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Sample records for albumins

  1. Protein Crystal Serum Albumin

    Science.gov (United States)

    1998-01-01

    As the most abundant protein in the circulatory system albumin contributes 80% to colloid osmotic blood pressure. Albumin is also chiefly responsible for the maintenance of blood pH. It is located in every tissue and bodily secretion, with extracellular protein comprising 60% of total albumin. Perhaps the most outstanding property of albumin is its ability to bind reversibly to an incredible variety of ligands. It is widely accepted in the pharmaceutical industry that the overall distribution, metabolism, and efficiency of many drugs are rendered ineffective because of their unusually high affinity for this abundant protein. An understanding of the chemistry of the various classes of pharmaceutical interactions with albumin can suggest new approaches to drug therapy and design. Principal Investigator: Dan Carter/New Century Pharmaceuticals

  2. Urinary albumin in space missions

    DEFF Research Database (Denmark)

    Cirillo, Massimo; De Santo, Natale G; Heer, Martina

    2002-01-01

    Proteinuria was hypothesized for space mission but research data are missing. Urinary albumin, as index of proteinuria, was analyzed in frozen urine samples collected by astronauts during space missions onboard MIR station and on ground (control). Urinary albumin was measured by a double antibody...... radioimmunoassay. On average, 24h urinary albumin was 27.4% lower in space than on ground; the difference was statistically significant. Low urinary albumin excretion could be another effect of exposure to weightlessness (microgravity)....

  3. Serum albumin: touchstone or totem?

    Science.gov (United States)

    Margarson, M P; Soni, N

    1998-08-01

    A decrease in serum albumin concentrations is an almost inevitable finding in disease states, and is primarily mediated in the acute phase by alterations in vascular permeability and redistribution. This change is not disease specific but marked changes that persist are generally associated with a poorer prognosis. Critical appraisal of long-standing practices and the availability of alternative colloid solutions have led to a reduction in albumin replacement therapy, and a widespread tolerance of lower albumin concentrations in patients. The factors determining serum albumin concentrations, their measurement and the implications of hypoalbuminaemia are reviewed. The clinical value of serum albumin measurement is discussed.

  4. Albumin-based drug delivery

    DEFF Research Database (Denmark)

    Larsen, Maja Thim; Kuhlmann, Matthias; Hvam, Michael Lykke

    2016-01-01

    The effectiveness of a drug is dependent on accumulation at the site of action at therapeutic levels, however, challenges such as rapid renal clearance, degradation or non-specific accumulation requires drug delivery enabling technologies. Albumin is a natural transport protein with multiple ligand...... binding sites, cellular receptor engagement, and a long circulatory half-life due to interaction with the recycling neonatal Fc receptor. Exploitation of these properties promotes albumin as an attractive candidate for half-life extension and targeted intracellular delivery of drugs attached by covalent...... conjugation, genetic fusions, association or ligand-mediated association. This review will give an overview of albumin-based products with focus on the natural biological properties and molecular interactions that can be harnessed for the design of a next-generation drug delivery platform....

  5. Amadori albumin in diabetic nephropathy

    Directory of Open Access Journals (Sweden)

