solutions and 85 ± 11 % from bovine serum albumin. - Highlights: • Indole alkaloid (gramine) imprinted polymer was synthesized. • Very high specifity of sorbent towards gramine was achieved. • Physico-chemical characteristics of novel material was presented. • Efficient MISPE protocol was proposed for separation of gramine from model sample.

  6. The Investigation of the Interaction between Lomefloxacin and Human Serume Albumin by Specteroscopic Methods

    Directory of Open Access Journals (Sweden)

    F. S. Goldouzian, Z. S.Goldouzian, M. Momen Heravi, J. Khanchamani

    2012-03-01

    Full Text Available Mechanism of the binding of lomefloxacin (LMF with human serum albumin has been studied at physiological pH (7.4 using fluorescence spectroscopic technique. LMF is a third-generation fluoroquinolone antibiotic that exhibits striking potency against a broad spectrum of Gram-negative and Gram-positive bacteria through inhibition of DNA gyrase. Lomefloxacin is a drug that is excreted in urine and has very variable systemic absorption. Human serum albumin (HSA is the most important and abundant constituent of blood plasma and serves as a protein storage component. Recently, the three-dimensional structure of HSA was determined through X-ray crystallographic measurement. Fluorescence studies showed that (LMF has an ability to quench the intrinsic fluorescence of HSA through a static quenching  procedure  according to the Stern–Volmer equation .LMF showed two types of binding sites, the first having a very high affinity (1/72 ×107M-1 and a secondary binding site with an affinity two orders lower than the primary site. The number of binding sites for complex: HSA-LMF at 280 nm was calculated 1and0.5. The microenvironment of tryptophan and tyrosin residues and more hydrophobic of fluorophores microenvironment were changed and disturbed by the blue shift in maximum wavelength and decreased in fluorescence intensity in the presence of lomefloxacin revealed  decreased polarity of the fluorophores. The binding site for LMF is in a hydrophobic pocket in the sub-domain II A of HSA.

  7. Synthesis and characterization of imprinted sorbent for separation of gramine from bovine serum albumin

    Energy Technology Data Exchange (ETDEWEB)

    Luliński, Piotr; Klejn, Dorota; Maciejewska, Dorota, E-mail: dmaciejewska@wum.edu.pl

    2016-08-01

    The aim of this study was to develop an efficient sorbent for separation of N,N-dimethyl-3-aminomethylindole (gramine) from bovine serum albumin. An imprinting technology was involved in the synthesis of polymers from nine different functional monomers in the presence of ethylene glycol dimethacrylate as a cross-linker. The analysis of binding capacities showed that the highest specificity towards gramine was achieved when 4-vinylbenzoic acid was used as the functional monomer in methanol to form the bulk imprinted polymer, MIP1 (imprinting factor equal to 21.3). The Scatchard analysis of MIP1 showed two classes of binding sites with the dissociation constants K{sub d} equal to 0.105 and 6.52 μmol L{sup −1}. The composition and morphology of polymers were defined by {sup 13}C CP/MAS NMR, BET and SEM-EDS analyses. The recognition mechanism of MIP1 was tested using the structurally related bioanalytes, and the dominant role of indole moiety and ethylamine side chain was revealed. A new MISPE protocol was optimized for separation of gramine. The total recoveries on MIP1 were equal to 94 ± 12 % from standard solutions and 85 ± 11 % from bovine serum albumin. - Highlights: • Indole alkaloid (gramine) imprinted polymer was synthesized. • Very high specifity of sorbent towards gramine was achieved. • Physico-chemical characteristics of novel material was presented. • Efficient MISPE protocol was proposed for separation of gramine from model sample.

  8. Clinical aspects of pulmonary radioactivity observed in radiocolloid liver scintigraphy

    International Nuclear Information System (INIS)

    So, Young; Lee, Kang Wook; Lee, Heon Young; Lee, Won Woo

    2002-01-01

    We studied clinical aspects and courses of patients with pulmonary radioactivity on liver scintigraphy and speculated the mechanism of pulmonary uptake of radiocolloids. Forty-nine patients with pulmonary radioactivity were classified into 5 diseases groups-liver disease, infection, cancer, ischemic necrosis of liver, etc.- and their presence of absence of chronic liver disease (CLD), Child-Pugh class, serum levels of AST and ALT, results of follow-up liver scintigraphy and clinical course were checked. Of total 49 patients 25 had CLD; there were 23 liver disease patients, 16 infection patients, 7 advanced cancer patients, 2 ischemic necrosis of liver patients, and 1 hemolytic anemia patient. Reversible rise of serum levels of AST and ALT was observed in all patients with liver disease and ischemic necrosis of liver; on one-way ANOVA, these rise were statistically significant (p<0.01). Serum level of ALT of liver disease group patients without CLD was significantly higher than that of infection group patients without CLD (p<0.05). Among 17 patients who underwent follow-up liver scintigraphy, 13 showed no pulmonary radioactivity. Total 12 patients died during follow-up and most of them were terminal cancer patients or CLD patients of Child-Pugh class C. Pulmonary radioactivity of radiocolloid liver scintigraphy could be attributed to the mobilization of reticuloendothelial system (RES) cells by the activation of RES cells in severe infection and terminal cancer, and also by the extensive liver desctruction in liver diseases

  9. Probing the binding of vitexin to human serum albumin by multispectroscopic techniques

    Energy Technology Data Exchange (ETDEWEB)

    Zhang Guowen, E-mail: gwzhang@ncu.edu.c [State Key Laboratory of Food Science and Technology, Nanchang University, 235, Nanjing East Road, Nanchang 330047, Jiangxi (China); Zhao Nan; Wang Lin [State Key Laboratory of Food Science and Technology, Nanchang University, 235, Nanjing East Road, Nanchang 330047, Jiangxi (China)

    2011-05-15

    The interaction between vitexin and human serum albumin (HSA) has been studied by using different spectroscopic techniques viz., fluorescence, UV-vis absorption, circular dichroism (CD) and Fourier transform infrared (FT-IR) spectroscopy under simulated physiological conditions. Fluorescence results revealed the presence of static type of quenching mechanism in the binding of vitexin to HSA. The binding constants (K{sub a}) between vitexin and HSA were obtained according to the modified Stern-Volmer equation. The thermodynamic parameters, enthalpy change ({Delta}H) and entropy change ({Delta}S) were calculated to be -57.29 kJ mol{sup -1} and -99.01 J mol{sup -1} K{sup -1} via the van't Hoff equation, which indicated that the interaction of vitexin with HSA was driven mainly by hydrogen bond and van der Waals forces. Fluorescence anisotropy data showed that warfarin and vitexin shared a common binding site I corresponding to the subdomain IIA of HSA. The binding distance (r) between the donor (HSA) and the acceptor (vitexin) was 4.16 nm based on the Foerster theory of non-radioactive energy transfer. In addition, the results of synchronous fluorescence, CD and FT-IR spectra demonstrated that the microenvironment and the secondary structure of HSA were changed in the presence of vitexin. - Research highlights: We investigate the binding mechanism of vitexin to human serum albumin (HSA) by different multi-spectroscopic techniques under simulated physiological conditions. Vitexin can strongly quench the fluorescence of HSA through a static quenching mechanism. The interaction of vitexin with HSA is driven mainly by hydrogen bond and van der Waals forces. The binding distance between HSA and vitexin is 4.16 nm, and vitexin is mainly located in the region of site I (subdomain IIA). The binding of vitexin to HSA can induce conformational changes of HSA.

  10. Comparative studies on drug binding to the purified and pharmaceutical-grade human serum albumins: Bridging between basic research and clinical applications of albumin.

    Science.gov (United States)

    Ashrafi-Kooshk, Mohammad Reza; Ebrahimi, Farangis; Ranjbar, Samira; Ghobadi, Sirous; Moradi, Nastaran; Khodarahmi, Reza

    2015-09-01

    Human serum albumin (HSA), the most abundant protein in blood plasma, is a monomeric multidomain protein that possesses an extraordinary capacity for binding, so that serves as a circulating depot for endogenous and exogenous compounds. During the heat sterilization process, the structure of pharmaceutical-grade HSA may change and some of its activities may be lost. In this study, to provide deeper insight on this issue, we investigated drug-binding and some physicochemical properties of purified albumin (PA) and pharmaceutical-grade albumin (PGA) using two known drugs (indomethacin and ibuprofen). PGA displayed significantly lower drug binding capacity compared to PA. Analysis of the quenching and thermodynamic parameters indicated that intermolecular interactions between the drugs and the proteins are different from each other. Surface hydrophobicity as well as the stability of PGA decreased compared to PA, also surface hydrophobicity of PA and PGA increased upon drugs binding. Also, kinetic analysis of pseudo-esterase activities indicated that Km and Vmax parameters for PGA enzymatic activity are more and less than those of PA, respectively. This in vitro study demonstrates that the specific drug binding of PGA is significantly reduced. Such studies can act as connecting bridge between basic research discoveries and clinical applications. Copyright © 2015 The International Alliance for Biological Standardization. Published by Elsevier Ltd. All rights reserved.

  11. The effect of glycation on bovine serum albumin conformation and ligand binding properties with regard to gliclazide

    Science.gov (United States)

    Żurawska-Płaksej, Ewa; Rorbach-Dolata, Anna; Wiglusz, Katarzyna; Piwowar, Agnieszka

    2018-01-01

    Albumin, the major serum protein, plays a variety of functions, including binding and transporting endogenous and exogenous ligands. Its molecular structure is sensitive to different environmental modifiers, among which glucose is one of the most significant. In vivo albumin glycation occurs under physiological conditions, but it is increased in diabetes. Since bovine serum albumin (BSA) may serve as a model protein in in vitro experiments, we aimed to investigate the impact of glucose-mediated BSA glycation on the binding capacity towards gliclazide, as well as the ability of this drug to prevent glycation of the BSA molecule. To reflect normo- and hyperglycemia, the conditions of the glycation process were established. Structural changes of albumin after interaction with gliclazide (0-14 μM) were determined using fluorescence quenching and circular dichroism spectroscopy. Moreover, thermodynamic parameters as well as energy transfer parameters were determined. Calculated Stern-Volmer quenching constants, as well as binding constants for the BSA-gliclazide complex, were lower for the glycated form of albumin than for the unmodified protein. The largest, over 2-fold, decrease in values of binding parameters was observed for the sample with 30 mM of glucose, reflecting the poorly controlled diabetic state, which indicates that the degree of glycation had a critical influence on binding with gliclazide. In contrast to significant changes in the tertiary structure of BSA upon binding with gliclazide, only slight changes in the secondary structure were observed, which was reflected by about a 3% decrease of the α-helix content of glycated BSA (regardless of glucose concentration) in comparison to unmodified BSA. The presence of gliclazide during glycation did not affect its progress. The results of this study indicate that glycation significantly changed the binding ability of BSA towards gliclazide and the scale of these changes depended on glucose concentration. It

  12. Spectroscopic studies of 7, 8-dihydroxy-4-methylcoumarin and its interaction with bovine serum albumin

    Energy Technology Data Exchange (ETDEWEB)

    Hussein, Belal H.M., E-mail: belalhussein102@yahoo.co [Chemistry Department, Faculty of Science, Suez Canal University, Ismailia 41522 (Egypt)

    2011-05-15

    The absorption and fluorescence spectra of 7, 8-dihydroxy-4-methylcoumarin (DHMC) in ethanol-water (1:9 v/v) solution at varying pH values were investigated . The interaction between DHMC and bovine serum albumin (BSA) was investigated by fluorescence, FT-IR, and circular dichroism (CD) spectroscopy. The Stern-Volmer quenching constant (K{sub SV}), the quenching rate constant of the bimolecular reaction (K{sub q}), the binding constant, and number of binding sites (n) of DHMC with BSA were evaluated. The results showed that DHMC quenches the fluorescence intensity of BSA through a static quenching process. Positive value of entropy change ({Delta}S) and negative value of enthalpy change ({Delta}H) of the BSA-DHMC interaction were obtained according to the van't Hoff equation. The interaction between DHMC and BSA was driven mainly by hydrophobic forces. The binding process was spontaneous and exothermic. The binding distance between the tryptophan residue in BSA and the DHMC was found to be about 2.6 nm based on the Foerster theory of non-radiation energy transfer. - Research highlights: {yields} 7,8-dihydroxy-4-methylcoumarin (DHMC) quenched the bovine serum albumin (BSA) fluorescence. {yields} The formation of the DHMC-BSA complex was spontaneous through a static quenching process. {yields} The polarity around the tryptophan residues decreased with the increase of DHMC concentration.

  13. Albumin and multiple sclerosis.

    Science.gov (United States)

    LeVine, Steven M

    2016-04-12

    Leakage of the blood-brain barrier (BBB) is a common pathological feature in multiple sclerosis (MS). Following a breach of the BBB, albumin, the most abundant protein in plasma, gains access to CNS tissue where it is exposed to an inflammatory milieu and tissue damage, e.g., demyelination. Once in the CNS, albumin can participate in protective mechanisms. For example, due to its high concentration and molecular properties, albumin becomes a target for oxidation and nitration reactions. Furthermore, albumin binds metals and heme thereby limiting their ability to produce reactive oxygen and reactive nitrogen species. Albumin also has the potential to worsen disease. Similar to pathogenic processes that occur during epilepsy, extravasated albumin could induce the expression of proinflammatory cytokines and affect the ability of astrocytes to maintain potassium homeostasis thereby possibly making neurons more vulnerable to glutamate exicitotoxicity, which is thought to be a pathogenic mechanism in MS. The albumin quotient, albumin in cerebrospinal fluid (CSF)/albumin in serum, is used as a measure of blood-CSF barrier dysfunction in MS, but it may be inaccurate since albumin levels in the CSF can be influenced by multiple factors including: 1) albumin becomes proteolytically cleaved during disease, 2) extravasated albumin is taken up by macrophages, microglia, and astrocytes, and 3) the location of BBB damage affects the entry of extravasated albumin into ventricular CSF. A discussion of the roles that albumin performs during MS is put forth.

  14. Increasing the X-ray Diffraction Power of Protein Crystals by Dehydration: The Case of Bovine Serum Albumin and a Survey of Literature Data

    Directory of Open Access Journals (Sweden)

    Irene Russo Krauss

    2012-03-01

    Full Text Available Serum albumin is one of the most widely studied proteins. It is the most abundant protein in plasma with a typical concentration of 5 g/100 mL and the principal transporter of fatty acids in plasma. While the crystal structures of human serum albumin (HSA free and in complex with fatty acids, hemin, and local anesthetics have been characterized, no crystallographic models are available on bovine serum albumin (BSA, presumably because of the poor diffraction power of existing hexagonal BSA crystals. Here, the crystallization and diffraction data of a new BSA crystal form, obtained by the hanging drop method using MPEG 5K as precipitating agent, are presented. The crystals belong to space group C2, with unit-cell parameters a = 216.45 Å, b = 44.72 Å, c = 140.18 Å, β = 114.5°. Dehydration was found to increase the diffraction limit of BSA crystals from ~8 Å to 3.2 Å, probably by improving the packing of protein molecules in the crystal lattice. These results, together with a survey of more than 60 successful cases of protein crystal dehydration, confirm that it can be a useful procedure to be used in initial screening as a method of improving the diffraction limits of existing crystals.

  15. Investigation of the binding affinity in vitamin B12-Bovine serum albumin system using various spectroscopic methods

    Science.gov (United States)

    Makarska-Bialokoz, Magdalena

    2017-09-01

    The binding affinity between vitamin B12 (VitB12) and bovine serum albumin (BSA) has been investigated in aqueous solution at pH = 7.4, employing UV-vis absorption and steady-state, synchronous and three-dimensional fluorescence spectra techniques. Representative effects noted for BSA intrinsic fluorescence resulting from the interactions with VitB12 confirm the formation of π-π stacked non-covalent and non-fluorescent complexes in the system VitB12-BSA. All the determined parameters, the binding, fluorescence quenching and bimolecular quenching rate constants (of the order of 104 L mol- 1, 103 L mol- 1 and 1011 L mol- 1 s- 1, respectively), as well as Förster resonance energy transfer parameters validate the mechanism of static quenching. The interaction with VitB12 induces folding of the polypeptide chains around Trp residues of BSA, resulting in a more hydrophobic surrounding. Presented outcomes suggest that the addition of VitB12 can lead to the more organized BSA conformation and its more folded tertiary structure, what could influence the physiological functions of bovine serum albumin, notably in case of its overuse or abnormal metabolism.

  16. Combined spectroscopic and molecular docking techniques to study interaction of Zn (II) DiAmsar with serum albumins

    Energy Technology Data Exchange (ETDEWEB)

    Bardajee, Ghasem Rezanejade, E-mail: rezanejad@pnu.ac.ir; Hooshyar, Zari; Shafagh, Pegah; Ghiasvand, Samira; Kakavand, Nahaleh

    2014-12-15

    Zinc (II) diamine-sarcophagine (Zn (II) DiAmsar) as a water soluble hexadentate ligand was synthesized and characterized by nuclear magnetic resonance (NMR), Fourier transform infrared (FT-IR) and UV–visible (UV–vis) spectroscopy. The bindings of Zn (II) DiAmsar with human serum albumin (HSA) and bovine serum albumin (BSA) were investigated under the simulative physiological conditions. To study this binding, the fluorescence spectra in combination with FT-IR, UV–vis, cyclic voltammetry (CV), and molecular docking techniques were used in the present work. The results indicate that Zn (II) DiAmsar quenched effectively the intrinsic fluorescence of HSA and BSA via a static quenching process. The fluorescence quenching data was also used to determine binding sites and binding constants at different temperatures. The calculated thermodynamic parameters (∆G°, ∆H°, and ∆S°) suggest that the binding process occurs spontaneously by involving hydrogen bond and van der Waals interactions. The distance between HSA (or BSA) as a donor and Zn (II) DiAmsar as an acceptor was obtained according to fluorescence resonance energy transfer (FRET). In addition, the docking results revealed the possible binding sites and assess the microenvironment around the bounded Zn (II) DiAmsar.

  17. Alkylation of human serum albumin by sulfur mustard in vitro and in vivo : Mass spectrometric analysis of a cysteine adduct as a sensitive biomarker of exposure

    NARCIS (Netherlands)

    Noort, D.; Hulst, A.G.; Jong, L.P.A. de; Benschop, H.P.

    1999-01-01

    To develop a mass spectrometric assay for the detection of sulfur mustard adducts with human serum albumin, the following steps were performed: quantitation of the binding of the agent to the protein by using [14C] sulfur mustard and analysis of acidic and tryptic digests of albumin from blood after

  18. Molecular interaction of PCB153 to human serum albumin: Insights from spectroscopic and molecular modeling studies

    Energy Technology Data Exchange (ETDEWEB)

    Han, Chao; Fang, Senbiao; Cao, Huiming; Lu, Yan; Ma, Yaqiong [School of Pharmacy, Lanzhou University, Lanzhou 730000 (China); Wei, Dongfeng [Institute of Basic Research in Clinical Medicine, China Academy of Chinese Medical Sciences, Beijing 100700 (China); Xie, Xiaoyun [College of Earth and Environmental Science, Lanzhou University, Lanzhou 730000 (China); Liu, Xiaohua [School of Pharmacy, Lanzhou University, Lanzhou 730000 (China); Li, Xin [College of Food and Bioengineering, Henan University of Science and Technology, Luoyang 471003 (China); Fei, Dongqing [School of Pharmacy, Lanzhou University, Lanzhou 730000 (China); Zhao, Chunyan, E-mail: zhaochy07@lzu.edu.cn [School of Pharmacy, Lanzhou University, Lanzhou 730000 (China)

    2013-03-15

    Highlights: ► We identify the binding mode of PCB153 to human serum albumin (HSA). ► Spectroscopic and molecular modeling results reveal that PCB153 binds at the site II. ► The interaction is mainly governed by hydrophobic and hydrogen bond forces. ► The work helps to probe transporting, distribution and toxicity effect of PCBs. -- Abstract: Polychlorinated biphenyls (PCBs) possessed much potential hazard to environment because of its chemical stability and biological toxicity. Here, we identified the binding mode of a representative compound, PCB153, to human serum albumin (HSA) using fluorescence and molecular dynamics simulation methods. The fluorescence study showed that the intrinsic fluorescence of HSA was quenched by addition of PCB153 through a static quenching mechanism. The thermodynamic analysis proved the binding behavior was mainly governed by hydrophobic force. Furthermore, as evidenced by site marker displacement experiments using two probe compounds, it revealed that PCB153 acted exactly on subdomain IIIA (site II) of HSA. On the other hand, the molecular dynamics studies as well as free energy calculations made another important contribution to understand the conformational changes of HSA and the stability of HSA-PCB153 system. Molecular docking revealed PCB153 can bind in a large hydrophobic activity of subdomain IIIA by the hydrophobic interaction and hydrogen bond interactions between chlorine atoms and residue ASN391. The present work provided reasonable models helping us further understand the transporting, distribution and toxicity effect of PCBs when it spread into human blood serum.