    Km. Neelofar

    2015-01-01

    Full Text Available Nonenzymatic glycation of macromolecules in diabetes mellitus (DM is accelerated due to persistent hyperglycemia. Reducing sugar such as glucose reacts non enzymatically with free €- amino groups of proteins through series of reactions forming Schiff bases. These bases are converted into Amadori product and further into AGEs. Non enzymatic glycation has the potential to alter the biological, structural and functional properties of macromolecules both in vitro and in vivo. Studies have suggested that amadori as well as AGEs are involved in the micro-macro vascular complications in DM, but most studies have focused on the role of AGEs in vascular complications of diabetes. Recently putative AGE-induced patho-physiology has shifted attention from the possible role of amadori-modified proteins, the predominant form of the glycated proteins in the development of the diabetic complications. Human serum albumin (HSA, the most abundant protein in circulation contains 59 lysine and 23 arginine residues that could, in theory be involved in glycation. Albumin has dual nature, first as a marker of intermediate glycation and second as a causative agent of the damage of tissues. Among the blood proteins, hemoglobin and albumin are the most common proteins that are glycated. HSA with a shorter half life than RBC, appears to be an alternative marker of glycemic control as it can indicate blood glucose status over a short period (2-3 weeks and being unaffected by RBCs life span and variant haemoglobin, anemia etc which however, affect HbA1c. On the other hand, Amadori albumin may accumulate in the body tissues of the diabetic patients and participate in secondary complications. Amadori-albumin has potential role in diabetic glomerulosclerosis due to long term hyperglycaemia and plays an important role in the pathogenesis of diabetic nephropathy. This review is an approach to compile both the nature of glycated albumin as a damaging agent of tissues and as an

  6. 21 CFR 640.80 - Albumin (Human).

    Science.gov (United States)

    2010-04-01

    ... 21 Food and Drugs 7 2010-04-01 2010-04-01 false Albumin (Human). 640.80 Section 640.80 Food and Drugs FOOD AND DRUG ADMINISTRATION, DEPARTMENT OF HEALTH AND HUMAN SERVICES (CONTINUED) BIOLOGICS ADDITIONAL STANDARDS FOR HUMAN BLOOD AND BLOOD PRODUCTS Albumin (Human) § 640.80 Albumin (Human). (a)...

  7. Human microglial cells synthesize albumin in brain.

    Directory of Open Access Journals (Sweden)

    Sung-Min Ahn

    Full Text Available Albumin, an abundant plasma protein with multifunctional properties, is mainly synthesized in the liver. Albumin has been implicated in Alzheimer's disease (AD since it can bind to and transport amyloid beta (Abeta, the causative agent of AD; albumin is also a potent inhibitor of Abeta polymerization. Despite evidence of non-hepatic transcription of albumin in many tissues including kidney and pancreas, non-hepatic synthesis of albumin at the protein level has been rarely confirmed. In a pilot phase study of Human Brain Proteome Project, we found evidence that microglial cells in brain may synthesize albumin. Here we report, for the first time, the de novo synthesis of albumin in human microglial cells in brain. Furthermore, we demonstrate that the synthesis and secretion of albumin from microglial cells is enhanced upon microglial activation by Abeta(1-42- or lipopolysaccharide (LPS-treatment. These data indicate that microglial cells may play a beneficial role in AD by secreting albumin that not only inhibits Abeta polymerization but also increases its clearance.

  8. Preparation and characterization of microspheres of albumin-heparin conjugates

    NARCIS (Netherlands)

    Kwon, Glen S.; Bae, You Han; Kim, Sung Wan; Cremers, Harry; 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 albumin-hepar

  9. ALBUMIN AS PROGNOSTIC VALUE IN HOSPITALISED PATIENTS

    Directory of Open Access Journals (Sweden)

    Chakrapani Alavala

    2016-07-01

    Full Text Available BACKGROUND In cases of a pathological state, there might be a low formation of the albumin in liver or high degradation of the albumin. In either of the ways, the serum albumin will be lowered. Stress and strain is also known to cause hypoalbuminemia i.e. low serum level of albumin. Since albumin is a protein, it has to be transcribed from the genes and studies have shown that TNF-alpha supresses this transcription process. The TNF-alpha is known to increase in any inflammation and thus forms a cascade. In case of hospitalised patients, the stress and strain in pre-surgical patients and chronically hospitalised patients, the serum albumin levels are known to be less than normal. In chronically hospitalised patients, the nutritional cause can also be taken into consideration for lower serum albumin levels. Early detection of these low levels of serum albumin levels helps the surgeons and the physicians to intervene and thus cut off the progression of the disease. A sincere effort has been made in this study to understand the relations of the serum albumin level and its effects on the prognosis of the disease and outcome of the surgery if the patient is undergoing any. This study is intended to help the physician, surgeon, and general practitioners to understand and intervene in the event and thus help the patient to recover earlier and in a better way. METHODS Aim of the study is to estimate the mean serum albumin levels in hospitalised patients to estimate the mean serum albumin levels in patients undergoing surgery and to correlate the serum albumin levels and the prognosis of the patient. The study has been done in the Department of Surgery, Government Medical College, Nizamabad. The study was done from October 2013 to November 2014. The study is a cross-sectional study. The study is also double blinded and randomised. The study is a multi-level study. The sample size included one hundred patients. One hundred patients were identified in the