  19. Albumin supplementation for hypoalbuminemia following burns: unnecessary and costly!

    Science.gov (United States)

    Melinyshyn, Alex; Callum, Jeannie; Jeschke, Marc C; Cartotto, Robert

    2013-01-01

    Following fluid resuscitation, patients with major burns frequently develop prolonged hypoalbuminemia. It is not known whether this should be corrected by albumin supplementation. The purpose of this study was to determine whether there are any benefits associated with albumin supplementation to correct hypoalbuminemia in burned adults. We conducted a retrospective comparison of patients with burns ≥ 20% TBSA admitted to an adult regional American Burn Association-verified burn center, from May 1, 2009, to September 30, 2010, where we did not routinely supplement albumin (control group), with patients admitted from October 1, 2010, to May 30, 2011, where we had instituted a protocol in which 5% human albumin was provided to maintain serum albumin levels >20 g/L (albumin group). Comparisons were made from postburn (PB) day 2 to day 30 inclusive. There were no significant differences between control (n = 26) and albumin (n = 17) in age (48 ± 15 vs 45 ± 21 years; P = .56), burn size (33 ± 13 vs 34 ± 13 %TBSA; P = .831), or full thickness burn size (19 ± 19 vs 23 ± 19 %TBSA; P = .581). Inhalation injury was significantly more frequent in the albumin group than in controls (71% vs 31%; P = .01). The groups did not differ significantly in need for admission escharotomy, admission Sequential Organ Failure Assessment (SOFA) score, number of surgical procedures/first 30 days, or 24 and 48 hours fluid resuscitation volume requirements. The overall mean daily serum albumin level from PB day 2 to 30 in the albumin group (26.9 ± 3.0 g/L) was significantly greater than in controls (21.9 ± 4.4 g/L; P patient per day). We conclude that routine supplementation of 5% human albumin to maintain a serum albumin level ≥ 20 g/L in burn patients is expensive and provides no benefit.

  20. Overestimation of Albumin Measured by Bromocresol Green vs Bromocresol Purple Method: Influence of Acute-Phase Globulins.

    Science.gov (United States)

    Garcia Moreira, Vanessa; Beridze Vaktangova, Nana; Martinez Gago, Maria Dolores; Laborda Gonzalez, Belen; Garcia Alonso, Sara; Fernandez Rodriguez, Eloy

    2018-05-22

    Usually serum albumin is measured with dye-binding assay as bromocresol green (BCG) and bromocresol purple (BCP) methods. The aim of this paper was to examine the differences in albumin measurements between the Advia2400 BCG method (AlbBCG), Dimension RxL BCP (AlbBCP) and capillary zone electrophoresis (CZE). Albumin concentrations from 165 serum samples were analysed using AlbBCG, AlbBCP and CZE. CZE was employed to estimate different serum protein fractions. Influence of globulins on albumin concentration discrepancies between methods was estimated as well as the impact of the albumin method on aCa concentrations. Medcalc was employed for statistical analysis, setting a value of P albumin concentrations. AlbBCG were positively biased versus CZE (3.54 g/L). There was good agreement between CZE and ALbBCP (Albumin results from the BCP and BCG methods may result in unacceptable differences and clinical confusion, especially at lower albumin concentrations. Serum acute phase proteins contribute to overestimating the albumin concentration using AlbBCG.

  1. Location and characterization of the warfarin binding site of human serum albumin A comparative study of two large fragments

    NARCIS (Netherlands)

    Bos, O.J.M.; Remijn, J.P.M.; Fischer, M.J.E.; Wilting, J.; Janssen, L.H.M.

    1988-01-01

    The warfarin binding behaviour of a large tryptic fragment (residues 198–585 which comprise domains two and three) and of a large peptic fragment (residues 1–387 which comprise domains one and two) of human serum albumin has been studied by circular dichroism and equilibrium dialysis in order to

  2. Interaction between Saikosaponin D, Paeoniflorin, and Human Serum Albumin.

    Science.gov (United States)

    Liang, Guo-Wu; Chen, Yi-Cun; Wang, Yi; Wang, Hong-Mei; Pan, Xiang-Yu; Chen, Pei-Hong; Niu, Qing-Xia

    2018-01-27

    Saikosaponin D (SSD) and paeoniflorin (PF) are the major active constituents of Bupleuri Radix and Paeonia lactiflora Pall , respectively, and have been widely used in China to treat liver and other diseases for many centuries. We explored the binding of SSD/PF to human serum albumin (HSA) by using fluorospectrophotometry, circular dichroism (CD) and molecular docking. Both SSD and PF produced a conformational change in HSA. Fluorescence quenching was accompanied by a blue shift in the fluorescence spectra. Co-binding of PF and SSD also induced quenching and a conformational change in HSA. The Stern-Volmer equation showed that quenching was dominated by static quenching. The binding constant for ternary interaction was below that for binary interaction. Site-competitive experiments demonstrated that SSD/PF bound to site I (subdomain IIA) and site II (subdomain IIIA) in HSA. Analysis of thermodynamic parameters indicated that hydrogen bonding and van der Waals forces were mostly responsible for the binary association. Also, there was energy transfer upon binary interaction. Molecular docking supported the experimental findings in conformation, binding sites and binding forces.

  3. Formation and Properties of Multilayer Films Based on Polyethyleneimine and Bovine Serum Albumin

    Science.gov (United States)

    Kulikouskaya, V. I.; Lazouskaya, M. E.; Kraskouski, A. N.; Agabekov, V. E.

    2018-01-01

    (Polyethyleneimine/bovine serum albumin) n ((PEI/BSA) n) multilayer films ( n = 1-10) are produced via the layer-by-later deposition of polyelectrolytes. It is shown that thickness and morphology of the formed coatings can be controlled by varying the solution's ionic strength during alternating adsorption of the components. (PEI/BSA)10 multilayer systems that contain up to 0.6 mg of antiseptic miramistin per 1 cm2 of film were created. It is established that the kinetics of miramistin release from (PEI/BSA)10 films in phosphate buffers and physiological solutions obey the Korsmeyer-Peppas equation with a high degree of accuracy ( R 2 > 0.95).

  4. Investigation of the topological shape of bovine serum albumin in solution by small-angle x-ray scattering at Beijing synchrotron radiation facility

    International Nuclear Information System (INIS)

    Dong Shuqiang; Chen Ximeng; Li Liqin; Liu Peng; Dong Yuhui

    2008-01-01

    This paper reports that at a newly constructed small-angle x-ray scattering station of Beijing Synchrotron Radiation Facility, the topological shape of ligand-free bovine serum albumin in solution has been investigated. An appropriate scattering curve is obtained and the calculated value of the gyration radius is 31.2ű0.25A (1Å=0.1 nm) which is coincident with other ones' results. It finds that the low-resolution structure models obtained by making use of ab initio reconstruction methods are fitting the crystal structure of human serum albumin very well. All of these results perform the potential of the beamline to apply to structural biology studies. The characteristics, the defects, and the improving measures of the station in future are also discussed. (condensed matter: structure, thermal and mechanical properties)

  5. Clinical usefulness of Tc-99M pertechnetate per-rectal portal scintigraphy in evaluation the severity of portal hypertension in cirrhotic patients

    International Nuclear Information System (INIS)

    Namwongprom, S.; Ekmahachai, M.; Boonyaprapa, S.; Vilasdechanon, N.; Taya, P.; Chankaew, N.; Chitapanarux, T.

    2004-01-01

    Objectives: Variceal hemorrhage is a potentially life-threatening complication in cirrhotic patients. Identification of patients at high risk for bleeding is particularly important. The aim of this study was to determine the clinical usefulness of per-rectal portal scintigraphy in evaluation the severity of portal hypertension in cirrhotic patients in terms of correlation between cirrhosis and classic indicators of hepatic functional reserve and identifying the difference of the portal shunt index (PSI) of the bleeding esophageal varices group and non-bleeding esophageal varices group. Material and methods: Portal circulations in 15 healthy volunteer's and in 67 patients with cirrhosis were evaluated by Tc-99m pertechnetate per-rectal p. ortal scintigraphy. Tc-99m pertechnetate (550 MBq) was instilled into the upper rectum, and dynamic images were taken. Radioactivity curves of the liver and the heart were generated sequentially. Through the analysis of these curves, the PSI was determined by calculating the ratio of counts of the liver to counts of the heart integrated for 24 seconds immediately after the appearance of the liver time-activity curve. Results: The results, expressed as PSI were: 13.63 +/- 6.28 % in healthy subjects and 66.32+/-22.80 % in cirrhotic patients. Of these, the PSIs were 56036 +/- 27.14 % in 31 cirrhotic patients without esophageal varices, and 74.89 +/- 13.62 % in 36 cirrhotic patients with esophageal varices. The PSI was significantly lower in cirrhotic patients without bleeding esophageal vances (BEV) than those with BEV (p=0.001). The PSI calculated with this method was correlated with the serum albumin, the serum bilirubin and the Child-Pugh's score. Conclusion: The Tc-99m pertechnetate per-rectal portal scintigraphy has clinical usefulness as a relatively non-invasive method of choice for quantitative evaluating the severity of portal hypertension in cirrhotic patients. (authors)

  6. Characterizing Active Pharmaceutical Ingredient Binding to Human Serum Albumin by Spin-Labeling and EPR Spectroscopy.

    Science.gov (United States)

    Hauenschild, Till; Reichenwallner, Jörg; Enkelmann, Volker; Hinderberger, Dariush

    2016-08-26

    Drug binding to human serum albumin (HSA) has been characterized by a spin-labeling and continuous-wave (CW) EPR spectroscopic approach. Specifically, the contribution of functional groups (FGs) in a compound on its albumin-binding capabilities is quantitatively described. Molecules from different drug classes are labeled with EPR-active nitroxide radicals (spin-labeled pharmaceuticals (SLPs)) and in a screening approach CW-EPR spectroscopy is used to investigate HSA binding under physiological conditions and at varying ratios of SLP to protein. Spectral simulations of the CW-EPR spectra allow extraction of association constants (KA ) and the maximum number (n) of binding sites per protein. By comparison of data from 23 SLPs, the mechanisms of drug-protein association and the impact of chemical modifications at individual positions on drug uptake can be rationalized. Furthermore, new drug modifications with predictable protein binding tendency may be envisaged. © 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

  7. Relationship between bone scintigraphy and tumor markers in patients with breast cancer

    International Nuclear Information System (INIS)

    Yildiz, M.; Oral, B.

    2004-01-01

    The aim of this study is to specify the precise role of bone scintigraphy and serum carcinoembryonic antigen (CEA) and breast cancer-associated antigen (CA) 15-3 assays in the monitoring of breast cancers in order to optimize their use and to determine whether it is possible to guide the prescription of bone scan by the use of CEA and CA 15-3 assays in the monitoring of breast cancer. For this purpose, from November 1997 to May 2002, 98 consecutive female breast cancer patients (median age, 52 years; range 35-77 years) underwent bone scintigraphy during follow-up. In these patients values of tumor markers were compared with the results of bone scintigraphy. Some of the patients with bone metastasis were checked repeatedly at intervals of 6 to 12 months, resulting in 49 patients with bone metastasis and 74 patients without bone metastasis being included in the study. In patients with bone metastasis, serum CEA levels were abnormal in 23/49 cases and CA 15-3 serum concentrations were elevated above the cut-off in 33/49 cases. Among patients without bone metastasis, CEA and CA 15-3 serum concentrations were normal in 50/74 and 55/74 cases respectively. The combination of the two markers improved the diagnostic sensitivity. Although serial tumor marker measurements are an efficient and cost effective method of monitoring disease progression, it does not allow prediction of the bone scan results; so it is not justifiable to reject a bone scintigraphy on the basis of these markers. (author)

  8. Changes in the pharmacokinetics of teicoplanin in patients with hyperglycaemic hypoalbuminaemia: Impact of albumin glycosylation on the binding of teicoplanin to albumin.

    Science.gov (United States)

    Enokiya, Tomoyuki; Muraki, Yuichi; Iwamoto, Takuya; Okuda, Masahiro

    2015-08-01

    There is large interindividual variability in serum teicoplanin (TEIC) concentrations after administration of a loading dose, and the factors that influence the pharmacokinetics of TEIC are disputed. The aim of this study was to clarify changes in the pharmacokinetics of TEIC that occur in patients with hyperglycaemia as well as the impact of albumin glycosylation on the pharmacokinetics of TEIC. This study consisted of retrospective and prospective investigations. The pharmacokinetic parameters of TEIC were retrospectively compared between patients receiving TEIC treatment. Ninety-four patients were divided into four groups according to their serum albumin and blood glucose concentrations [(i) hyperglycaemic hypoalbuminaemia (albuminalbumin≥3.0g/dL) (n=9); and (iv) non-hyperglycaemic normoalbuminaemia (n=40)]. In addition, the concentration of glycosylated albumin was prospectively determined in 28 patients. At 12h after administration of a loading dose, patients with hyperglycaemic hypoalbuminaemia displayed significantly lower serum TEIC concentrations (Palbumin was significantly correlated with the association constant (Ka) of TEIC for albumin (r=0.53, P=0.004) and the Vd (r=0.41, P=0.031). These results suggest that hyperglycaemic hypoalbuminaemia lowers the serum TEIC concentration, which is attributable to the decreased Ka and increased Vd of TEIC by albumin glycosylation. Copyright © 2015 Elsevier B.V. and the International Society of Chemotherapy. All rights reserved.

  9. LOCALIZATION OF POLYSOME-BOUND ALBUMIN AND SERINE DEHYDRATASE IN RAT LIVER CELL FRACTIONS

    Science.gov (United States)

    Ikehara, Yukio; Pitot, Henry C.

    1973-01-01

    The polysomes involved in albumin and serine dehydratase synthesis were identified and localized by the binding to rat liver polysomes of anti-rat serum albumin and anti-serine dehydratase [125I]Fab dimer and monomer. Techniques were developed for the isolation of undegraded free and membrane-bound polysomes and for the preparation of [125I]Fab monomers and dimers from the IgG obtained from the antisera to the two proteins, rat serum albumin and serine dehydratase. The distribution of anti-rat serum albumin [125I]Fab dimer in the polysome profile is in accordance with the size of polysomes that are expected to be synthesizing albumin. By direct precipitation, it has been demonstrated that nascent chains isolated from the membrane-bound polysomes by puromycin were precipitated by anti-rat serum albumin-IgG at a level of 5–6 times those released from free polysomes. Anti-rat serum albumin-[125I]Fab dimer reacted with membrane-bound polysomes almost exclusively compared to the binding of nonimmune, control [125I]Fab dimer; a significant degree of binding of anti-rat serum albumin-[125I]Fab to free polysomes was also obtained. The [125I]Fab dimer made from normal control rabbit serum does not react with polysomes from liver at all and this preparation will not interact with polysomes extracted from tissues that do not synthesize rat serum albumin. Both anti-serine dehydratase-[125I]Fab monomer and dimer react with free and bound polysomes from livers of animals fed a chow diet or those fed a high 90% protein diet and given glucagon. In the latter instance, however, it is clear that the majority of the binding occurs to the bound polysomes. Furthermore, the specificity of this reaction may be further shown by the use of kidney polysomes that do not normally synthesize serine dehydratase. When these latter polysomes are isolated, even after the addition of crude and purified serine dehydratase, no reaction with anti-serine dehydratase-Fab fragments could be

  10. Preparation and radiolabeling of human serum albumin (HSA)-coated magnetite nanoparticles for magnetically targeted therapy

    International Nuclear Information System (INIS)

    Zhang Chunfu; Cao Jinquan; Yin Duanzhi; Wang Yongxian; Feng Yanlin; Tan Jiajue

    2004-01-01

    In this paper, we describe the preparation of human serum albumin-coated magnetic particles of about 200 nm in diameter with narrow size distribution radiolabeled with 188 Re for the purpose of magnetically targeted therapy. The optimum radiolabeling conditions are: SnCl 2 ·2H 2 O 8 mg/ml, citric acid 20 mg/ml, vitamin C 8 mg/ml, labeling volume 500 μl and a reaction time of 3 h. The stability of the radiolabeled particles is suitable for in vivo study

  11. Ligand-Modified Human Serum Albumin Nanoparticles for Enhanced Gene Delivery.

    Science.gov (United States)

    Look, Jennifer; Wilhelm, Nadine; von Briesen, Hagen; Noske, Nadja; Günther, Christine; Langer, Klaus; Gorjup, Erwin

    2015-09-08

    The development of nonviral gene delivery systems is a great challenge to enable safe gene therapy. In this study, ligand-modified nanoparticles based on human serum albumin (HSA) were developed and optimized for an efficient gene therapy. Different glutaraldehyde cross-linking degrees were investigated to optimize the HSA nanoparticles for gene delivery. The peptide sequence arginine-glycine-aspartate (RGD) and the HIV-1 transactivator of transduction sequence (Tat) are well-known as promising targeting ligands. Plasmid DNA loaded HSA nanoparticles were covalently modified on their surface with these different ligands. The transfection potential of the obtained plasmid DNA loaded RGD- and Tat-modified nanoparticles was investigated in vitro, and optimal incubation conditions for these preparations were studied. It turned out that Tat-modified HSA nanoparticles with the lowest cross-linking degree of 20% showed the highest transfection potential. Taken together, ligand-functionalized HSA nanoparticles represent promising tools for efficient and safe gene therapy.

  12. Interactions of human serum albumin with doxorubicin in different media

    Science.gov (United States)

    Gun'ko, Vladimir M.; Turov, Vladimir V.; Krupska, Tetyana V.; Tsapko, Magdalina D.

    2017-02-01

    Interactions of human serum albumin (10 wt% H2O and 0.3 wt% sodium caprylate) with doxorubicin hydrochloride (1 wt%) were studied alone or with addition of HCl (3.6 wt% HCl) using 1H NMR spectroscopy. A model of hydrated HSA/12DOX was calculated using PM7 method with COSMO showing large variations in the binding constant depending on structural features of DOX/HSA complexes. DOX molecules/ions displace bound water from narrow intramolecular voids in HSA that leads to diminution of freezing-melting point depression of strongly bound water (SBW). Structure of weakly bound water (WBW) depends much weaker on the presence of DOX than SBW because a major fraction of DOX is bound to adsorption sites of HSA. Addition of HCl results in strong changes in structure of macromolecules and organization of water in hydration shells of HSA (i.e., mainly SBW) and in the solution (i.e., WBW + non-bound bulk water).

  13. Experimental and theoretical investigation of bezafibrate binding to serum albumins

    Energy Technology Data Exchange (ETDEWEB)

    Gałęcki, Krystian, E-mail: kgalecki87@gmail.com [Technical University of Lodz, Lodz (Poland); Hunter, Kelsey [Glasgow Caledonian University, Glasgow, Scotland (United Kingdom); Daňková, Gabriela [Masarykova Univerzita, Brno (Czech Republic); Rivera, Elsy [University of Houston-Downtown, Houston (United States); Tung, Lo Wing [The Hong Kong Polytechnic University (Hong Kong); Mc Sherry, Kenneth [Trinity College Dublin, Dublin (Ireland)

    2016-09-15

    The purpose of this investigation was to provide insight into the possible mechanism of the intermolecular interactions between antilipemic agent bezafibrate and serum albumins (SAs) including human (HSA) and bovine (BSA). The aim was to indicate the most probable sight of these interactions. Both experimental (spectroscopic) and theoretical methods were applied. It was determined that bezafibrate binds to SAs in one specific binding site, the fatty acid binding site 6. The results obtained from the steady-state and time-resolved fluorescence experiments suggested that existing two distinct stable conformations of the proteins with different exposure to the quencher. The dominate conformer of HSA and BSA characterized by the Stern–Volmer quenching constant (from ratio F{sub 0}/F) equal to 1.24·10{sup 4} and 8.48·10{sup 3} M{sup −1} at 298 K, respectively. The docking results and calculated thermodynamics parameters may be suggested that the binding process is spontaneous and might involve van der Waals and hydrogen bonding forces.

  14. Serum albumin is an important prognostic factor for carotid blowout syndrome

    International Nuclear Information System (INIS)

    Lu Hsuehju; Chen Kuowei; Chen Minghuang; Tzeng Chenghwai; Chang Peter Muhsin; Yang Muhhwa; Chu Penyuan; Tai Shyhkuan

    2013-01-01

    Carotid blowout syndrome is a severe complication of head and neck cancer. High mortality and major neurologic morbidity are associated with carotid blowout syndrome with massive bleeding. Prediction of outcomes for carotid blowout syndrome patients is important for clinicians, especially for patients with the risk of massive bleeding. Between 1 January 2001 and 31 December 2011, 103 patients with carotid blowout syndrome were enrolled in this study. The patients were divided into groups with and without massive bleeding. Prognostic factors were analysed with proportional hazard (Cox) regressions for carotid blowout syndrome-related prognoses. Survival analyses were based on the time from diagnosis of carotid blowout syndrome to massive bleeding and death. Patients with massive bleeding were more likely to have hypoalbuminemia (albumin 1000 cells/μl, P=0.041) and hypoalbuminemia (P=0.010) were important to prognosis. Concurrent chemoradiotherapy (P=0.007), elevated lactate dehydrogenase (>250 U/l; P=0.050), local recurrence (P=0.022) and hypoalbuminemia (P=0.038) were related to poor prognosis in carotid blowout syndrome-related death. In multivariate analysis, best supportive care and hypoalbuminemia were independent factors for both carotid blowout syndrome-related massive bleeding (P=0.000) and carotid blowout syndrome-related death (P=0.013), respectively. Best supportive care and serum albumin are important prognostic factors in carotid blowout syndrome. It helps clinicians to evaluate and provide better supportive care for these patients. (author)

  15. Twenty cases of ectopic thyroid gland detected by thyroid scintigraphy

    International Nuclear Information System (INIS)

    Hashimoto, Teisuke; Kubo, Atsushi; Hashimoto, Shozo

    1988-01-01

    20 cases of ectopic thyroid gland were detected out of 5,261 thyroid scintigraphy from 1973. Except for 1 case, all cases were female. Considering of thyroid function, 11 cases were euthyroid and rest of 9 cases were hypothyroid function. Clinical symptom of hypothyroid cases were mainly retarded linear growth and high value of serum TSH and in case of euthyroid cases were sublingual tumor and fullness or tightness in throat. Thyroid scintigraphy is very useful to diagnose the sublingual tumor whether it is ectopic thyroid gland or not. In case of congenital hypothyroidism children, ectopic thyroid gland causing hypothyroidism is definitely diagnosed by thyroid scintigraphy. (author)

  16. Relationship between urine albumin and endothelin in children with anaphylactoid purpura

    International Nuclear Information System (INIS)

    Duan Yongqiang; Chen Nianfa

    2009-01-01

    To study the function of urine albumin and endothelin (ET-1) in the occurrence and progress of ansphylactoid purura (HSP) and anaphylaxis purura nephritis (HSPN) in children, the serum level of ET-1 and urine albumin excretion rate in 29 children with HSP and 21 normal controls was detected by RIA and salicylic acid nephelometry respectively. The results showed that the content of urine albumin in 24 hours in HSP group has no significant difference compared with that of control group (P>0.05) , but the corresponding content in HSPN group has significant difference compared with that of control and HSP group (P<0.01). The serum ET-1 in HSP group has significant difference compared with control group (P<0.05), and the corresponding content in HSPN group has significant difference compared with control group and HSP group (P<0.01, P<0.05). The levels of urine albumin of 24 hours and serum ET-1 in HSPN group after treatment were decreased obviously compared with those before treatment (P<0.01). The content of urine albumin of 24 hours was positively correlated with serum levels of ET-1. The ET-1 participated the formation of HSP and HSPN, and was related to the occurrence and progress of urine albumin. (authors)

  17. The impact of the treatment method on intradialytic intercurrences and serum levels of hemoglobin, calcium and albumin of the person with chronic kidney disease

    Directory of Open Access Journals (Sweden)

    JOAQUIM CARREIRA

    2016-12-01

    Full Text Available ABSTRACT: Introdution: The high prevalence of chronic kidney disease has led to the development of renal function replacement techniques as a treatment for individuals with the disease. Hemodialysis (HD is the most commonly used method for the treatment of patients with the disease. Even if it has improved a lot, the intercurrences during dialysis continue to be a reality. The literature is not consensual when it relates the modalities of treatment and the benefits and harms associated with them. If on the one hand there is evidence that hemodiafiltration (HDF has fewer implications for patients than hemodialysis, others do not show significant differences when comparing the two treatment modalities. Methods: A prospective, comparative, quasi-experimental study was developed over a period of 8 months to determine if there were differences in the number of intercurrences and serum levels of calcium, albumin and hemoglobin observed in each treatment modality, HD versus HDF. Results and discussion: The data obtained show that there are no statistically significant differences in the number of intercurrences and serum levels of calcium, albumin and hemoglobin observed in each treatment modality. Conclusions: It was not possible to determine which of the treatment modalities is associated with major/minor intradialytic intercurrences or serum levels of hemoglobin, calcium and albumin.

  18. Production and characterization of monoclonal antibodies (mAbs) against human serum albumin (HSA) for the development of an immunoaffinity system with oriented anti-HSA mAbs as immobilized ligand.

    Science.gov (United States)

    Rajak, Poonam; Vijayalakshmi, M A; Jayaprakash, N S

    2013-05-05

    Proteins present in human serum are of immense importance in the field of biomarker discovery. But, the presence of high-abundant proteins like albumin makes the analysis more challenging because of masking effect on low-abundant proteins. Therefore, removal of albumin using highly specific monoclonal antibodies (mAbs) can potentiate the discovery of low-abundant proteins. In the present study, mAbs against human serum albumin (HSA) were developed and integrated in to an immunoaffinity based system for specific removal of albumin from the serum. Hybridomas were obtained by fusion of Sp2/0 mouse myeloma cells with spleen cells from the mouse immunized with HSA. Five clones (AHSA1-5) producing mAbs specific to HSA were established and characterized by enzyme linked immunosorbent assay (ELISA) and immunoblotting for specificity, sensitivity and affinity in terms of antigen binding. The mAbs were able to bind to both native albumin as well as its glycated isoform. Reactivity of mAbs with different mammalian sera was tested. The affinity constant of the mAbs ranged from 10(8) to 10(9)M(-1). An approach based on oriented immobilization was followed to immobilize purified anti-HSA mAbs on hydrazine activated agarose gel and the dynamic binding capacity of the column was determined. Copyright © 2013 Elsevier B.V. All rights reserved.

  19. Serum albumin binding sites properties in donors and in schizophrenia patients: the study of fluorescence decay of the probe K-35 using S-60 synchrotron pulse excitation

    Energy Technology Data Exchange (ETDEWEB)

    Gryzunov, Y.A. E-mail: grysunov@sci.lebedev.ru; Syrejshchikova, T.I.; Komarova, M.N.; Misionzhnik, E.Yu.; Uzbekov, M.G.; Molodetskich, A.V.; Dobretsov, G.E.; Yakimenko, M.N

    2000-06-21

    The properties of serum albumin obtained from donors and from paranoid schizophrenia patients were studied with the fluorescent probe K-35 (N-carboxyphenylimide of dimethylaminonaphthalic acid) and time-resolved fluorescence spectroscopy on the SR beam station of the S-60 synchrotron of the Lebedev Physical Institute. The mean fluorescence quantum yield of K-35 in patients serum was decreased significantly by 25-60% comparing with donors. The analysis of pre-exponential factors of fluorescence decay using 'amplitude standard' method has shown that in patient sera the fraction of K-35 molecules bound with albumin and inaccessible to fluorescence quenchers ('bright' K-35 molecules with {tau}{sub 1}=8.0{+-}0.4 ns) is 1.2-3 times less than in the donor sera. The fraction of K-35 molecules with partly quenched fluorescence ({tau}{sub 2}=1.44{+-}0.22 ns) was significantly increased in schizophrenia patients. The results obtained suggest that the properties of binding region in serum albumin molecules of acute paranoid schizophrenia patients change significantly.

  20. Serum albumin binding sites properties in donors and in schizophrenia patients: the study of fluorescence decay of the probe K-35 using S-60 synchrotron pulse excitation

    International Nuclear Information System (INIS)

    Gryzunov, Y.A.; Syrejshchikova, T.I.; Komarova, M.N.; Misionzhnik, E.Yu.; Uzbekov, M.G.; Molodetskich, A.V.; Dobretsov, G.E.; Yakimenko, M.N.

    2000-01-01

    The properties of serum albumin obtained from donors and from paranoid schizophrenia patients were studied with the fluorescent probe K-35 (N-carboxyphenylimide of dimethylaminonaphthalic acid) and time-resolved fluorescence spectroscopy on the SR beam station of the S-60 synchrotron of the Lebedev Physical Institute. The mean fluorescence quantum yield of K-35 in patients serum was decreased significantly by 25-60% comparing with donors. The analysis of pre-exponential factors of fluorescence decay using 'amplitude standard' method has shown that in patient sera the fraction of K-35 molecules bound with albumin and inaccessible to fluorescence quenchers ('bright' K-35 molecules with τ 1 =8.0±0.4 ns) is 1.2-3 times less than in the donor sera. The fraction of K-35 molecules with partly quenched fluorescence (τ 2 =1.44±0.22 ns) was significantly increased in schizophrenia patients. The results obtained suggest that the properties of binding region in serum albumin molecules of acute paranoid schizophrenia patients change significantly

  1. Serum albumin binding sites properties in donors and in schizophrenia patients: the study of fluorescence decay of the probe K-35 using S-60 synchrotron pulse excitation

    Science.gov (United States)

    Gryzunov, Yu. A.; Syrejshchikova, T. I.; Komarova, M. N.; Misionzhnik, E. Yu; Uzbekov, M. G.; Molodetskich, A. V.; Dobretsov, G. E.; Yakimenko, M. N.

    2000-06-01

    The properties of serum albumin obtained from donors and from paranoid schizophrenia patients were studied with the fluorescent probe K-35 (N-carboxyphenylimide of dimethylaminonaphthalic acid) and time-resolved fluorescence spectroscopy on the SR beam station of the S-60 synchrotron of the Lebedev Physical Institute. The mean fluorescence quantum yield of K-35 in patients serum was decreased significantly by 25-60% comparing with donors. The analysis of pre-exponential factors of fluorescence decay using "amplitude standard" method has shown that in patient sera the fraction of K-35 molecules bound with albumin and inaccessible to fluorescence quenchers ("bright" K-35 molecules with τ1=8.0±0.4 ns) is 1.2-3 times less than in the donor sera. The fraction of K-35 molecules with partly quenched fluorescence ( τ2=1.44±0.22 ns) was significantly increased in schizophrenia patients. The results obtained suggest that the properties of binding region in serum albumin molecules of acute paranoid schizophrenia patients change significantly.

  2. Proximal Tubules Have the Capacity to Regulate Uptake of Albumin.

    Science.gov (United States)

    Wagner, Mark C; Campos-Bilderback, Silvia B; Chowdhury, Mahboob; Flores, Brittany; Lai, Xianyin; Myslinski, Jered; Pandit, Sweekar; Sandoval, Ruben M; Wean, Sarah E; Wei, Yuan; Satlin, Lisa M; Wiggins, Roger C; Witzmann, Frank A; Molitoris, Bruce A

    2016-02-01

    Evidence from multiple studies supports the concept that both glomerular filtration and proximal tubule (PT) reclamation affect urinary albumin excretion rate. To better understand these roles of glomerular filtration and PT uptake, we investigated these processes in two distinct animal models. In a rat model of acute exogenous albumin overload, we quantified glomerular sieving coefficients (GSC) and PT uptake of Texas Red-labeled rat serum albumin using two-photon intravital microscopy. No change in GSC was observed, but a significant decrease in PT albumin uptake was quantified. In a second model, loss of endogenous albumin was induced in rats by podocyte-specific transgenic expression of diphtheria toxin receptor. In these albumin-deficient rats, exposure to diphtheria toxin induced an increase in albumin GSC and albumin filtration, resulting in increased exposure of the PTs to endogenous albumin. In this case, PT albumin reabsorption was markedly increased. Analysis of known albumin receptors and assessment of cortical protein expression in the albumin overload model, conducted to identify potential proteins and pathways affected by acute protein overload, revealed changes in the expression levels of calreticulin, disabled homolog 2, NRF2, angiopoietin-2, and proteins involved in ATP synthesis. Taken together, these results suggest that a regulated PT cell albumin uptake system can respond rapidly to different physiologic conditions to minimize alterations in serum albumin level. Copyright © 2016 by the American Society of Nephrology.

  3. Correlation Between Bone Scintigraphy and Tumor Markers in Patients with Breast Carcinoma

    Directory of Open Access Journals (Sweden)

    Amela Begić

    2006-02-01

    Full Text Available A characteristic feature of many cancer types is their ability to metastasise to the skeleton. Bone is the most common site of metastatic invasion, after hematogenous spreading of breast cancer. Early detection of bone metastases is mandatory in the evaluation and management of these patients. Bone scintigraphy is commonly performed in detection and evaluation bone metastases. Tumor markers are present in healthy individuals as well as in patients with malignant diseases but in different concentration. Aim of study was to correlate serum levels of tumor marker Ca (15-3, CEA and presence of bone metastases detected by bone scintigraphy. Study included 25 patients with breast cancer, previously surgically treated. All patients underwent whole body scintigraphy. Ca (15-3 and CEA was measured by radioimmunoassay. Presence, number of bone metastases were correlated with Ca (15-3 and CEA levels. Median age of patients included in study was 50 varying from 30 to 67. Bone scintigraphy revealed bone metastases in 16 (64% patients. A weak correlation was found between number of metastases and level of Ca (15-3 (r=0.139, p=0.254. Significant differences in Ca (15-3 level was found in patient with metastases compared to patients without metastases (chi square 0, p=1.0. Good correlation was found between number of metastases and serum level of CEA. Correlation between level of two tumor markers Ca (15-3 and CEA was a weak (r = 0.096 , p=0.323. Bone scintigraphy is a sensitive diagnostic toll for detecting breast cancer metastases to bone. Serum levels of tumor markes in isolation can not give complete accuracy about bone metastases.

  4. An albumin-fixed membrane for the removal of protein-bound toxins

    International Nuclear Information System (INIS)

    Ge Dongtao; Wu Dewang; Shi Wei; Ma Yuanyuan; Tian Xiangdong; Liang Pengfei; Zhang Qiqing

    2006-01-01

    Established methods for kidney dialysis do not work for liver failure because kidney dialysis removes only water-soluble toxins, while the liver normally removes albumin-bound toxins. In the present study, a polysulfone dialysis membrane with a -OH reactive group was prepared by hydrolyzing the chloromethylated polysulfone membrane, and the bovine serum albumin molecules were fixed into the membrane with 1,1'-carbonyldiimidazole activation. The content of albumin of the albumin-fixed membrane was 121.3 mg (g membrane) -1 . The albumin-fixed dialysis membranes were used to remove protein-bound toxins, bilirubin, from the bilirubin-albumin solution. The transfer rate of bilirubin of the albumin-fixed membrane was obviously higher compared to the normal dialysis membrane. The clearance of bilirubin with the albumin-fixed membrane was 49.8%. The albumin-fixed membrane can easily be regenerated by the bovine serum albumin and NaOH solution. Regeneration of the membrane suggested good mechanical and chemical stability, as well as good clearance of bilirubin. In addition, the effects of membrane thickness and bilirubin initial concentration on the removal of bilirubin were discussed

  5. Low serum albumin may predict the need for gastric resection in patients with perforated peptic ulcer.

    Science.gov (United States)

    Seow, J G; Lim, Y R; Shelat, V G

    2017-06-01

    Perforated peptic ulcer (PPU) is a common surgical emergency and treatment involves omental patch repair (PR). Gastric resection (GR) is reserved for difficult pathologies. We audit the outcomes of GR at our institution and evaluate the pre-operative factors predicting the need for GR. This is a single-institution, retrospective study of patients with PPU who underwent surgery from 2004 to 2012. Demographics, clinical presentation and intra-operative findings were studied to identify factors predicting the need for GR in PPU. An audit of clinical outcomes and mortality for all patients with GR is reported. 537 (89.6 %) patients underwent PR and 62 (10.4 %) patients GR. Old age (p peptic ulcer disease (PUD) (p = 0.0159), low hemoglobin (p ulcer size (p < 0.0001) predict the need for GR. On multivariate analysis only low serum albumin (OR 5.57, 95 % CI 1.56-19.84, p = 0.008) predicted the need for GR. The presence of Helicobacter pylori infection was protective against GR (OR 0.25, 95 %CI 0.14-0.44, p < 0.0001). Morbidity and mortality of GR was 27.7 and 24.2 %, respectively. GR is needed in one in ten cases of PPU. Low serum albumin predicted the need for GR on multivariate analysis. Morbidity and mortality of GR remains high.