  10. [Urinary albumin fragmentation and immunoreactivity].

    Science.gov (United States)

    Kurihara, Yuriko; Nishimaki, Junichi; Nakajima, Toshie; Ida, Takashi; Shiba, Kiyoko

    2009-02-01

    Urinary albumin (ALB) has been measured as a marker for the early detection of diabetic nephropathy. In 2004, Comper et al. developed a gel-filtration high-performance liquid chromatography (HPLC) procedure for the determination of urinary ALB. They demonstrated the presence in its albumin fraction of non immunoreactive ALB with the total molecular weight of a monomeric ALB that was non-reactive with the existing anti-ALB antibody, and reported that the level of urinary non-immunoreactive ALB was higher in diabetic patients than in normal subjects. In this study, we isolated urinary ALB from diabetic patients using an anti-ALB antibody-coupled affinity column to test its immunoreactivity. In some diabetic patients, the results of HPLC and turbidimetric immunoassay for urinary ALB were discrepant. Western blot analysis showed that ALB samples from such patients were contaminated with proteins other than ALB, and contained ALB, whose molecular weight became lower using a reductive procedure. In addition, the reactivity of ALB with anti-ALB antibody differed depending on whether it was in a reduced or non-reduced state. These results indicate that ALB in such patients is susceptible to structural changes due to disease-induced urinary factors and, thus, their urine contains ALB with an altered reactivity to antibody.

  11. Total Protein and Albumin/Globulin Ratio Test

    Science.gov (United States)

    ... limited. Home Visit Global Sites Search Help? Total Protein and Albumin/Globulin (A/G) Ratio Share this ... Globulin Ratio; A/G Ratio Formal name: Total Protein; Albumin to Globulin Ratio Related tests: Albumin ; Liver ...

  12. Fibrinogen adsorption on blocked surface of albumin

    DEFF Research Database (Denmark)

    Holmberg, Maria; Hou, Xiaolin

    2011-01-01

    We have investigated the adsorption of albumin and fibrinogen onto PET (polyethylene terephthalate) and glass surfaces and how pre-adsorption of albumin onto these surfaces can affect the adsorption of later added fibrinogen. For materials and devices being exposed to blood, adsorption...... of fibrinogen is often a non-wanted event, since fibrinogen is part of the clotting cascade and unspecific adsorption of fibrinogen can have an influence on the activation of platelets. Albumin is often used as blocking agent for avoiding unspecific protein adsorption onto surfaces in devices designed to handle...... energies, the adsorption of both albumin and fibrinogen has been monitored simultaneously on the same sample. Information about topography and coverage of adsorbed protein layers has been obtained using AFM (Atomic Force Microscopy) analysis in liquid. Our studies show that albumin adsorbs in a multilayer...

  13. Cubilin is an albumin binding protein important for renal tubular albumin reabsorption.

    Science.gov (United States)

    Birn, H; Fyfe, J C; Jacobsen, C; Mounier, F; Verroust, P J; Orskov, H; Willnow, T E; Moestrup, S K; Christensen, E I

    2000-05-01

    Using affinity chromatography and surface plasmon resonance analysis, we have identified cubilin, a 460-kDa receptor heavily expressed in kidney proximal tubule epithelial cells, as an albumin binding protein. Dogs with a functional defect in cubilin excrete large amounts of albumin in combination with virtually abolished proximal tubule reabsorption, showing the critical role for cubilin in the uptake of albumin by the proximal tubule. Also, by immunoblotting and immunocytochemistry we show that previously identified low-molecular-weight renal albumin binding proteins are fragments of cubilin. In addition, we find that mice lacking the endocytic receptor megalin show altered urinary excretion, and reduced tubular reabsorption, of albumin. Because cubilin has been shown to colocalize and interact with megalin, we propose a mechanism of albumin reabsorption mediated by both of these proteins. This process may prove important for understanding interstitial renal inflammation and fibrosis caused by proximal tubule uptake of an increased load of filtered albumin.

  14. 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...

  15. Cubilin is an albumin binding protein important for renal tubular albumin reabsorption

    OpenAIRE

    Birn, H.; J. C. Fyfe; Jacobsen, C.; Mounier, F.; Verroust, P. J.; Orskov, H; Willnow, T.E.; Moestrup, S K; Christensen, E I

    2000-01-01

    Using affinity chromatography and surface plasmon resonance analysis, we have identified cubilin, a 460-kDa receptor heavily expressed in kidney proximal tubule epithelial cells, as an albumin binding protein. Dogs with a functional defect in cubilin excrete large amounts of albumin in combination with virtually abolished proximal tubule reabsorption, showing the critical role for cubilin in the uptake of albumin by the proximal tubule. Also, by immunoblotting and immunocytochemistry we show ...

  16. A review of albumin binding in CKD.

    Science.gov (United States)

    Meijers, Björn K I; Bammens, Bert; Verbeke, Kristin; Evenepoel, Pieter

    2008-05-01

    Hypoalbuminemia is associated with excess mortality in patients with kidney disease. Albumin is an important oxidant scavenger and an abundant carrier protein for numerous endogenous and exogenous compounds. Several specific binding sites for anionic, neutral, and cationic ligands were described. Overall, the extent of binding depends on the ligand and albumin concentration, albumin-binding affinity, and presence of competing ligands. Chronic kidney disease affects all these determinants. This may result in altered pharmacokinetics and increased risk of toxicity. Renal clearance of albumin-bound solutes mainly depends on tubular clearance. Dialytic clearance by means of conventional hemodialysis/hemofiltration and peritoneal dialysis is limited. Other epuration techniques combining hemodialysis with adsorption have been developed. However, the benefit of these techniques remains to be proved.

  17. Paclitaxel Albumin-stabilized Nanoparticle Formulation

    Science.gov (United States)

    This page contains brief information about paclitaxel albumin-stabilized nanoparticle formulation and a collection of links to more information about the use of this drug, research results, and ongoing clinical trials.

  18. Distribution and degradation of albumin in extensive skin disease

    DEFF Research Database (Denmark)

    Worm, Anne-Marie; Taaning, E; Rossing, N;

    1981-01-01

    The distribution and degradation of albumin were determined in twelve patients with extensive skin disease and in ten control subjects by measuring the metabolic turnover and transcapillary escape of 132 I-labelled albumin. The ratio of intravascular to total mass of albumin was normal. Thus the ...... catabolic rate of albumin supports the concept of a causal relationship between these parameters....

  19. 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.

  20. Bisalbuminemia. A new molecular variant, albumin Vancouver.

    Science.gov (United States)

    Frohlich, J; Kozier, J; Campbell, D J; Curnow, J V; Tárnoky, A L

    1978-11-01

    Of 18 members of a Fiji Indian family investigated, eight of the 12 males and two of the six females had an electrophoretically slow-type bisalbuminemia (alloalbuminemia). The albumin was characterized by the hiterto unique ratio of the two bands (Al A 35%: variant 65%), and by dye-binding studies and electrophoretic mobility in different media. The data suggest that this is a new variant, which we propose to call albumin Vancouver (Al Va).