  6. Binding of the neuroleptic drug, gabapentin, to bovine serum albumin: Insights from experimental and computational studies

    International Nuclear Information System (INIS)

    Jalali, Fahimeh; Dorraji, Parisa S.; Mahdiuni, Hamid

    2014-01-01

    The interaction between antiepileptic drug, gabapentin (GP), and bovin serum albumin (BSA) was studied by spectroscopic and computational methods. The native fluorescence of BSA was quenched by GP. Stern–Volmer quenching constant was calculated at different temperatures which suggested a static mechanism. The association constant (K a ) was calculated from fluorescence quenching studies, which increased with temperature rising. GP competed well with warfarine for hydrophobic subdomain IIA (Sudlow's site I) on the protein. Enthalpy and entropy changes during the interaction of GP with BSA were obtained using van't Hoff plot, which showed an entropy-driven process and involvement of hydrophobic forces (ΔH>0 and ΔS>0). Synchronous fluorescence measurements of BSA solution in the presence of GP showed a considerable blue shift when Δλ=15 nm, therefore, GP interacts with tyrosine-rich sites on BSA. Optimized docked model of BSA–GP mixture confirmed the experimental results. -- Highlights: • Interaction of gabapentin and bovine serum albumin (BSA) is investigated by spectroscopic techniques. • Gabapentin can quench the fluorescence of BSA through a static quenching procedure. • The binding of gabapentin to BSA is driven mainly by hydrophobic interactions. • Subdomain IIA (Sudlow's site I) of BSA is found to be the main binding site for gabapentin. • Molecular docking modeling confirmed the experimental results

  7. Preparation and radiolabeling of human serum albumin (HSA)-coated magnetite nanoparticles for magnetically targeted therapy

    Energy Technology Data Exchange (ETDEWEB)

    Zhang Chunfu E-mail: zchunfu@yahoo.com.cn; Cao Jinquan; Yin Duanzhi; Wang Yongxian; Feng Yanlin; Tan Jiajue

    2004-12-01

    In this paper, we describe the preparation of human serum albumin-coated magnetic particles of about 200 nm in diameter with narrow size distribution radiolabeled with {sup 188}Re for the purpose of magnetically targeted therapy. The optimum radiolabeling conditions are: SnCl{sub 2}{center_dot}2H{sub 2}O 8 mg/ml, citric acid 20 mg/ml, vitamin C 8 mg/ml, labeling volume 500 {mu}l and a reaction time of 3 h. The stability of the radiolabeled particles is suitable for in vivo study.

  8. Pre-Clinical Intravenous Serum Pharmacokinetics of Albumin Binding and Non-Half-Life Extended Nanobodies®

    Directory of Open Access Journals (Sweden)

    Sven Hoefman

    2015-07-01

    Full Text Available Nanobodies are antigen-binding, single variable domain proteins derived from naturally-occurring, heavy chain only antibodies. They are highly soluble, stable, and can be linked to build multi-specific formats. Several Nanobodies are currently in clinical development in different therapeutic areas, for both chronic and acute applications. For the former, prolonged exposure is achieved by half-life extending moieties that target endogenous albumin, while for the latter, non-half-life extended constructs are preferable. To demonstrate the general pharmacokinetic behavior of both formats, serum levels of seven intravenously administered Nanobodies were analyzed in cynomolgus monkeys, mice or rabbits. In monkeys, the total clearance of a monomeric irrelevant Nanobody was rapid (2.0 mL/(min*kg and approximated the species glomerular filtration rate, indirectly suggesting that the Nanobody was mainly eliminated via the kidneys. When linked to an anti-albumin Nanobody, a 376-fold decrease in clearance was observed, resulting in a terminal half-life of 4.9 days, corresponding to the expected species albumin half-life. Similar conclusions were drawn for (non- half-life extended mono-, bi- and trimeric Nanobodies in mice or rabbits, suggesting that these kinetic principles apply across species. Applying this knowledge to species translation and study design is crucial for successful pre-clinical development of novel therapeutic Nanobody candidates.

  9. Variability of albumin in blood serum as a possible reflection of evolutional influence of diluvial horses on population of native mountain horse in Serbia

    Directory of Open Access Journals (Sweden)

    Trailović Ružica

    2013-01-01

    Full Text Available Native mountain horse is an autochthonous ungulata with a domicile extending to the whole mountaneous region of Serbia, south of the Sava and Danube rivers. Along with native horses of other Balkan countries it is classified as Mediterranean pony, but unlike Balkan horses such as Skiros, Pinea, Pindos, Karakachan, Bosnian mountineous horse etc., mountineous horses in Serbia neither have been morphologically described nor were of concern to the scientific community till the end of the twentieth century. Investigations of albumin polymorphism in blood serum of native mountain horse were taken within a comprehensive reserch on morphologic, physiologic and genetic structure of this autochtonous ungulata breed. On the basis of the results obtained by electrophoretic separation of albumine types in native mountaneous horse blood serum, there were determined four albumine phenotypes: AA, AB, BB and BI which are inherited by three autosomal alleles AlA, Alb, All . The appearance of All allele in native mountaneous horse population points out to diluvial forest horse impact on process of microevolution of autochtonous native mountaneous horse. Occidental- specific albumin isoforms presence indicate the necessity of thorough study of evolution position and historic influence of different ancestors, and especially occidental horses on native mountain horse population in Serbia.

  10. Investigation of interaction between alkoxy substituted phthalocyanines with different lengths of alkyl residue and bovine serum albumin

    Energy Technology Data Exchange (ETDEWEB)

    Lebedeva, Natalya Sh., E-mail: nsl@isc-ras.ru [G.A. Krestov Institute of Solution Chemistry of the Russian Academy of Sciences, Akademicheskaya, 1, 153045 Ivanovo (Russian Federation); Gubarev, Yury A.; Vyugin, Anatoly I. [G.A. Krestov Institute of Solution Chemistry of the Russian Academy of Sciences, Akademicheskaya, 1, 153045 Ivanovo (Russian Federation); Koifman, Oscar I. [Research Institute of Macroheterocycles of Ivanovo State University of Chemistry and Technology, 153000 Ivanovo (Russian Federation)

    2015-10-15

    Interaction between bovine serum albumin and alkoxy substituted phthalocyanines was studied by means of electron absorption spectroscopy, fluorescence spectroscopy and viscosimetry. The binding constants and binding distance were calculated. It was found that ZnPc(4-NH-CO-C{sub 6}H{sub 4}-OC{sub 10}H{sub 21}){sub 4} prevents twisting of BSA molecule and localizes between subdomains IB and IIA in protein globule. ZnPc(4-NH-CO-C{sub 6}H{sub 4}-OC{sub 6}H{sub 13}){sub 4} and ZnPc(4-NH-CO-C{sub 6}H{sub 4}-OC{sub 8}H{sub 17}){sub 4} are located on the outer surface of the protein globule. In the case of ZnPc(4-NH-CO-C{sub 6}H{sub 4}-OC{sub 3}H{sub 7}){sub 4} it can be assumed that the phthalocyanine molecule is in the immediate vicinity of the subdomains IB and IIA. - Highlights: • Interaction between bovine serum albumin and alkoxy substituted phthalocyanines was studied by means of electron absorption spectroscopy, fluorescence spectroscopy and viscosimetry. • The binding constants and binding distance were calculated by using the Scatchard method. • Photochemical characteristics of phthalocyanines of studied phthalocyanines are defined. • Localization of phthalocyanines on the protein globule is defined.

  11. Study of interactions of an anticancer drug neratinib with bovine serum albumin: Spectroscopic and molecular docking approach

    Science.gov (United States)

    Wani, Tanveer A.; Bakheit, Ahmed H.; Abounassif, M. A.; Zargar, Seema

    2018-03-01

    Binding of therapeutic agents to plasma proteins, particularly to serum albumin, provides valuable information in the drug development. This study was designed to evaluate the binding interaction of neratinib with bovine serum albumin (BSA). Neratinib blocks HER2 signaling and is effective in trastuzumab-resistant breast cancer treatment. Spectrofluorometric, UV spectrophotometric, and fourier transform infrared (FT-IR) and molecular docking experiments were performed to study this interaction. The fluorescence of BSA is attributed to the presence of tryptophan (Trp) residues. The fluorescence of BSA in presence of neratinib was studied using the excitation wavelength of 280 nm and the emission was measured at 300-500 nm at three different temperatures. Neratinib quenched the BSA intrinsic fluorescence by static mechanism. A complex formation occurred due to the interaction leading to BSA absorption shift. The fluorescence, UV- absorption, three dimensional fluorescence and FT-IR data showed conformational changes occurred in BSA after interaction with neratinib. The binding constant values decreased as the temperature increased suggesting an instable complex formation at high temperature. Site I (sub-domain IIA) was observed as the principal binding site for neratinib. Hydrogen bonding and Van der Waals forces were suggested to be involved in the BSA-neratinib interaction due to the negative values of entropy and enthalpy changes.

  12. Study of Interactions of an Anticancer Drug Neratinib With Bovine Serum Albumin: Spectroscopic and Molecular Docking Approach

    Directory of Open Access Journals (Sweden)

    Tanveer A. Wani

    2018-03-01

    Full Text Available Binding of therapeutic agents to plasma proteins, particularly to serum albumin, provides valuable information in the drug development. This study was designed to evaluate the binding interaction of neratinib with bovine serum albumin (BSA. Neratinib blocks HER2 signaling and is effective in trastuzumab-resistant breast cancer treatment. Spectrofluorometric, UV spectrophotometric, and fourier transform infrared (FT-IR and molecular docking experiments were performed to study this interaction. The fluorescence of BSA is attributed to the presence of tryptophan (Trp residues. The fluorescence of BSA in presence of neratinib was studied using the excitation wavelength of 280 nm and the emission was measured at 300-500 nm at three different temperatures. Neratinib quenched the BSA intrinsic fluorescence by static mechanism. A complex formation occurred due to the interaction leading to BSA absorption shift. The fluorescence, UV- absorption, three dimensional fluorescence and FT-IR data showed conformational changes occurred in BSA after interaction with neratinib. The binding constant values decreased as the temperature increased suggesting an instable complex formation at high temperature. Site I (sub-domain IIA was observed as the principal binding site for neratinib. Hydrogen bonding and Van der Waals forces were suggested to be involved in the BSA-neratinib interaction due to the negative values of entropy and enthalpy changes.

  13. Bovine serum albumin nanoparticles loaded with Photosens photosensitizer for effective photodynamic therapy

    Science.gov (United States)

    Khanadeev, Vitaly; Khlebtsov, Boris; Packirisamy, Gopinath; Khlebtsov, Nikolai

    2017-03-01

    Polymeric nanoparticles (NPs) are widely used for drug delivery applications due to high biodegradability, low toxicity and high loading capacity. The focus of this study is the development of photosensitizer Photosens (PS) loaded albumin NPs for efficient photodynamic therapy (PDT). To fabricate PS-loaded bovine serum albumin nanoparticles (BSA-PS NPs), we used a coacervation method with glutaraldehyde followed by passive loading of PS. Successful loading of PS was confirmed by appearance of characteristic peak in absorption spectrum which allows to determine the PS loading in BSA NPs. The synthesized BSA-PS NPs demonstrated low toxicity to HeLa cells at therapeutic concentrations of loaded PS. Compared to free PS solution, the synthesized BSA-PS NPs generated the singlet oxygen more effectively under laser irradiation at 660 nm. In addition, due to presence of various chemical groups on the surface of BSA-PS NPs, they are capable to adsorb on cell surface and accumulate in cells due to cellular uptake mechanisms. Owing to combination of PD and cell uptake advantages, BSA-PS NPs demonstrated higher efficacy of photodynamic damage to cancer cells as compared to free PS at equivalent concentrations. These results suggest that non-targeted BSA-PS NPs with high PD activity and low-fabrication costs of are promising candidates for transfer to PD clinic treatments.

  14. Interaction of 1-pyrene sulfonic acid sodium salt with human serum albumin

    Energy Technology Data Exchange (ETDEWEB)

    Steblecka, Malgorzata, E-mail: gosia@mitr.p.lodz.pl; Wolszczak, Marian, E-mail: marianwo@mitr.p.lodz.pl; Szajdzinska-Pietek, Ewa, E-mail: espietek@mitr.p.lodz.pl

    2016-04-15

    Steady state and time-resolved techniques of optical spectroscopy were applied to examine the interaction between 1-pyrene sulfonic acid (PSA) sodium salt and human serum albumin (HSA). This work is directed towards finding a convenient fluorescent marker (or blocker) of hydrophobic binding sites within the protein, to be used in the in vitro studies of HSA−drug systems. The observed variation of PSA absorbance with HSA concentration was interpreted in terms of two possible probe/protein binding modes with the binding constants K{sub b,1}=(6.5±0.6)∙10{sup 6} M{sup −1} (a specific receptor site), and K{sub b,2}=(3.8±0.8)∙10{sup 5} M{sup −1} (non-specific binding of up to three probe molecules). The PSA fluorescence is quenched by the albumin (via both static and dynamic mechanisms), and also the HSA–Trp214 fluorescence is quenched by PSA (via resonance energy transfer). These results indicate that the probe is bound in the domain IIA of the secondary HSA structure. At lower [PSA]/[HSA] ratios the PSA fluorescence lifetime is longer than that in homogeneous buffer solutions (not containing HSA). Therefore, we conclude that lower affinity binding sites are distant from the tryptophan residue. This is confirmed by complementary studies on the transient T–T absorbance and on luminescence of the photosensitized singlet oxygen.

  15. The preparation and properties of a highly specific antiserum elicited with 3-dehydrocholylglycine 3-succinyl-bovine serum albumin conjugate

    International Nuclear Information System (INIS)

    Orban, E.C.; Pal, Z.

    1986-01-01

    This report describes the synthesis of a new cholylglycine derivative-bovine serum albumin conjugate. The hapten is linked to the carrier protein at the C-3 position, through a hemisuccinate bridge. Antiserum elicited by this antigen is highly specific to cholylglycine. Cross-reactions with free cholic acid (less than 0.1%) or cholyltaurine (0.5%) are minimal. (author)

  16. Development of Diagnostic Fragment Ion Library for Glycated Peptides of Human Serum Albumin: Targeted Quantification in Prediabetic, Diabetic, and Microalbuminuria Plasma by Parallel Reaction Monitoring, SWATH, and MSE*

    OpenAIRE

    Korwar, Arvind M.; Vannuruswamy, Garikapati; Jagadeeshaprasad, Mashanipalya G.; Jayaramaiah, Ramesha H.; Bhat, Shweta; Regin, Bhaskaran S.; Ramaswamy, Sureshkumar; Giri, Ashok P.; Mohan, Viswanathan; Balasubramanyam, Muthuswamy; Kulkarni, Mahesh J.

    2015-01-01

    Human serum albumin is one of the most abundant plasma proteins that readily undergoes glycation, thus glycated albumin has been suggested as an additional marker for monitoring glycemic status. Hitherto, only Amadori-modified peptides of albumin were quantified. In this study, we report the construction of fragment ion library for Amadori-modified lysine (AML), N(ε)-(carboxymethyl)lysine (CML)-, and N(ε)-(carboxyethyl)lysine (CEL)-modified peptides of the corresponding synthetically modified...

  17. Effects of Serum Albumin, Calcium Levels, Cancer Stage and Performance Status on Weight Loss in Parathyroid Hormone-Related Peptide Positive or Negative Patients with Cancer

    Directory of Open Access Journals (Sweden)

    Ji-Yeon Lee

    2018-03-01

    Full Text Available BackgroundA recent animal study showed that parathyroid hormone-related peptide (PTHrP is associated with cancer cachexia by promoting adipose tissue browning, and we previously demonstrated that PTHrP predicts weight loss (WL in patients with cancer. In this study, we investigated whether prediction of WL by PTHrP is influenced by clinical factors such as serum albumin, corrected calcium levels, cancer stage, and performance status (PS.MethodsA cohort of 219 patients with cancer whose PTHrP level was measured was enrolled and followed for body weight (BW changes. Subjects were divided into two groups by serum albumin (cutoff value, 3.7 g/dL, corrected calcium (cutoff value, 10.5 mg/dL, cancer stage (stage 1 to 3 or 4, or PS (Eastern Cooperative Oncology Group 0 to 1 or 2 to 4, respectively. Clinically significant WL was defined as either percent of BW change (% BW <−5% or % BW <−2% plus body mass index (BMI <20 kg/m2.ResultsAfter a median follow-up of 327 days, 74 patients (33.8% experienced clinically significant WL. A positive PTHrP level was associated with a 2-fold increased risk of WL after adjusting for age, baseline BMI, serum albumin, corrected calcium level, cancer stage, and PS. The effect of PTHrP on WL remained significant in patients with low serum albumin, stage 4 cancer, and good PS. Regardless of calcium level, the effect of PTHrP on WL was maintained, although there was an additive effect of higher calcium and PTHrP levels.ConclusionEarly recognition of patients with advanced cancer who are PTHrP positive with hypercalcemia or hypoalbuminemia is needed for their clinical management.

  18. Residual bovine serum albumin (BSA) quantitation in vaccines using automated Capillary Western technology.

    Science.gov (United States)

    Loughney, John W; Lancaster, Catherine; Ha, Sha; Rustandi, Richard R

    2014-09-15

    Bovine serum albumin (BSA) is a major component of fetal bovine serum (FBS), which is commonly used as a culture medium during vaccine production. Because BSA can cause allergic reactions in humans the World Health Organization (WHO) has set a guidance of 50 ng or less residual BSA per vaccine dose. Vaccine manufacturers are expected to develop sensitive assays to detect residual BSA. Generally, sandwich enzyme-linked immunosorbent assays (ELISA) are used in the industry to detect these low levels of BSA. We report the development of a new improved method for residual BSA detection using the SimpleWestern technology to analyze residual BSA in an attenuated virus vaccine. The method is based on automated Capillary Western and has linearity of two logs, >80% spike recovery (accuracy), intermediate precision of CV <15%, and LOQ of 5.2 ng/ml. The final method was applied to analyze BSA in four lots of bulk vaccine products and was used to monitor BSA clearance during vaccine process purification. Copyright © 2014 Elsevier Inc. All rights reserved.

  19. Unexpected effects of absorbed normal rabbit serum and bovine serum albumin on survival of Haemophilus influenzae type b in the infant rat.

    Science.gov (United States)

    Loeb, M R

    1988-01-01

    In the course of using the infant rat model to determine the ability of various rabbit antisera to protect against challenge by Haemophilus influenzae type b we made two unexpected observations. In these experiments 4-day-old rats were inoculated s.c. on the dorsum with either rabbit serum or physiological buffers (sham serum) and then were challenged the next day with H. influenzae type b injected i.p. Bacteremia, as a marker for disease, was measured 24 h later on day 6. We observed the following. (i) Pre-immune, i.e., normal rabbit serum, containing minimal levels of antibodies to outer membrane proteins and depleted of antibodies to capsule and lipopolysaccharide, nevertheless significantly (P less than 0.01) protected the rats from challenge with H. influenzae type b when compared to a sham inoculation of buffer; (ii) In the absence of a serum inoculation on day 4 (a buffer was used as a sham serum inoculation), the levels of bacteremia obtained after inoculation with bacteria on day 5 depended upon the composition of the buffer in which the H. influenzae inoculum was suspended. Use of phosphate buffered saline (PBS) resulted in higher levels of bacteremia than PBS containing 0.5% bovine serum albumin (PBS-BSA) (P less than 0.001), i.e. the BSA apparently acted to protect the rats from H. influenzae infection. In fact the use of PBS-BSA as an inoculum buffer masked the protective effect noted above of the absorbed normal rabbit serum.

  20. Studies of the labelling of human serum albumin with 99mTc using Sn(II) tartrate and Sn(II)Cl2 as reducing agents

    International Nuclear Information System (INIS)

    El-Kolaly, M.T.; El-Asrag, H.A.; El-Wetery, A.S.; El-Mohty, A.A.

    1990-01-01

    A comparative study has been carried out on the effect of Sn(II) tartrate and Sn(II)Cl 2 on the labelling efficiency and tissue distribution of 99m Tc-human serum albumin. The effect of reductant content, reaction time (incubation time), albumin content, pH, and ascorbic acid on the efficiency of labelling and the tissue distribution of the labelled albumin has been investigated. The percentage of labelling was determined by paper and thin layer radiochromatography. Ascorbic acid shows no effect on either labelling efficiency or tissue distribution of 99m Tc-HSA prepared by Sn(II) tartrate or Sn(II)Cl 2 . (author)

  1. Polyacrylic acids–bovine serum albumin complexation: Structure and dynamics

    International Nuclear Information System (INIS)

    Othman, Mohamed; Aschi, Adel; Gharbi, Abdelhafidh

    2016-01-01

    The study of the mixture of BSA with polyacrylic acids at different masses versus pH allowed highlighting the existence of two regimes of weak and strong complexation. These complexes were studied in diluted regime concentration, by turbidimetry, dynamic light scattering (DLS), zeta-potential measurements and nuclear magnetic resonance (NMR). We have followed the pH effect on the structure and properties of the complex. This allowed refining the interpretation of the phase diagram and understanding the observed phenomena. The NMR measurements allowed probing the dynamics of the constituents versus the pH. The computational method was used to precisely determine the electrostatic potential of BSA and how the polyelectrolyte binds to it at different pH. - Highlights: • Influence of physico-chemical parameters on the electrostatic interactions in the complex system (polyelectrolyte/protein). • Stabilization and encapsulation of biological macromolecules solution by mean of polyelectrolyte. • Properties and structure of mixture obtained by screening the charges of globular protein and at different masses of polyacrylic acids. • Dynamic of the constituents formed by complexes particles. • Evaluation of the electrostatic properties of bovine serum albumin versus pH through solution of the Poisson-Boltzmann equation.

  2. Mass spectrometry characterization of circulating human serum albumin microheterogeneity in patients with alcoholic hepatitis.

    Science.gov (United States)

    Naldi, Marina; Baldassarre, Maurizio; Domenicali, Marco; Giannone, Ferdinando Antonino; Bossi, Matteo; Montomoli, Jonathan; Sandahl, Thomas Damgaard; Glavind, Emilie; Vilstrup, Hendrik; Caraceni, Paolo; Bertucci, Carlo

    2016-04-15

    Human serum albumin (HSA) is the most abundant plasma protein, endowed with several biological properties unrelated to its oncotic power, such as antioxidant and free-radicals scavenging activities, binding and transport of many endogenous and exogenous substances, and regulation of endothelial function and inflammatory response. These non-oncotic activities are closely connected to the peculiarly dynamic structure of the albumin molecule. HSA undergoes spontaneous structural modifications, mainly by reaction with oxidants and saccharides; however, patients with cirrhosis show extensive post-transcriptional changes at several molecular sites of HSA, the degree of which parallels the severity of the disease. The present work reports the development and application of an innovative LC-MS analytical method for a rapid and reproducible determination of the relative abundance of HSA isoforms in plasma samples from alcoholic hepatitis (AH) patients. A condition of severe oxidative stress, similar to that observed in AH patients, is associated with profound changes in circulating HSA microheterogeneity. More interestingly, the high resolution provided by the analytical platform allowed the monitoring of novel oxidative products of HSA never reported before. Copyright © 2016 Elsevier B.V. All rights reserved.

  3. Species Differences in the Binding of Sodium 4-Phenylbutyrate to Serum Albumin.

    Science.gov (United States)

    Yamasaki, Keishi; Enokida, Taisuke; Taguchi, Kazuaki; Miyamura, Shigeyuki; Kawai, Akito; Miyamoto, Shuichi; Maruyama, Toru; Seo, Hakaru; Otagiri, Masaki

    2017-09-01

    Sodium 4-phenylbutyrate (PB) is clinically used as a drug for treating urea cycle disorders. Recent research has shown that PB also has other pharmacologic activities, suggesting that it has the potential for use as a drug for treating other disorders. In the process of drug development, preclinical testing using experimental animals is necessary to verify the efficacy and safety of PB. Although the binding of PB to human albumin has been studied, our knowledge of its binding to albumin from the other animal species is extremely limited. To address this issue, we characterized the binding of PB to albumin from several species (human, bovine, rabbit, and rat). The results indicated that PB interacts with 1 high-affinity site of albumin from these species, which corresponds to site II of human albumin. The affinities of PB to human and bovine albumins were higher than those to rabbit and rat albumin, and that to rabbit albumin was the lowest. Binding and molecular docking studies using structurally related compounds of PB suggested that species differences in the affinity are attributed to differences in the structural feature of the PB-binding sites on albumins (e.g., charge distribution, hydrophobicity, shape, or size). Copyright © 2017 American Pharmacists Association®. Published by Elsevier Inc. All rights reserved.

  4. Selective fluorescence resonance energy transfer from serum albumins to a bio-active 3-pyrazolyl-2-pyrazoline derivative: A spectroscopic analysis

    Energy Technology Data Exchange (ETDEWEB)

    Sarkar, Arindam [Department of Chemistry, Jadavpur University, Kolkata 700032 (India); Bhattacharya, Subhash Chandra, E-mail: sbjuchem@yahoo.com [Department of Chemistry, Jadavpur University, Kolkata 700032 (India)

    2012-10-15

    A novel fluorescent probe and pharmaceutically significant: 3-pyrazolyl-2-pyrazoline derivative (PYZ) has been selected as an acceptor molecule for fluorescence resonance energy transfer (FRET) interaction with serum albumins. Steady state and time resolved fluorescence techniques were applied to elucidate the nature of interaction of PYZ with serum albumins (BSA and HSA). Negligible FRET mediated emission occurred in the case of HSA but an efficient FRET mediated emission resulted in case of BSA. To gain further insight into the FRET selectivity of PYZ with the proteins, FRET from L-tryptophan (donor; native tryptophan) to PYZ (acceptor) was performed with the aim of getting an idea about the steric restrictions imposed on PYZ by the other groups present in BSA and HSA. The studies revealed that the surface bound Trp-134 in BSA allows an efficient FRET process with PYZ while the buried Trp-214 in HSA does not. The unusual selectivity for FRET in case of PYZ and the serum albumins has also been attributed to the complex structure of PYZ due to the presence of bulkier phenyl moieties in it. The complex nature of the excited state photophysics of tryptophan (Trp) in proteins also accounts for this FRET selectivity of PYZ with BSA and HSA. - Highlights: Black-Right-Pointing-Pointer FRET from BSA/HSA to PYZ was monitored using steady state and time resolved fluorescence methods. Black-Right-Pointing-Pointer Efficient FRET process resulted in BSA-PYZ system in contrast with the HSA-PYZ system. Black-Right-Pointing-Pointer Surface bound Trp-134 in BSA facilitates the FRET process with PYZ than the buried Trp-214 in HSA. Black-Right-Pointing-Pointer Rigid and complex structure of PYZ also accounts for the FRET selectivity of PYZ with BSA/HSA.

  5. Albumin-drug interaction and its clinical implication.

    Science.gov (United States)

    Yamasaki, Keishi; Chuang, Victor Tuan Giam; Maruyama, Toru; Otagiri, Masaki

    2013-12-01

    Human serum albumin acts as a reservoir and transport protein for endogenous (e.g. fatty acids or bilirubin) and exogenous compounds (e.g. drugs or nutrients) in the blood. The binding of a drug to albumin is a major determinant of its pharmacokinetic and pharmacodynamic profile. The present review discusses recent findings regarding the nature of drug binding sites, drug-albumin binding in certain diseased states or in the presence of coadministered drugs, and the potential of utilizing albumin-drug interactions in clinical applications. Drug-albumin interactions appear to predominantly occur at one or two specific binding sites. The nature of these drug binding sites has been fundamentally investigated as to location, size, charge, hydrophobicity or changes that can occur under conditions such as the content of the endogenous substances in question. Such findings can be useful tools for the analysis of drug-drug interactions or protein binding in diseased states. A change in protein binding is not always a problem in terms of drug therapy, but it can be used to enhance the efficacy of therapeutic agents or to enhance the accumulation of radiopharmaceuticals to targets for diagnostic purposes. Furthermore, several extracorporeal dialysis procedures using albumin-containing dialysates have proven to be an effective tool for removing endogenous toxins or overdosed drugs from patients. Recent findings related to albumin-drug interactions as described in this review are useful for providing safer and efficient therapies and diagnoses in clinical settings. This article is part of a Special Issue entitled Serum Albumin. Copyright © 2013 Elsevier B.V. All rights reserved.

  6. On-site preparation of technetium-99m labeled human serum albumin for clinical application

    International Nuclear Information System (INIS)

    Wang Yuhfeng; Chuang Meihua; Cham Thauming; Chung Meiing; Chiu Jainnshiun

    2007-01-01

    Technetium-99m labeled human serum albumin (Tc-99m HSA) is an important radiopharmaceutical for clinical applications, such as cardiac function tests or protein-losing gastroenteropathy assessment. However, because of transfusion-induced infectious diseases, the safety of serum products is a serious concern. In this context, serum products acquired from patients themselves are the most ideal tracer. However, the development of rapid separation and easy clinical labeling methods is not yet well established. Under such situation, products from the same ethnic group or country are now recommended by the World Health Organization as an alternative preparation. This article describes the on-site preparation of Tc-99m HSA from locally supplied serum products. Different formulations were prepared and the labeling efficiency and stability were examined. Radio-labeling efficiencies were more than 90% in all preparation protocols, except for one that omitted the stannous solution. The most cost-effective protocol contained HSA 0.1 mg, treated with stannous fluoride 0.2 mg, and mixed with Tc-99m pertechnetate 30 mCi. A biodistribution study was performed in rats using a gamma camera immediately after intravenous administration of radiolabeled HSA. Tissue/organ uptake was obtained by measuring the radioactivity in organs after sacrificing the rats at timed intervals. The biologic half-life was about 32 min, determined from sequential venous blood collections. These data indicate that our preparation of Tc-99m HSA is useful and potentially applicable clinically. In addition, this on-site preparation provides the possibility of labeling a patient's own serum for subsequent clinical application. (author)

  7. A combined spectroscopic and molecular docking study on site selective binding interaction of Toluidine blue O with Human and Bovine serum albumins

    Energy Technology Data Exchange (ETDEWEB)

    Selva Sharma, Arumugam [Department of Chemistry, Bharathiar University, Coimbatore 641046 (India); Anandakumar, Shanmugam [Department of Bioinformatics, Bharathiar University, Coimbatore 641046 (India); Ilanchelian, Malaichamy, E-mail: chelian73@yahoo.com [Department of Chemistry, Bharathiar University, Coimbatore 641046 (India)

    2014-07-01

    In the present investigation the interaction of a biologically active photodynamic therapeutic agent Toluidine blue O (TBO) with Serum albumins viz Human serum albumin (HSA) and Bovine serum albumin (BSA) was studied using absorption, emission, circular dichroism spectroscopy and molecular docking experiments. The emission titration experiments between HSA/BSA and TBO revealed the existence of strong interactions between TBO and the proteins. The site competitive experiment of HSA and BSA showed that the primary binding site of TBO is located in site I of HSA/BSA involving hydrophobic, hydrogen bonding and electrostatic interaction. To ascertain the results of site competitive experiments, molecular docking was utilized to characterize the binding models of TBO–HSA/BSA complexes. From the molecular docking studies, free energy calculations were undertaken to examine the energy contributions and the role of various amino acid residues of HSA/BSA in TBO binding. The existence of Forster Resonance Energy Transfer (FRET) between the ligand and the protein was utilized to calculate the donor–acceptor distance of TBO and protein. The TBO induced conformational changes of HSA/BSA was established using synchronous emission, three dimensional emission and circular dichroism studies. - Highlights: • Site selective binding interaction of TBO with HSA and BSA were investigated. • TBO quenches the intrinsic fluorescence of HSA/BSA by static quenching process. • Computational studies of TBO with HSA/BSA substantiate the experimental findings. • 3D and CD spectral studies of TBO–HSA/BSA revealed structural changes in protein. • The distance (r) between TBO and HSA/BSA were estimated from FRET theory.

  8. Comprehensive analysis of prognostic factors in hospitalized patients with pneumonia occurring outside hospital: Serum albumin is not less important than pneumonia severity assessment scale.

    Science.gov (United States)

    Miyazaki, Hiroyuki; Nagata, Nobuhiko; Akagi, Takanori; Takeda, Satoshi; Harada, Taishi; Ushijima, Shinichiro; Aoyama, Takashi; Yoshida, Yuji; Yatsugi, Hiroshi; Fujita, Masaki; Watanabe, Kentaro

    2018-08-01

    This study aimed to elucidate factors related to 30-day mortality of pneumonia occurring outside hospital by comprehensively analyzing data considered relevant to prognosis. Data considered relevant to prognosis were retrospectively examined from clinical charts and chest X-ray images of all patients with pneumonia occurring outside hospital admitted to our hospital from 2010 to 2016. The primary outcome was 30-day mortality. Data were collected from 534 patients (317 community-acquired pneumonia and 217 nursing- and healthcare associated pneumonia patients; 338 men (63.3%); mean age, 76.2 years-old). Eighty-three patients (9.9%) died from pneumonia within 30 days from the date of admission. The numbers of patients with pneumonia severity index (PSI) classes of I/II/III/IV/V and age, dehydration, respiratory failure, orientation disturbance, pressure (A-DROP) scores of 0/1/2/3/4/5 were 29/66/127/229/83, and 71/107/187/132/30/7, respectively. Mean (standard deviation) body mass index (BMI), serum albumin, blood procalcitonin, white blood cell and C-reactive protein were 20.00 (4.12) kg/m 2 , 3.16 (0.60) g/dL, 3.69 (13.15) ng/mL, 11559.4 (5656.9)/mm 3 , and 10.92 (8.75) mg/dL, respectively. Chest X-ray images from 152 patients exhibited a pneumonia shadow over a quarter of total lung field. Logistic regression analysis revealed that PSI class or A-DROP score, BMI, serum albumin, and extent of pneumonia shadow were related to 30-day mortality. Receiver operating characteristics curve analysis revealed that serum albumin was superior to PSI class or A-DROP score for predicting 30-day mortality. Serum albumin is not less important than PSI class or A-DROP score for predicting 30-day mortality in hospitalized patients with pneumonia occurring outside hospital. Copyright © 2018 Japanese Society of Chemotherapy and The Japanese Association for Infectious Diseases. Published by Elsevier Ltd. All rights reserved.

  9. Drug binding properties of neonatal albumin

    DEFF Research Database (Denmark)

    Brodersen, R; Honoré, B

    1989-01-01

    Neonatal and adult albumin was isolated by gel chromatography on Sephacryl S-300, from adult and umbilical cord serum, respectively. Binding of monoacetyl-diamino-diphenyl sulfone, warfarin, sulfamethizole, and diazepam was studied by means of equilibrium dialysis and the binding data were analyzed...... by the method of several acceptable fitted curves. It was found that the binding affinity to neonatal albumin is less than to adult albumin for monoacetyl-diamino-diphenyl sulfone and warfarin. Sulfamethizole binding to the neonatal protein is similarly reduced when more than one molecule of the drug is bound...

  10. Early diagnosis of morphologic-functional changes of the airways by a simple method of inhalation scintigraphy

    International Nuclear Information System (INIS)

    Flierdt, E. van de; Bauer, R.; Laubenbacher, C.; Didic, M.; Langhammer, H.R.; Pabst, H.W.

    1992-01-01

    In order to validate a method of inhalation scintigraphy with 99m Tc-labeled human serum albumin in the early diagnosis of morphologic-functional changes of the airways 35 volunteers and patients (12 healthy non-smokers and smokers each, 11 patients with bronchitis) were studied. Deposition of the aerosol immediately after inhalation was calculated quantitatively by a ROI technique and qualitatively (scoring of central deposition, homogeneity, and recognizability of lung outline). Additionally, the regional clearance of the inhaled aerosol was determined by continuous lung imaging up to 60 min (mainly regional mucociliary removal rates). Discrimination between healthy volunteers and patients with bronchitis was possible by means of deposition patterns immediately after inhalation. On the other hand, no differences could be recognized in this way between healthy non-smokers and smokers. Regional mucociliary removal was higher in non-smokers than in smokers, but there was no difference between smokers and patients with bronchitis. (orig.) [de

  11. Development of ELISA kit for rat albumin

    International Nuclear Information System (INIS)

    Yuan Zhigang; Han Shiquan; Liu Yibing; Xu Wenge; Jia Juanjuan

    2009-01-01

    The Anti-rat albumin serum was prepared by immunized the sheep with rat albumin. A ELISA method was established for rat albumin. The measurement range of the assay was 1-50 mg/L, sensitivity of the assay was 0.42 mg/L, recovery rate was 85.0%-106.0%. Intra-and inter-assay variation coefficients were <8.9% and <12.8% respectively. The correlation coefficients between measured and expected values were 0.999 after serial dilution of the urine samples with high concentrations of rat albumin. A good correlation was observed between the ELISA and RIA methods, and the kit for rat albumin might provide a convenience in exploitation of renal drugs and experimental injury of the kidney. (authors)

  12. Effects of pH and ionic strength on the thermodynamics of human serum albumin-photosensitizer binding

    International Nuclear Information System (INIS)

    Jones, Cecil L.; Dickson, TiReJe; Hayes, Ronald; Thomas, Lana

    2012-01-01

    Highlights: ► The pH dependence of entropy and enthalpy changes was determined for zinc phthalocyanine tetrasulfonic acid, ZnPcS 4 binding to human serum albumin, HSA. ► The ionic strength dependence of entropy and enthalpy changes was determined for ZnPcS 4 acid binding to HSA. ► The primary driving force governing the interaction between ZnPcS 4 and HSA over the range of pH and ionic strength was solution dynamics. ► The interplay between entropy and enthalpy changes was demonstrated. - Abstract: Fluorescence spectroscopy was used to measure the effects of pH and ionic strength on thermodynamic parameters governing the interaction of human serum albumin with zinc phthalocyanine tetrasulfonic acid. Fluorescence emission of zinc phthalocyanine increases at 686 nm with increasing concentrations of the protein. The non-linear correlation between protein concentration and emission of the photosensitizer was fitted using Chipman's analysis to calculate the binding affinities. The standard enthalpy and entropy changes were estimated from van’t Hoff analysis of data that were acquired from temperature ramping studies. Results show that reaction is primarily driven by solution dynamics and that the change in enthalpy for the system becomes increasingly unfavorable with increasing pH and ionic strength. The effect of ionic strength on the entropy change for binding is shown to be significantly greater than the effects of pH. The interplay between entropy and enthalpy changes is demonstrated.

  13. Generation of fatty acids from 1,2-dipalmitoyl-sn-glycero-3-phosphocholine/cardiolipin liposomes that stabilize recombinant human serum albumin.

    Science.gov (United States)

    Frahm, Grant E; Cameron, Brooke E; Smith, Jeffrey C; Johnston, Michael J W

    2013-06-01

    At elevated temperatures, studies have shown that serum albumin undergoes irreversible changes to its secondary structure. Anionic fatty acids and/or anionic surfactants have been shown to stabilize human serum albumin (HSA) against thermal denaturation through bridging hydrophobic domains and cationic amino acids residues of the protein. As albumin can readily interact with a variety of liposomes, this study proposes that cardiolipin delivered via 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) liposomes can improve the thermal stability of recombinant HSA produced in Saccharomyces cerevisiae (ScrHSA) in a similar manner to anionic fatty acids. Thermal stability and structure of ScrHSA in the absence and presence of DPPC/cardiolipin liposomes was assessed with U/V circular dichroism spectropolarimetry and protein thermal stability was confirmed with differential scanning calorimetry. Although freshly prepared DPPC/cardiolipin liposomes did not improve the stability of ScrHSA, DPPC/cardiolipin liposomes incubated at room temperature for 7 d (7dRT) dramatically improved the thermal stability of the protein. Mass spectrometry analysis identified the presence of fatty acids in the 7dRT liposomes, not identified in freshly prepared liposomes, to which the improved stability was attributed. The generation of fatty acids is attributed to either the chemical hydrolysis or oxidative cleavage of the unsaturated acyl chains of cardiolipin. By modulating the lipid composition through the introduction of lipids with higher acyl chain unsaturation, it may be possible to generate the stabilizing fatty acids in a more rapid manner.