  1. Foaming properties of guar foaming albumin

    OpenAIRE

    細見, 典子; Hosomi, Noriko; 原田, 麻子; Harada, Asako; 下山, 亜美; Shimoyama, Ami; 土居, 幸雄; Doi, Yukio

    2009-01-01

    From guar meal we recently isolated an albumin fraction with a high foaming ability, named guar foaming albumin (GFA) . Here, we further characterized the foaming activity, foam stability and surface tension of GFA solutions. Foaming activity and foam stability were estimated by measuring the conductivity of foam using a glass column with a conductivity cell. Surface tension was measured by the drop weight method using a stalagmometer. GFA showed higher foaming activity than casein at any pro...

  2. How albumin administration for cirrhosis impacts on hospital albumin consumption and expenditure

    Institute of Scientific and Technical Information of China (English)

    Federica Mirici-Cappa; Paolo Caraceni; Marco Domenicali; Ernesto Gelonesi; Barbara Benazzi; Giacomo Zaccherini; Franco Trevisani; Cristina Puggioli; Mauro Bernardi

    2011-01-01

    AIM: To assess the impact of guidelines for albumin prescription in an academic hospital, which is a referral center for liver diseases. METHODS: Although randomized trials and guidelines support albumin administration for some complications of cirrhosis, the high cost of albumin greatly limits its use in clinical practice. In 2003, a multidisciplinary panel at Sant'Orsola-Malpighi University Hospital (Bologna, Italy) used a literature-based consensus method to list all the acute and chronic conditions for which albumin is indicated as first- or second-line treatment. Indications in hepatology included prevention of post-paracentesis circulatory dysfunction and renal failure induced by spontaneous bacterial peritonitis, and treatment of hepatorenal syndrome and refractory ascites. Although still debated, albumin administration in refractory ascites is

  3. Binding of Sulpiride to Seric Albumins.

    Science.gov (United States)

    da Silva Fragoso, Viviane Muniz; de Morais Coura, Carla Patrícia; Hoppe, Luanda Yanaan; Soares, Marília Amável Gomes; Silva, Dilson; Cortez, Celia Martins

    2016-01-04

    The aim of this work was to study the interaction of sulpiride with human serum albumin (HSA) and bovine serum albumin (BSA) through the fluorescence quenching technique. As sulpiride molecules emit fluorescence, we have developed a simple mathematical model to discriminate the quencher fluorescence from the albumin fluorescence in the solution where they interact. Sulpiride is an antipsychotic used in the treatment of several psychiatric disorders. We selectively excited the fluorescence of tryptophan residues with 290 nm wavelength and observed the quenching by titrating HSA and BSA solutions with sulpiride. Stern-Volmer graphs were plotted and quenching constants were estimated. Results showed that sulpiride form complexes with both albumins. Estimated association constants for the interaction sulpiride-HSA were 2.20 (±0.08) × 10⁴ M(-1), at 37 °C, and 5.46 (±0.20) × 10⁴ M(-1), at 25 °C. Those for the interaction sulpiride-BSA are 0.44 (±0.01) × 10⁴ M(-1), at 37 °C and 2.17 (±0.04) × 10⁴ M(-1), at 25 °C. The quenching intensity of BSA, which contains two tryptophan residues in the peptide chain, was found to be higher than that of HSA, what suggests that the primary binding site for sulpiride in albumin should be located next to the sub domain IB of the protein structure.

  4. Binding of Sulpiride to Seric Albumins

    Directory of Open Access Journals (Sweden)