  14. Molecular modeling and multispectroscopic studies of the interaction of hepatitis B drug, adefovir dipivoxil with human serum albumin

    International Nuclear Information System (INIS)

    Shahabadi, Nahid; Falsafi, Monireh; Hadidi, Saba

    2015-01-01

    The interaction of hepatitis B drug, adefovir dipivoxil with human serum albumin (HSA) was studied by using UV–vis, fluorometric, circular dichroism (CD) and molecular docking techniques. The results indicated that the binding of the drug to HSA caused fluorescence quenching through static quenching mechanism with binding constant of 1.3×103 M −1 . The thermodynamic parameters indicated that the hydrophobic force contacts are the major forces in the stability of protein-drug complex (ΔH>0 and ΔS>0). The displacement experiments using the site probes viz., warfarin and ibuprofen showed that adefovir dipivoxil could bind to the site III of HSA. The results of CD and UV–vis spectroscopy indicated that the binding of the drug induced some conformational changes in HSA. Furthermore, the study of molecular docking also confirmed binding of adefovir dipivoxil to the site III of HSA by hydrophobic interaction. - Highlights: • The interaction of adefovir dipivoxil, drug for the treatment of HIV and HBV with human serum albumin (HSA) is investigated. • The drug bound to HSA by hydrophobic force and induced some conformational changes in HSA. • The study of molecular docking showed that adefovir dipivoxil could bind to the site III of HSA mainly

  15. Molecular modeling and multispectroscopic studies of the interaction of hepatitis B drug, adefovir dipivoxil with human serum albumin

    Energy Technology Data Exchange (ETDEWEB)

    Shahabadi, Nahid, E-mail: nahidshahabadi@yahoo.com [Department of Chemistry, Faculty of Science, Razi University, Kermanshah (Iran, Islamic Republic of); Medical Biology Research Center (MBRC) Kermanshah University of Medical Sciences, Kermanshah (Iran, Islamic Republic of); Falsafi, Monireh [Department of Chemistry, Faculty of Science, Razi University, Kermanshah (Iran, Islamic Republic of); Hadidi, Saba [Department of Chemistry, Faculty of Science, Razi University, Kermanshah (Iran, Islamic Republic of); Medical Biology Research Center (MBRC) Kermanshah University of Medical Sciences, Kermanshah (Iran, Islamic Republic of)

    2015-11-15

    The interaction of hepatitis B drug, adefovir dipivoxil with human serum albumin (HSA) was studied by using UV–vis, fluorometric, circular dichroism (CD) and molecular docking techniques. The results indicated that the binding of the drug to HSA caused fluorescence quenching through static quenching mechanism with binding constant of 1.3×103 M{sup −1}. The thermodynamic parameters indicated that the hydrophobic force contacts are the major forces in the stability of protein-drug complex (ΔH>0 and ΔS>0). The displacement experiments using the site probes viz., warfarin and ibuprofen showed that adefovir dipivoxil could bind to the site III of HSA. The results of CD and UV–vis spectroscopy indicated that the binding of the drug induced some conformational changes in HSA. Furthermore, the study of molecular docking also confirmed binding of adefovir dipivoxil to the site III of HSA by hydrophobic interaction. - Highlights: • The interaction of adefovir dipivoxil, drug for the treatment of HIV and HBV with human serum albumin (HSA) is investigated. • The drug bound to HSA by hydrophobic force and induced some conformational changes in HSA. • The study of molecular docking showed that adefovir dipivoxil could bind to the site III of HSA mainly.

  16. Influence of galloyl moiety in interaction of epicatechin with bovine serum albumin: a spectroscopic and thermodynamic characterization.

    Directory of Open Access Journals (Sweden)

    Sandip Pal

    Full Text Available The health benefits stemming from green tea are well known, but the exact mechanism of its biological activity is not elucidated. Epicatechin (EC and epicatechin gallate (ECG are two dietary catechins ubiquitously present in green tea. Serum albumins functionally carry these catechins through the circulatory system and eliminate reactive oxygen species (ROS induced injury. In the present study ECG is observed to have higher antioxidant activity; which is attributed to the presence of galloyl moiety. The binding affinity of these catechins to bovine serum albumin (BSA will govern the efficacy of their biological activity. EC and ECG bind with BSA with binding constants 1.0 × 10(6 M(-1 and 6.6 × 10(7 M(-1, respectively. Changes in secondary structure of BSA on interaction with EC and ECG have been identified by circular dichroism (CD and Fourier transform infrared (FT-IR spectroscopy. Thermodynamic characterization reveals the binding process to be exothermic, spontaneous and entropy driven. Mixed binding forces (hydrophobic, electrostatic and hydrogen bonding exist between ECG and BSA. Binding site for EC is primarily site-II in sub-domain IIIA of BSA and for ECG; it is site-I in sub-domain IIA. ECG with its high antioxidant activity accompanied by high affinity for BSA could be a model in drug designing.

  17. Multi-spectroscopic characterization of bovine serum albumin upon interaction with atomoxetine

    Directory of Open Access Journals (Sweden)

    Arunkumar T. Buddanavar

    2017-06-01

    Full Text Available The quenching interaction of atomoxetine (ATX with bovine serum albumin (BSA was studied in vitro under optimal physiological condition (pH=7.4 by multi-spectroscopic techniques. The mechanism of ATX-BSA system was a dynamic quenching process and was confirmed by the fluorescence spectra and lifetime measurements. The number of binding sites, binding constants and other binding characteristics were computed. Thermodynamic parameters ∆H° and ∆S° indicated that intermolecular hydrophobic forces predominantly stabilized the drug-protein system. The average binding distance between BSA and ATX was studied by Försters theory. UV-absorption, Fourier transform infrared spectroscopy (FT-IR, circular dichroism (CD, synchronous spectra and three-dimensional (3D fluorescence spectral results revealed the changes in micro-environment of secondary structure of protein upon the interaction with ATX. Displacement of site probes and the effects of some common metal ions on the binding of ATX with BSA interaction were also studied.

  18. Studies on kinetics of albumin in uraemic patients on chronic haemodialysis: evidence of interstitial albumin wash-down

    DEFF Research Database (Denmark)

    Hildebrandt, P; Jensen, H A; Henriksen, Jens Henrik Sahl

    1983-01-01

    Albumin-kinetic studies were performed in nine uraemic patients without oedema on chronic haemodialysis and in seven normal controls in order to determine microvascular leakiness and thereby, during steady state, lymph drainage of albumin. Transvascular escape rate of albumin [TERalb i.......e. the fraction of intravascular mass (IVMalb) passing into, or returning from, the extravascular space per unit time] and the distribution ratio (DRalb) between IVMalb and total albumin mass were determined from intravenously injected radioiodinated serum albumin. Before haemodialysis, TERalb was significantly...... with respect to controls (mean 0 X 44, range 0 X 42-0 X 48, P less than 0 X 01), and the extravascular mass of albumin was significantly decreased (mean 27 X 9 mumol kg-1, range 14.1 - 41.2 v. mean 35.9, range 27.1 - 43.8, P less than 0.05). We interpret the results as to indicate increased transvascular...

  19. Mass spectrometric characterization of human serum albumin dimer: A new potential biomarker in chronic liver diseases.

    Science.gov (United States)

    Naldi, Marina; Baldassarre, Maurizio; Nati, Marina; Laggetta, Maristella; Giannone, Ferdinando Antonino; Domenicali, Marco; Bernardi, Mauro; Caraceni, Paolo; Bertucci, Carlo

    2015-08-10

    Human serum albumin (HSA) undergoes several structural alterations affecting its properties in pro-oxidant and pro-inflammatory environments, as it occurs during liver cirrhosis. These modifications include the formation of albumin dimers. Although HSA dimers were reported to be an oxidative stress biomarker, to date nothing is known about their role in liver cirrhosis and related complications. Additionally, no high sensitive analytical method was available for HSA dimers assessment in clinical settings. Thus the HSA dimeric form in human plasma was characterized by mass spectrometry using liquid chromatography tandem mass spectrometry (LC-ESI-Q-TOF) and matrix assisted laser desorption time of flight (MALDI-TOF) techniques. N-terminal and C-terminal truncated HSA, as well as the native HSA, undergo dimerization by binding another HSA molecule. This study demonstrated the presence of both homo- and hetero-dimeric forms of HSA. The dimerization site was proved to be at Cys-34, forming a disulphide bridge between two albumin molecules, as determined by LC-MS analysis after tryptic digestion. Interestingly, when plasma samples from cirrhotic subjects were analysed, the dimer/monomer ratio resulted significantly increased when compared to that of healthy subjects. These isoforms could represent promising biomarkers for liver disease. Additionally, this analytical approach leads to the relative quantification of the residual native HSA, with fully preserved structural integrity. Copyright © 2014 Elsevier B.V. All rights reserved.

  20. Hot spot(s) of the lung in technetium-99m albumin colloid liver-spleen scintigraphy: case report

    International Nuclear Information System (INIS)

    Shih, W.J.; Brandenburg, S.; Coupal, J.J.; Sullivan, J.D.; Beeler, J.A.; Magoun, S.; Ryo, U.Y.

    1988-01-01

    The authors replaced /sup 99m/Tc albumin colloid for /sup 99m/Tc sulfur colloid as a radiopharmaceutical for liver-spleen imaging and found two instances of hot spot(s) in the lung. The preparation procedure of albumin colloid is easier and more convenient as compared to that of sulfur colloid. Whereas replacement of /sup 99m/Tc sulfur colloid by /sup 99m/Tc albumin colloid is inevitable, it should be emphasized that one should avoid blood withdrawal in the syringe containing albumin colloid to prevent formation of clot(s) during the venous puncture for /sup 99m/Tc albumin colloid

  1. Investigating the influence of effective parameters on molecular characteristics of bovine serum albumin nanoparticles

    Energy Technology Data Exchange (ETDEWEB)

    Rohiwal, S.S.; Satvekar, R.K.; Tiwari, A.P.; Raut, A.V.; Kumbhar, S.G.; Pawar, S.H., E-mail: pawar_s_h@yahoo.com

    2015-04-15

    Graphical abstract: The physiochemical properties of nanoparticles provide the basic aspects about the conformational transitions which could have a strong bearing on the bioavailability for bioactive molecules such as peptides and hormones. - Highlights: • Synthesis and surface and structural properties of Bovine Serum Albumin nanoparticles (BSANPs). • Study of conformational transitions of BSANPs by spectroscopic techniques. • Studies on the effect of pH and protein concentration on formulation of BSANPs. - Abstract: The protein nanoparticles formulation is a challenging task as they are prone to undergo conformational transitions while processing which may affect bioavailability for bioactive compounds. Herein, a modified desolvation method is employed to prepare Bovine Serum Albumin nanoparticles, with controllable particle size ranging from 100 to 300 nm and low polydispersity index. The factors influencing the size and structure of BSA NPs viz. protein concentration, pH and the conditions for purification are well investigated. The structure of BSA NPs is altered due to processing, and may affect the effective binding ability with drugs and bioactive compounds. With that aims, investigations of molecular characteristics of BSA NPs are carried out in detail by using spectroscopic techniques. UV–visible absorption and Fourier Transform Infrared demonstrate the alteration in protein structure of BSA NPs whereas the FT-Raman spectroscopy investigates changes in the secondary and tertiary structures of the protein. The conformational changes of BSA NPs are observed by change in fluorescence intensity and emission maximum wavelength of tryptophan residue by fluorescence spectroscopy. The field emission scanning electron and atomic force microscopy micrographs confirm the size and semi-spherical morphology of the BSA NPs. The effect of concentration and pH on particle size distribution is studied by particle size analyzer.

  2. Interaction of indomethacin with adult human albumin and neonatal serum

    DEFF Research Database (Denmark)

    Honoré, B; Brodersen, R; Robertson, A

    1983-01-01

    The binding of indomethacin to albumin was investigated at 37 degrees C, pH 7.4. The first stoichiometric binding constant is 2.5 X 10(5) M-1. Indomethacin utilizes both the bilirubin and diazepam binding functions equally. The effect on bilirubin binding to albumin is negligible at therapeutic...

  3. The development of radioimmunoassay kit for rat albumin

    International Nuclear Information System (INIS)

    Yuan Zhigang; Han Shiquan; Liu Yibing; Xu Wenge

    2006-01-01

    The Anti-rat albumin serum is prepared by immunized the sheep with rat albumin. A radioimmunoassay method is established for rat albumin. The measurement range of the assay is 1-50 mg/L, sensitivity of the assay is 0.12 mg/L, recovery rate is 97.8%- 108.4%. Intra- and inter-assay variation coefficients are <4.0% and <8.2% respectively. The correlation coefficients between measured and expected values are more than 0.990 after serial dilution of the urine samples with high concentrations of rat albumin. The kit for rat albumin might provide a convenience in exploitation of renal drugs and experimental in- jury of the kidney. (authors)

  4. Studies of quality control of 99mTc-labelled macroaggregated albumin: Pt. 1

    International Nuclear Information System (INIS)

    Fukuoka, Masamichi; Kobayashi, Tetsu; Tanaka, Akira; Satoh, Takemichi; Kubodera, Akiko

    1993-01-01

    The aggregative condition of albumin was investigated using bovine serum albumin (BSA) as a model for quality control of 99m Tc-macroaggregated albumin ( 99 Tc-MAA). Uniformalized aggregates were obtained from the oxidized non-mercapt-type of BSA by heating. The size of the aggregates was affected by the pH and the types of buffer solutions used as well as the concentrations of albumin and buffers. The β form structure of the albumin was more stable on heating and this may contribute to its aggregation. Aggregation of oxidized non-mercaptalbumin afforded a portion of smaller sized particles in MAA, this being an inappropriate factor for scintiscanning of lungs. Our results suggest that it is necessary to remove oxidized type albumin from human serum albumin as the starting material, in order to prepare MAA with a uniform and larger particle size. (Author)

  5. Epitope imprinted polymer nanoparticles containing fluorescent quantum dots for specific recognition of human serum albumin

    International Nuclear Information System (INIS)

    Wang, Yi-Zhi; Li, Dong-Yan; He, Xi-Wen; Li, Wen-You; Zhang, Yu-Kui

    2015-01-01

    Epitope imprinted polymer nanoparticles (EI-NPs) were prepared by one-pot polymerization of N-isopropylacrylamide in the presence of CdTe quantum dots and an epitope (consisting of amino acids 598 to 609) of human serum albumin (HSA). The resulting EI-NPs exhibit specific recognition ability and enable direct fluorescence quantification of HSA based on a fluorescence turn-on mode. The polymer was characterized by FT-IR, X-ray photoelectron spectroscopy, transmission electron microscopy and dynamic light scattering. The linear calibration graph was obtained in the range of 0.25–5 μmol · mL −1 with the detection limit of 44.3 nmol · mL −1 . The EI-NPs were successfully applied to the direct fluorometric quantification of HSA in samples of human serum. Overall, this approach provides a promising tool to design functional fluorescent materials with protein recognition capability and specific applications in proteomics. (author)

  6. Diagnostic pharmaco-scintigraphy with hepatic intra-arterial technetium-99m macroaggregated albumin in the determination of tumour to non-tumour uptake ratio in hepatocellular carcinoma

    International Nuclear Information System (INIS)

    Lau, W.Y.; Leung, T.W.T.; Chan, M.; Leung, N.W.Y.; Metreweli, C.; Li, A.K.C.

    1994-01-01

    Between October 1990 and March 1993, 124 patients with hepatocellular carcinoma (HCC) underwent diagnostic pharmaco-scintigraphy with hepatic intraarterial technetium-99m macroaggregated albumin (TcMAA) to determine the tumorous to non-tumorous liver tissue uptake ratio (T/N ratio). There were 110 males and 14 females. Ages ranged from 16 to 73 with a median of 55 years. The range of T/N ratio was 0.7 to 19.3 with a median of 3.8. 12 patients with inoperable HCC were subsequently selected by predetermined criteria to undergo treatment with hepatic intraarterial yttrium-90 microspheres and the T/N ratios in these patients were validated by beta probe dosimetry and liquid scintillation count of multiple liver biopsies. The T/N ratio determined by preoperative diagnostic TcMAA scan corrected well with intraoperative beta probe dosimetry, with coefficient of correlation r = 0.82. Preoperative TcMAA scan also correlated well with liquid scintillation count of biopsy specimens. (author)

  7. Studies of the competition for thorium ion between chelating agents and bovine serum albumin

    International Nuclear Information System (INIS)

    Luo Meichu; Zhang Meizhen; Sun Meizhen; Chen Shijie

    1995-01-01

    Fourteen chelation agents (polyaminopolcarboxylate type--TTHA, DTPA, EDTA; phenolicpolycarboxylate type--811, 8102, 7601, 7602, 7603, 7616, 7711, 7724, 7803, 7804, 8307) were studied their competitive ability to mobilize the thorium with bovine serum albumin (BSA). The experimental results showed that the competitive ability of TTHA, 8102, 811 to chelate Thorium with BSA were the strongest, and EDTA was the worst in all chelating agents. The measured order of the competitive ability of chelators is basically consistent with animal experimental results in vivo. The parameter F is defined as the competitive ability of chelators. F is taken as a screening criterion for de-corporate thorium which is simple, quick and effective method in vitro

  8. Aerosol lung inhalation scintigraphy in normal subjects

    Energy Technology Data Exchange (ETDEWEB)

    Sui, Osamu; Shimazu, Hideki

    1985-03-01

    We previously reported basic and clinical evaluation of aerosol lung inhalation scintigraphy with /sup 99m/Tc-millimicrosphere albumin (milli MISA) and concluded aerosol inhalation scintigraphy with /sup 99m/Tc-milli MISA was useful for routine examination. But central airway deposit of aerosol particles was found in not only the patients with chronic obstructive pulmonary disease (COPD) but also normal subjects. So we performed aerosol inhalation scintigraphy in normal subjects and evaluated their scintigrams. The subjects had normal values of FEVsub(1.0)% (more than 70%) in lung function tests, no abnormal findings in chest X-ray films and no symptoms and signs. The findings of aerosol inhalation scintigrams in them were classified into 3 patterns; type I: homogeneous distribution without central airway deposit, type II: homogeneous distribution with central airway deposit, type III: inhomogeneous distribution. These patterns were compared with lung function tests. There was no significant correlation between type I and type II in lung function tests. Type III was different from type I and type II in inhomogeneous distribution. This finding showed no correlation with %VC, FEVsub(1.0)%, MMF, V radical50 and V radical50/V radical25, but good correlation with V radical25 in a maximum forced expiratory flow-volume curve. Flow-volume curve is one of the sensitive methods in early detection of COPD, so inhomogeneous distribution of type III is considered to be due to small airway dysfunction.

  9. Differential solubility of curcuminoids in serum and albumin solutions: implications for analytical and therapeutic applications

    Directory of Open Access Journals (Sweden)

    Quitschke Wolfgang W

    2008-11-01

    Full Text Available Abstract Background Commercially available curcumin preparations contain a mixture of related polyphenols, collectively referred to as curcuminoids. These encompass the primary component curcumin along with its co-purified derivatives demethoxycurcumin and bisdemethoxycurcumin. Curcuminoids have numerous biological activities, including inhibition of cancer related cell proliferation and reduction of amyloid plaque formation associated with Alzheimer disease. Unfortunately, the solubility of curcuminoids in aqueous solutions is exceedingly low. This restricts their systemic availability in orally administered formulations and limits their therapeutic potential. Results Methods are described that achieve high concentrations of soluble curcuminoids in serum. Solid curcuminoids were either mixed directly with serum, or they were predissolved in dimethyl sulfoxide and added as aliquots to serum. Both methods resulted in high levels of curcuminoid-solubility in mammalian sera from different species. However, adding aliquots of dimethyl sulfoxide-dissolved curcuminoids to serum proved to be more efficient, producing soluble curcuminoid concentrations of at least 3 mM in human serum. The methods also resulted in the differential solubility of individual curcuminoids in serum. The addition of dimethyl sulfoxide-dissolved curcuminoids to serum preferentially solubilized curcumin, whereas adding solid curcuminoids predominantly solubilized bisdemethoxycurcumin. Either method of solubilization was equally effective in inhibiting dose-dependent HeLa cell proliferation in culture. The maximum concentration of curcuminoids achieved in serum was at least 100-fold higher than that required for inhibiting cell proliferation in culture and 1000-fold higher than the concentration that has been reported to prevent amyloid plaque formation associated with Alzheimer disease. Curcuminoids were also highly soluble in solutions of purified albumin, a major component of

  10. Bovine serum albumin adsorption on functionalized porous silicon surfaces

    Science.gov (United States)

    Tay, Li-Lin; Rowell, Nelson L.; Lockwood, David J.; Boukherroub, Rabah

    2004-10-01

    The large surface area within porous Si (pSi) and its strong room temperature photoluminescence (PL) make it an ideal host for biological sensors. In particular, the development of pSi-based optical sensors for DNA, enzyme and other biochemical molecules have become of great interest. Here, we demonstrate that the in-situ monitoring of the pSi PL behaviour can be used as a positive identification of bovine serum albumin (BSA) protein adsorption inside the porous matrix. Electrochemically prepared pSi films were first functionalized with undecylenic acid to produce an organic monolayer covalently attached to the porous silicon surfaces. The acid terminal group also provided favourable BSA binding sites on the pSi matrix sidewalls. In-situ PL spectra showed a gradual red shift (up to 12 meV) in the PL peak energy due to the protein incorporation into the porous matrix. The PL then exhibited a continuous blue shift after saturation of the protein molecules in the pores. This blue shift of the PL peak frequency and a steady increase in the PL intensity is evidence of surface oxidation. Comparing the specular reflectance obtained by Fourier transform infrared spectroscopy (FTIR) before and after BSA incubation confirmed the adsorption of protein in the pSi matrix.

  11. Albumin levels and cause-specific mortality in community-dwelling older adults.

    Science.gov (United States)

    Wu, Chen-Yi; Hu, Hsiao-Yun; Huang, Nicole; Chou, Yi-Chang; Li, Chung-Pin; Chou, Yiing-Jenq

    2018-04-09

    To investigate the association between serum albumin levels and cause-specific mortality among community-dwelling older adults. This cohort study was based on data obtained from the government-sponsored Annual Geriatric Health Examination Program for the older adults in Taipei City between 2006 and 2010. The study sample consisted of 77,531 community-dwelling Taipei citizens (≥65 years old). Mortality was determined by matching the participants' medical records with national death files. Serum albumin levels were categorized into dwelling older adults had a mean albumin level of 4.3 g/dL, which significantly reduced by age. Compared to albumin levels ≥4.4 g/dL, mildly low albumin levels (4.2-4.3 g/dL) were associated with an increased mortality risk (hazard ratio [HR]: 1.16, 95% confidence interval [CI]: 1.05-1.28 for all-cause mortality), and albumin levels dwelling older adults, and mortality risk increased as the albumin level decreased. Copyright © 2017. Published by Elsevier Inc.

  12. Pemberian diet ekstra formula komersial dan diet ekstra filtrat ikan gabus intradialisis serta pengaruhnya terhadap kadar serum albumin dan kreatinin pasien dengan hemodialisis di RSU Dr. Saiful Anwar Malang

    Directory of Open Access Journals (Sweden)

    Etik Sulistyowati

    2008-11-01

    Conclusion: There was significant effect of the supply of commercial formula and local catfish filtrate extra diet to increase of albumin serum level of the subject and there was no significant effect of the supply of extra diet to creatinine serum level; however, the supply of local catfish filtrate extra diet could maintain creatinine serum level.

  13. Serum uric acid concentration is associated with early changes of glomerular filtration rate in patients with diabetes type 1 without increased albumin excretion.

    Science.gov (United States)

    Spaleniak, Sebastian; Korzeniewska-Dyl, Irmina; Moczulski, Dariusz

    2014-10-01

    The early loss of renal function in patients with type 1 diabetes may begin before proteinuria. Only 30% of patients with diabetes manifest overt proteinuria. According to the previous studies, increased urinary albumin excretion, which is considered a classic marker of progression of diabetic kidney disease, can regress to normal urine albumin excretion. The current studies conducted in patients with type 1 diabetes without increased urine albumin excretion showed that the uric acid concentration was an independent factor for the development of diabetic kidney disease. The aim of study was to assess the impact of uric acid concentration and to identify risk factors of the early glomerular filtration loss in patients with type 1 diabetes and normal urinary albumin excretion. 147 patients (61 women and 86 men) with type 1 diabetes without increased urine albumin excretion were analysed. GFR (gromerular filtration rate) was estimated based on the serum cystatin C concentration. Centile charts were used to determine the variation of uric acid concentration depending on GFR and gender. The mean value of the filtration rate for the study group was 117 ml/min/m2. The uric acid level above 90th percentile in relation to GFR was diagnosed in 8.2% of women and 0% of men, between 90th and 50th percentile in 44.3 % of women and 5.8% of men and below 50th percentile in 47.5% of women and 94.2% of men. Contrary to men in women higher serum acid concentration was strongly associated with higher glomerular filtration rate. Hyperfiltraion was diagnosed in 15 of women and 19 of men. The high normal uric acid concentration in women with type 1 diabetes might play a crucial role in development of hyperfiltration.

  14. Use of 125I-labeled human serum albumin for quantitation of microvascular permeability in rat skin: reevaluation of an old method for studies on substances with an enhancing effect on microvascular permeability

    International Nuclear Information System (INIS)

    Gerdin, B.

    1981-01-01

    A method of determining the leakage of 125I-labeled human serum albumin in the plasma into a standardized area of rat skin to study the effects of intracutaneous application of vasoactive substances on microvascular permeability, was reevaluated. The effect is expressed as a quotient (Q) between the amount of labeled albumin in the test area and that in an area injected with buffer. This calculation is simple and as reliable as more complicated expressions of activity. Within a limited dose range, linear/log dose-response curves can be obtained after application of histamine or bradykinin. Locally injected 125I-labeled human serum albumin is eliminated very slowly from rat skin and determination of the amount of radiolabeled albumin in skin after an intravenous injection therefore represents leakage from the vascular compartments. The potentialities and advantages of this method in pharmacological studies are stressed

  15. Lung perfusion and ventilation scintigraphy in pre- and postoperative diagnostics

    International Nuclear Information System (INIS)

    Sandrock, D.; Munz, D.L.

    1998-01-01

    Lung perfusion (Tc-99m labeled albumin particles) and ventilation (Xe-133 gas) are used prior to thoracic surgery in order to evaluate changes in perfusion and ventilation due to the underlying diseases. Furthermore, perfusion scintigraphy allows combined with spirometry the prediction of the postinterventional vital capacity and the forced expiratory volume in 1 s. The correlation coefficient for this procedure compared with values measured postoperatively are in the range of 0.8. The method allows the assessment of operability in terms of postinterventional function. (orig.) [de

  16. Lung inhalation scintigraphy with radioactive aerosols in several pulmonary diseases. Cintigrafia de ventialacao pulmonar por aerosol em diversas patologias pulmonares

    Energy Technology Data Exchange (ETDEWEB)

    Martins, L R; Marioni Filho, H [Instituto Dante Pazzanese de Cardiologia, Sao Paulo, SP (Brazil); Romaldini, H; Uehara, C; Alonso, G [Escola Paulista de Medicina, Sao Paulo, SP (Brazil)

    1983-01-01

    The pulmonary ventilation scintigraphy with 99m Tc diethylene-triamine-pentaacetate (99mTc-DTPA) delivered through a new nebulizer system when analyzed together with the classic lung perfusion scintigraphy with 99mTc-labeled albumin macroaggregates (99mTcMAA) is a very important diagnostic tool in several pulmonary diseases. Several aspects of the lung ventilation-perfusion scintigraphy are studied in 15 people with no lung disease, smokers and nonsmokers. The findings with the lung ventilation-perfusion scintigraphy are also discussed in 34 patients with several pulmonary diseases: lung cancer, chronic obstructive lung disease, policystic pulmonary disease, and pulmonary embolims. The authors concluded that the procedure is a valuable diagnostic tool in several pulmonary diseases, especially because good lung images are obtained, no side effects were detected, the technique is ease and low cost, and it brings new informations, not available with other diagnostic methods. (author).

  17. Fluorescence study on the interaction of human serum albumin with Butein in liposomes

    Science.gov (United States)

    Toprak, Mahmut

    2016-02-01

    The interaction of Butein with human serum albumin in L-egg lecithin phosphatidycholine (PC) liposome has been investigated by fluorescence and absorption spectroscopy. The results of the fluorescence measurement indicated that Butein effectively quenched the intrinsic fluorescence of HSA via static quenching. The Stern-Volmer plots in all the liposome solutions showed a positive deviation from the linearity. According to the thermodynamic parameters, the hydrophobic interactions appeared be the major interaction forces between Butein and HSA. The effect of Butein on the conformation of HSA was also investigated by the synchronous fluorescence under the same experimental conditions. In addition, the partition coefficient of the Butein in the PC liposomes was also determined by using the fluorescence quenching process. The obtained results can be of biological significance in pharmacology and clinical medicine.

  18. Interaction of Human Serum Albumin with Metal Protoporphyrins

    Science.gov (United States)

    Hu, Jie; Brancaleon, Lorenzo

    2015-03-01

    Fluorescence spectroscopy is widely used in biotechnology, nanotechnology, and molecular biophysics, since it can provide information on a wide range of molecular processes, e.g. the interactions of solvent molecules with fluorophores, conformational changes, and binding interactions etc. In this study, we present the photophysical properties of the interaction of human serum albumin (HSA) with a series of metal compound of Protoporphyrin IX (PPIX), including ZnPPIX, FePPIX, MgPPIX, MnPPIX and SnPPIX respectively, as well as the free base PPIX. Binding constants were retrieved independently using the Benesi-Hildebrand analysis of the porphyrin emission or absorption spectra and the fluorescence quenching (i.e. Stern-Volmer analysis) and reveal that the two methods yield a difference of approximately one order or magnitude between the two. Fluorescence lifetimes was used to probe whether binding of the porphyrin changes the conformation of the protein or if the interaction places the porphyrin at a location that can prompt resonance energy transfer with the lone Tryptophan residue. In recent years it has been discovered that HSA provides a specific binding site for metal-chelated protoporphyrins in subdomain IA. This has opened a novel field of study over the importance of this site for biomedical applications but it has also created the potential for a series of biotechnological applications of the HSA/protoporphyrin complexes. Our study provides a preliminary investigation of the interaction with metal-chelated protoporphyrins that had not been previously investigated.

  19. Methods of albumin estimation in clinical biochemistry: Past, present, and future.

    Science.gov (United States)

    Kumar, Deepak; Banerjee, Dibyajyoti

    2017-06-01

    Estimation of serum and urinary albumin is routinely performed in clinical biochemistry laboratories. In the past, precipitation-based methods were popular for estimation of human serum albumin (HSA). Currently, dye-binding or immunochemical methods are widely practiced. Each of these methods has its limitations. Research endeavors to overcome such limitations are on-going. The current trends in methodological aspects of albumin estimation guiding the field have not been reviewed. Therefore, it is the need of the hour to review several aspects of albumin estimation. The present review focuses on the modern trends of research from a conceptual point of view and gives an overview of recent developments to offer the readers a comprehensive understanding of the subject. Copyright © 2017 Elsevier B.V. All rights reserved.

  20. Spectroscopic exploration of interaction between PEG-functionalized Ag2S nanoparticles with bovine serum albumin

    Science.gov (United States)

    Prasanth, S.; RitheshRaj, D.; Vineeshkumar, T. V.; Sudarsanakumar, C.

    2018-05-01

    The introduction of nanoparticles into biological fluids often leads to the formation of biocorona over the surface of nanoparticles. For the effective use of nanoparticles in biological applications it is very essential to understand their interactions with proteins. Herein, we investigated the interactions of Poly ethylene glycol capped Ag2S nanoparticles with Bovine Serum Albumin by spectroscopic techniques. By the addition of Ag2S nanoparticles, a ground state complex is formed. The CD spectroscopy reveals that the secondary structure of BSA is altered by complexation with PEG-Ag2S nanoparticles, while the overall tertiary structure remains closer to that of native BSA.

  1. Performance study of ultrafiltration membrane with bovine serum albumin as feed solution

    International Nuclear Information System (INIS)

    Syahril Ahmad

    2009-01-01

    Bovine serum albumin solutions at different temperature, pH, flow rate and operation pressure have been used as feed solution for studying performance of ultrafiltration membrane. Polysulfone membranes used for this experiment were in form of hollow fibers that have Molecular Weight Cut Off (MWCO) 60 kDa. Observation was focused on flux parameter and rejection coefficient towards protein during the process. Result shows that temperature, pH of BSA feed solution, flow rate and operation pressure can affect the flux and rejection coefficient of membrane. High temperature feed solution tend to decrease the flux but increase rejection coefficient. Rejection coefficient of membrane will increase while flux decreasing at pH of feed solution near to protein isoelectric point. High pressure of feed solution will increase flux but decrease rejection of membrane. Rejection of membrane will decrease and flux will increase when the process operated in slow flow rate. (author)

  2. Revisitation of FRET methods to measure intraprotein distances in Human Serum Albumin

    Energy Technology Data Exchange (ETDEWEB)

    Santini, S.; Bizzarri, A.R.; Cannistraro, S., E-mail: cannistr@unitus.it

    2016-11-15

    We revisited the FRET methods to measure the intraprotein distance between Trp-214 (used as donor) of Human Serum Albumin and its Cys-34, labelled with 1.5-Iaedans (used as acceptor). Variation of Trp fluorescence emission in terms of both intensity and lifetime, as well the enhancement of the acceptor fluorescence emission upon Trp excitation, have been monitored. A careful statistical analysis of the fluorescence results from ten independently prepared samples, combined with suitable spectral corrections, provided reproducible distances estimations by each one of the three methods. Even if monitoring of the donor lifetime variation in the presence of the acceptor reproduces at the best the crystallographic data, by allowing even sub-nanometre distance variations to be appreciated, we suggest that a comparative analysis of all the three methods, applied with statistical significance, should be preferred to achieve a better reliability of the FRET technique.

  3. Gold nanoparticles synthesized by gamma radiation and stabilized by bovine serum albumin

    Energy Technology Data Exchange (ETDEWEB)

    Leal, Jessica; Silva, Andressa A.; Geraldes, Adriana N.; Lugao, Ademar B., E-mail: jessicaleal@usp.br [Instituto de Pesquisas Energeticas e Nucleares (IPEN/CNEN-SP), Sao Paulo, SP (Brazil); Grasselli, Mariano, E-mail: mariano.grasselli@gmail.com [Departamento de Ciencia y Tecnologia, Universidad Nacional de Quilmes, Bernal (Argentina)

    2015-07-01

    Gold nanoparticles (AuNPs) are a new option for pharmaceutical and cosmetic industries due to their interesting chemical, electrical and catalytic properties. Research for cancer treatments have been developed using this promising radiotherapy agent. The challenge of gold nanoparticles is to keep them stable, due to metallic behavior. It is know that surface plasma resonance promotes agglomeration of metallic nanoparticles, but they are not stable. Stabilizers have been used to reduce agglomeration. The aim of this work is reduction of HAuCl{sub 4} salt to AuNPs performed by gamma radiation {sup 60}Co source and the stabilization of gold nanoparticles using bovine serum albumin (BSA) fraction V as stabilizer agent. AuNPs were characterized by UV-visible to verify the nanoparticles formation. Samples containing BSA and samples obtained by the conventional method (without stabilizer) were monitored for two weeks and analyzed. Results were compared. (author)

  4. Gold nanoparticles synthesized by gamma radiation and stabilized by bovine serum albumin

    International Nuclear Information System (INIS)

    Leal, Jessica; Silva, Andressa A.; Geraldes, Adriana N.; Lugao, Ademar B.; Grasselli, Mariano

    2015-01-01

    Gold nanoparticles (AuNPs) are a new option for pharmaceutical and cosmetic industries due to their interesting chemical, electrical and catalytic properties. Research for cancer treatments have been developed using this promising radiotherapy agent. The challenge of gold nanoparticles is to keep them stable, due to metallic behavior. It is know that surface plasma resonance promotes agglomeration of metallic nanoparticles, but they are not stable. Stabilizers have been used to reduce agglomeration. The aim of this work is reduction of HAuCl 4 salt to AuNPs performed by gamma radiation 60 Co source and the stabilization of gold nanoparticles using bovine serum albumin (BSA) fraction V as stabilizer agent. AuNPs were characterized by UV-visible to verify the nanoparticles formation. Samples containing BSA and samples obtained by the conventional method (without stabilizer) were monitored for two weeks and analyzed. Results were compared. (author)

  5. Thyroglobulin Gene Mutation with Cold Nodule on Thyroid Scintigraphy

    Directory of Open Access Journals (Sweden)

    Toshio Kahara

    2012-01-01

    Full Text Available Thyroglobulin gene mutation is a rare cause of congenital hypothyroidism, but thyroglobulin gene mutations are thought to be associated with thyroid cancer development. A 21-year-old Japanese man treated with levothyroxine for congenital hypothyroidism had an enlarged thyroid gland with undetectable serum thyroglobulin despite elevated serum TSH level. The patient was diagnosed with thyroglobulin gene mutation, with compound heterozygosity for Gly304Cys missense mutation and Arg432X nonsense mutation. Ultrasonography showed a hypovascular large tumor in the left lobe that appeared as a cold nodule on thyroid scintigraphy. He underwent total thyroidectomy, but pathological study did not reveal findings of thyroid carcinoma, but rather a hyperplastic nodule with hemorrhage. Strong cytoplasmic thyroglobulin immunostaining was observed, but sodium iodide symporter immunostaining was hardly detected in the hyperplastic nodule. The clinical characteristics of patients with thyroglobulin gene mutations are diverse, and some patients are diagnosed by chance on examination of goiter in adults. The presence of thyroid tumors that appear as cold nodules on thyroid scintigraphy should consider the potential for thyroid carcinoma, if the patient has relatively low serum thyroglobulin concentration in relation to the degree of TSH without thyroglobulin autoantibody.

  6. Detection of carrier heterogeneity by rate of ligand dialysis: medium-chain fatty acid interaction with human serum albumin and competition with chloride

    DEFF Research Database (Denmark)

    Honoré, B; Brodersen, R

    1988-01-01

    Binding equilibria for decanoate, octanoate, and hexanoate to defatted human serum albumin were investigated by dialysis exchange rate determinations in 66 mM sodium phosphate buffer, pH 7.4, 37 degrees C. The binding isotherms for decanoate and octanoate could not be fitted by the general binding......(5) M-1, respectively, for decanoate; 1.6 X 10(6) and 3.5 X 10(4) for octanoate; and 7.1 X 10(4) and 8.0 X 10(2) M-1 for hexanoate. The high-affinity albumin component binds 1 mol decanoate, 1 mol octanoate, or 2 mol hexanoate more than is bound to the low-affinity component. Chloride ions compete...

  7. Study on the interaction between tabersonine and human serum albumin by optical spectroscopy and molecular modeling methods

    Energy Technology Data Exchange (ETDEWEB)

    Jiang Hua; Chen, Rongrong [Department of Biology, College of Life Science and Technology, Jinan University, Guangzhou 510632 (China); Pu Hanlin, E-mail: tphl@jnu.edu.cn [Department of Biology, College of Life Science and Technology, Jinan University, Guangzhou 510632 (China)

    2012-03-15

    The mechanism of interaction between tabersonine (TAB) and human serum albumin (HSA) was investigated by the methods of fluorescence spectroscopy, UV-vis absorption spectroscopy and molecular modeling under simulative physiological conditions. Results obtained from analysis of fluorescence spectrum and fluorescence intensity indicated that TAB has a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure. The binding site number n and apparent binding constant K{sub a}, corresponding thermodynamic parameters {Delta}G, {Delta}H and {Delta}S at different temperatures were calculated. The distance r between donor (human serum albumin) and acceptor (tabersonine) was obtained according to the Foerster theory of non-radiation energy transfer. The effect of common ions on binding constant was also investigated. The synchronous fluorescence and three-dimensional fluorescence spectra were used to investigate the structural change of HSA molecules with addition of TAB. Furthermore, the study of molecular modeling indicated that TAB could bind to the site I of HSA and hydrophobic interaction was the major acting force, which was in agreement with the binding mode study. - Highlights: Black-Right-Pointing-Pointer Fluorescence study of the mechanism of interaction between tabersonine and HSA. Black-Right-Pointing-Pointer The binding parameters and thermodynamic parameters were calculated. Black-Right-Pointing-Pointer The distance r was obtained and common ions effects was investigated. Black-Right-Pointing-Pointer Conformation of HSA and its molecular modeling was analyzed.

  8. Study of the interaction of kaempferol with bovine serum albumin

    Science.gov (United States)

    Tian, Jianniao; Liu, Jiaqin; Tian, Xuan; Hu, Zhide; Chen, Xingguo

    2004-03-01

    The binding of kaempferol with bovine serum albumin (BSA) was investigated at three temperatures, 296, 310 and 318 K, by the fluorescence, circular dichroism (CD) and Fourier transform infrared spectroscopy (FT-IR) at pH 7.40. The CD and FT-IR studies indicate that kaempferol binds strongly to BSA. The association constant K was determined by Stern-Volmer equation based on the quenching of the fluorescence BSA in the presence of kaempferol. The thermodynamic parameters were calculated according to the dependence of enthalpy change on the temperature as follows: Δ H0 and Δ S0 possess small negative (-1.694 kJ/mol) and positive values (88.814 J/mol K), respectively. According to the displacement experimental and the thermodynamic results, it is considered that kaempferol binding site II (subdomain III) mainly by hydrophobic interaction. The results studied by FT-IR and CD experiments indicate that the secondary structures of the protein have been changed by the interaction of kaempferol with BSA. The distance between the tryptophan residues in BSA and kaempferol bound to site II was estimated to be 2.78 nm using Foster's equation on the basis of fluorescence energy transfer.

  9. Polymorphism complexity and handedness inversion in serum albumin amyloid fibrils.

    Science.gov (United States)

    Usov, Ivan; Adamcik, Jozef; Mezzenga, Raffaele

    2013-12-23

    Protein-based amyloid fibrils can show a great variety of polymorphic structures within the same protein precursor, although the origins of these structural homologues remain poorly understood. In this work we investigate the fibrillation of bovine serum albumin--a model globular protein--and we follow the polymorphic evolution by a statistical analysis of high-resolution atomic force microscopy images, complemented, at larger length scales, by concepts based on polymer physics formalism. We identify six distinct classes of coexisting amyloid fibrils, including flexible left-handed twisted ribbons, rigid right-handed helical ribbons and nanotubes. We show that the rigid fibrils originate from flexible fibrils through two diverse polymorphic transitions, first, via a single-fibril transformation when the flexible left-handed twisted ribbons turn into the helical left-handed ribbons, to finally evolve into nanotube-like structures, and second, via a double-fibril transformation when two flexible left-handed twisted ribbons wind together resulting in a right-handed twisted ribbon, followed by a rigid right-handed helical ribbon polymorphic conformation. Hence, the change in handedness occurs with an increase in the level of the fibril's structural organization.

  10. Small-volume resuscitation from hemorrhagic shock with polymerized human serum albumin.

    Science.gov (United States)

    Messmer, Catalina; Yalcin, Ozlem; Palmer, Andre F; Cabrales, Pedro

    2012-10-01

    Human serum albumin (HSA) is used as a plasma expander; however, albumin is readily eliminated from the intravascular space. The objective of this study was to establish the effects of various-sized polymerized HSAs (PolyHSAs) during small-volume resuscitation from hemorrhagic shock on systemic parameters, microvascular hemodynamics, and functional capillary density in the hamster window chamber model. Polymerized HSA size was controlled by varying the cross-link density (ie, molar ratio of glutaraldehyde to HSA). Hemorrhage was induced by controlled arterial bleeding of 50% of the animal's blood volume (BV), and hypovolemic shock was maintained for 1 hour. Resuscitation was implemented in 2 phases, first, by infusion of 3.5% of the BV of hypertonic saline (7.5% NaCl) then followed by infusion of 10% of the BV of each PolyHSA. Resuscitation provided rapid recovery of blood pressure, blood gas parameters, and microvascular perfusion. Polymerized HSA at a glutaraldehyde-to-HSA molar ratio of 60:1 (PolyHSA(60:1)) provided superior recovery of blood pressure, microvascular blood flow, and functional capillary density, and acid-base balance, with sustained volume expansion in relation to the volume infused. The high molecular weight of PolyHSA(60:1) increased the hydrodynamic radius and solution viscosity. Pharmacokinetic analysis of PolyHSA(60:1) indicates reduced clearance and increased circulatory half-life compared with monomeric HSA and other PolyHSA formulations. In conclusion, HSA molecular size and solution viscosity affect central hemodynamics, microvascular blood flow, volume expansion, and circulation persistence during small-volume resuscitation from hemorrhagic shock. In addition, PolyHSA can be an alternative to HSA in pathophysiological situations with compromised vascular permeability. Copyright © 2012 Elsevier Inc. All rights reserved.

  11. The cytotoxic effect of spiroflavanone derivatives, their binding ability to human serum albumin (HSA) and a DFT study on the mechanism of their synthesis

    Science.gov (United States)

    Budzisz, Elzbieta; Paneth, Piotr; Geromino, Inacrist; Muzioł, Tadeusz; Rozalski, Marek; Krajewska, Urszula; Pipiak, Paulina; Ponczek, Michał B.; Małecka, Magdalena; Kupcewicz, Bogumiła

    2017-06-01

    This paper examines the cytotoxic effect of nine compounds with spiropyrazoline structures, and determines the reaction mechanism between diazomethane and selected benzylideneflavanones, their lipophilicity, and their binding ability to human serum albumin. The cytotoxic effect was determined on two human leukaemia cell lines (HL-60 and NALM-6) and melanoma WM-115 cells, as well as on normal human umbilical vein endothelial cells (HUVEC). The highest cytotoxicity was exhibited by compound B7: it was found to have an IC50 of less than 10 μM for all three cancer cell lines, with five to 12-fold lower sensitivity against normal cells (HUVEC). All the compounds exhibit comparable affinity energy in human serum albumin binding (from -8.1 to -8.6 kcal mol-1) but vary in their binding sites depending on the substituent. X-ray crystallography of two derivatives confirmed their synthetic pathway, and their structures were carefully examined.

  12. Tc-99m-Human Serum Albumin Transit Time as a Measure of Arm Breast Cancer-Related Lymphedema

    DEFF Research Database (Denmark)

    Toyserkani, Navid M; Hvidsten, Svend; Tabatabaeifar, Siavosh

    2017-01-01

    34-68 years, with unilateral arm lymphedema following breast cancer treatment underwent bilateral lymphoscintigraphy using intradermal injection in both hands of technetium-99m-labeled human serum albumin and sequential 5 min imaging for 5 hours. The mean transit time (MTT) in the arms was calculated...... based on time activity curves generated from injection site and arm regions. Visual lymphedema scoring was performed based on dermal backflow and lymph node presence. Excess arm volume was calculated from circumference measurements. RESULTS: The MTT (mean ± SD) was significantly longer in the lymphedema...

  13. Pulse radiolytic and spectrophotometric investigation of the binding of bilirubin to bovine serum albumin

    International Nuclear Information System (INIS)

    Adhikari, S.; Guha, S.N.; Gopinathan, C.

    1994-01-01

    Bilirubin (BR) exhibits marked change in its absorption properties in the presence of bovine serum albumin (BSA). The λ max of BR observed at 440 nm is red shifted by about 20 nm with 8% increase in band intensity when BSA is present in the matrix. Medium polarity and salt effects were also studied in this system and it was inferred that BR is bound to BSA to form a complex, which becomes unstable at high salt concentration or in a medium of low dielectric constant such as water-alcohol mixture. Pulse radiolysis study of this system employing CO 2 .- radical revealed that BR blocks the sites of CO 2 .- attack in the BSA molecule. (author). 3 refs., 2 figs

  14. alpha-Glucosidase-albumin conjugates: effect of chronic administration in mice

    International Nuclear Information System (INIS)

    Allen, T.M.; Murray, L.; Bhardwaj, D.; Poznansky, M.J.

    1985-01-01

    Enzyme albumin conjugates have been proposed as a means of increasing the efficacy of enzyme use in vivo and decreasing immune response to the enzyme. Particulate drug carriers, however, have a pronounced tendency to localize in the mononuclear phagocyte (reticuloendothelial) system. The authors have examined in mice the effect on phagocytic index, tissue distribution and organ size of continued administration of conjugates of alpha-glucosidase with either homologous or heterologous albumin. Mice received 10 X 2-mg injections of bovine serum albumin (BSA) or mouse serum albumin (MSA), either free, polymerized or conjugated with alpha-glucosidase. Experiments involving BSA had to be terminated before the end of the experiment because of anaphylaxis, but these reactions were less severe to the polymerized albumin than to free albumin. Free BSA, BSA polymer and BSA-enzyme conjugates all caused a decrease in phagocytic index after six injections. Mice receiving MSA showed no evidence of anaphylaxis, but mice receiving six or more injections of free MSA, MSA polymer or MSA-enzyme conjugate had significantly decreased phagocytic indices as compared to controls. Phagocytic indices had returned to normal by 7 days after the final injection. Tissue distribution of 125 I-labeled albumin preparations was determined in either naive or chronically injected mice

  15. Aggregation of bovine serum albumin upon cleavage of its disulfide bonds, studied by the time-resolved small-angle X-ray scattering technique with synchrotron radiation

    Energy Technology Data Exchange (ETDEWEB)

    Ueki, Tatzuo; Inoko, Yoji; Hiragi, Yuzuru; Kataoka, Mikio; Amemiya, Yoshiyuki; Izumi, Yoshinobu; Tagawa, Hiroyuki; Muroga, Yoshio

    1985-11-01

    A rapid mixing system of the stopped-flow type, used with small-angle X-ray scattering equipment using synchrotron radiation, is described. The process of aggregation of bovine serum albumin was traced with a time interval of 50s, initiated upon cleavage of its disulfide bonds by reduction with dithiothreitol. The results indicate that a 218-fold molar excess of dithiothreitol over the number of moles of disulfide bonds in bovine serum albumin is sufficient to initiate the reaction immediately after mixing, which reaches equilibrium in about 15 min. On the other hand, half this amount is not sufficient to initiate the reaction, so that the reaction is delayed by about 150s. Such a single-shot time-resolved experiment showed that experiments with a time interval of 100 ms are possible with repeated multi-shot runs. 26 refs.; 8 figs.

  16. Aggregation of bovine serum albumin upon cleavage of its disulfide bonds, studied by the time-resolved small-angle X-ray scattering technique with synchrotron radiation

    International Nuclear Information System (INIS)

    Ueki, Tatzuo; Inoko, Yoji; Izumi, Yoshinobu; Tagawa, Hiroyuki; Muroga, Yoshio

    1985-01-01

    A rapid mixing system of the stopped-flow type, used with small-angle X-ray scattering equipment using synchrotron radiation, is described. The process of aggregation of bovine serum albumin was traced with a time interval of 50 s, initiated upon cleavage of its disulfide bonds by reduction with dithiothreitol. The results indicate that a 218-fold molar excess of dithiothreitol over the number of moles of disulfide bonds in bovine serum albumin is sufficient to initiate the reaction immediately after mixing, which reaches equilibrium in about 15 min. On the other hand, half this amount is not sufficient to initiate the reaction, so that the reaction is delayed by about 150 s. Such a single-shot time-resolved experiment showed that experiments with a time interval of 100 ms are possible with repeated multi-shot runs. (Auth.)

  17. Recognition of malignant processes with neural nets from ESR spectra of serum albumin

    Energy Technology Data Exchange (ETDEWEB)

    Seidel, P. [Inst. of Medical Physics and Biophysics, Univ. Leipzig (Germany); Gurachevsky, A.; Muravsky, V.; Schnurr, K.; Seibt, G. [Medinnovation GmbH, Wildau (Germany); Matthes, G. [Inst. of Transfusion Medicine, Univ. Hospital Leipzig (Germany)

    2005-07-01

    Cancer diseases are the focus of intense research due to their frequent occurrence. It is known from the literature that serum proteins are changed in the case of malignant processes. Changes of albumin conformation, transport efficiency, and binding characteristics can be determined by electron spin resonance spectroscopy (ESR). The present study analysed the binding/dissociation function of albumin with an ESR method using 16-doxyl stearate spin probe as reporter molecule and ethanol as modifier of hydrophobic interactions. Native and frozen plasma of healthy donors (608 samples), patients with malignant diseases (423 samples), and patients with benign conditions (221 samples) were analysed. The global specificity was 91% and the sensitivity 96%. In look-back samples of 27 donors, a malignant process could be detected up to 30 months before clinical diagnosis. To recognise different entities of malignant diseases from the ESR spectra, Artificial neural networks were implemented. For 48 female donors with breast cancer, the recognition specificity was 85%. Other carcinoma entities (22 colon, 18 prostate, 12 stomach) were recognised with specificities between 75% and 84%. Should these specificity values be reproduced in larger studies, the described method could be used as a new specific tumour marker for the early detection of malignant processes. Since transmission of cancer via blood transfusion cannot be excluded as yet, the described ESR method could also be used as a quality test for plasma products. (orig.)

  18. Recognition of malignant processes with neural nets from ESR spectra of serum albumin

    International Nuclear Information System (INIS)

    Seidel, P.; Gurachevsky, A.; Muravsky, V.; Schnurr, K.; Seibt, G.; Matthes, G.

    2005-01-01

    Cancer diseases are the focus of intense research due to their frequent occurrence. It is known from the literature that serum proteins are changed in the case of malignant processes. Changes of albumin conformation, transport efficiency, and binding characteristics can be determined by electron spin resonance spectroscopy (ESR). The present study analysed the binding/dissociation function of albumin with an ESR method using 16-doxyl stearate spin probe as reporter molecule and ethanol as modifier of hydrophobic interactions. Native and frozen plasma of healthy donors (608 samples), patients with malignant diseases (423 samples), and patients with benign conditions (221 samples) were analysed. The global specificity was 91% and the sensitivity 96%. In look-back samples of 27 donors, a malignant process could be detected up to 30 months before clinical diagnosis. To recognise different entities of malignant diseases from the ESR spectra, Artificial neural networks were implemented. For 48 female donors with breast cancer, the recognition specificity was 85%. Other carcinoma entities (22 colon, 18 prostate, 12 stomach) were recognised with specificities between 75% and 84%. Should these specificity values be reproduced in larger studies, the described method could be used as a new specific tumour marker for the early detection of malignant processes. Since transmission of cancer via blood transfusion cannot be excluded as yet, the described ESR method could also be used as a quality test for plasma products. (orig.)

  19. Spectroscopic studies on the binding of barbital to bovine serum albumin

    International Nuclear Information System (INIS)

    Ding Fei; Pan Hong; Li Zhiyuan; Liu Feng; Sun Ying

    2009-01-01

    In this paper, the interaction between barbital and bovine serum albumin (BSA) was investigated by the method of fluorescence spectroscopy under simulative physiological conditions. Fluorescence data revealed that the fluorescence quenching of BSA by barbital was the result of the formation of BSA-barbital complex, and the effective quenching constants (K a ) were 1.468x10 4 , 1.445x10 4 and 1.403x10 4 M -1 at 297, 303 and 310 K, respectively. The thermodynamic parameters enthalpy change (ΔH) and entropy change (ΔS) for the reaction were calculated to be -2.679 kJ mol -1 and 70.76 J mol -1 K -1 , respectively, according to the van't Hoff equation. The results indicated that hydrophobic and electrostatic interactions were the dominant intermolecular force in stabilizing the complex. The results of synchronous fluorescence spectra showed that binding of barbital with BSA can induce conformational changes in BSA. In addition, the effects of Cu 2+ and Zn 2+ on the constants of BSA-barbital complex were also discussed.

  20. Evaluation on the toxicity of nanoAg to bovine serum albumin

    Energy Technology Data Exchange (ETDEWEB)

    Liu Rutao, E-mail: rutaoliu@sdu.edu.cn [School of Environmental Science and Engineering, Shandong University, 27 Shanda South Road, Jinan 250100 (China); Sun Feng; Zhang Lijun; Zong Wansong; Zhao Xingchen; Wang Li; Wu Ruolin [School of Environmental Science and Engineering, Shandong University, 27 Shanda South Road, Jinan 250100 (China); Hao Xiaopeng [State Key Laboratory of Crystal Materials, Shandong University, Jinan, 250100 (China)

    2009-06-15

    Measuring protein damage by nanomaterials may give insight into the mechanisms of toxicity of nanomaterials. The toxic effects of nanoAg on bovine serum albumin (BSA) were thoroughly studied using fluorescence spectroscopy, ultraviolet-visible absorption spectroscopy, resonance light scattering spectroscopy (RLS), circular dichroism spectroscopy (CD) and transmission electron microscopy (TEM). NanoAg had obvious toxic effects on BSA: nanoAg could increase the amount of helix and decrease the beta sheet structure, leading to a loosening of the protein skeleton. In the loose structure, internal hydrophobic amino acids are exposed and the characteristic fluorescence of BSA is obviously quenched. When the ratio of nanoAg and BSA increased to 1: 96 (wt/wt), the impact of nanoAg on the spectral properties leveled off. The RLS spectrum, TEM, CD spectra and electrophoresis results showed that BSA had destroyed the double-layer structure of nanoAg and covered its surface, generating a BSA-nanoAg complex held together by van der Waals and electrostatic forces. This paper provides a new perspective and method for determining the toxic effects of nanoAg on biological macromolecules.

  1. Vertebral uptake of Tc-99m macroaggregated albumin (MAA) with SPECT/CT occurring in superior vena cava obstruction

    Energy Technology Data Exchange (ETDEWEB)

    Karls, Shawn; Hassoun, Hani; Derbekyan, Vilma [Dept. of Nuclear Madicine, Royal Victoria Hospital, Montreal (Canada)

    2016-09-15

    A 67-year-old male presented with dyspnea for which lung scintigraphy was ordered to rule out pulmonary embolus. Planar images demonstrated abnormal midline uptake of Tc-99m macroaggregated albumin, which SPECT/CT localized to several thoracic vertebrae. Thoracic vertebral uptake on perfusion lung scintigraphy was previously described on planar imaging. Radionuclide venography and contrast-enhanced CT subsequently demonstrated superior vena cava (SVC) obstruction with collateralization through the azygous/hemiazygous system and vertebral venous plexus. SPECT/CT differentiated residual esophageal/tracheal ventilation activity, a clinically insignificant finding, from vertebral uptake indicative of SVC obstruction, a potentially life-threatening condition.

  2. Bilirubin Albumin Binding and Unbound Unconjugated Hyperbilirubinemia in Premature Infants.

    Science.gov (United States)

    Amin, Sanjiv B; Wang, Hongyue

    2018-01-01

    To evaluate the associations between unbound bilirubin (UB) and total serum bilirubin (TSB), bilirubin:albumin molar ratio (BAMR), and bilirubin albumin binding affinity (Ka) as a f