    Viviane Muniz da Silva Fragoso

    2016-01-01

    Full Text Available The aim of this work was to study the interaction of sulpiride with human serum albumin (HSA and bovine serum albumin (BSA through the fluorescence quenching technique. As sulpiride molecules emit fluorescence, we have developed a simple mathematical model to discriminate the quencher fluorescence from the albumin fluorescence in the solution where they interact. Sulpiride is an antipsychotic used in the treatment of several psychiatric disorders. We selectively excited the fluorescence of tryptophan residues with 290 nm wavelength and observed the quenching by titrating HSA and BSA solutions with sulpiride. Stern-Volmer graphs were plotted and quenching constants were estimated. Results showed that sulpiride form complexes with both albumins. Estimated association constants for the interaction sulpiride–HSA were 2.20 (±0.08 × 104 M−1, at 37 °C, and 5.46 (±0.20 × 104 M−1, at 25 °C. Those for the interaction sulpiride-BSA are 0.44 (±0.01 × 104 M−1, at 37 °C and 2.17 (±0.04 × 104 M−1, at 25 °C. The quenching intensity of BSA, which contains two tryptophan residues in the peptide chain, was found to be higher than that of HSA, what suggests that the primary binding site for sulpiride in albumin should be located next to the sub domain IB of the protein structure.

  5. Imidazole binding to human serum albumin.

    Science.gov (United States)

    Rodrigo, M C; Ceballos, A; Mariño, E; Cachaza, J M; Domínguez-Gil, A; Kuemmerle, H P

    1988-06-01

    Imidazole is a substance released by the organism when a new salicylate derivative, imidazole salicylate is administered. A study was made of the binding of imidazole to human serum albumin by an in vitro assay employing an ultrafiltration technique. For the concentration range that imidazole was found in plasma following administration of the drug to healthy volunteers, the mean binding percentages were: 12.1 +/- 1.8 and 19.7 +/- 3.1 at 37 degrees C and 25 degrees C, respectively. The results obtained in the study follow a model entailing three equal and independent binding sites of imidazole to serum albumin and the values of the corresponding constants were determined. Apparently, the presence in the plasma samples of sodium salicylate at a concentration of 100 micrograms/ml does not affect the binding of imidazole to human serum albumin.

  6. Bidirectional peritoneal transport of albumin in continuous ambulatory peritoneal dialysis

    DEFF Research Database (Denmark)

    Joffe, P; Henriksen, Jens Henrik Sahl

    1995-01-01

    The present study was undertaken in order to assess bidirectional peritoneal kinetics of albumin after simultaneous i.v. and i.p. injection of radioiodinated albumin tracers (125I-RISA and 131I-RISA) in eight clinically stable uraemic patients undergoing continuous ambulatory peritoneal dialysis...... (CAPD). The plasma volume, intravascular albumin mass (IVM), and overall extravasation rate of albumin were not significantly different from that found in healthy controls. Albumin flux from the plasma into the peritoneal cavity was 3.71 +/- 0.82 (SD) mumol/h, which was only 3% of the overall...... extravasation rate (137 +/- 52 mumol/h). Albumin flux from the peritoneal cavity into the plasma was substantially lower (0.22 +/- 0.07 mumol/h, P peritoneal accumulation of the albumin from plasma over 4 h was 14 +/- 3.2 mumol, which was significantly lower than the intraperitoneal albumin...

  7. 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...

  8. 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...

  9. Interaction of Citrinin with Human Serum Albumin

    Directory of Open Access Journals (Sweden)

    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.

  10. 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 iod......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...... 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...

  11. Preparation and characterization of albumin-heparin microspheres

    NARCIS (Netherlands)

    Cremers, H.F.M.; Kwon, G.; Bae, Y.H.; Kim, S.W.; Verrijk, R.; Noteborn, H.P.J.M.; Feijen, J.

    1994-01-01

    Albumin-heparin microspheres were prepared by a two-step process which involved the preparation of a soluble albumin-heparin conjugate, followed by formation of microspheres from this conjugate or by a double cross-linking technique involving both coupling of soluble albumin and heparin and microsph

  12. Release of macromolecules from albumin-heparin microspheres

    NARCIS (Netherlands)

    Kwon, Glen S.; Bae, You Han; Cremers, Harry; Feijen, Jan; Kim, Sung Wan

    1992-01-01

    Hydrophilic microspheres based on albumin-heparin conjugates have been prepared as a macromolecular delivery system. The soluble albumin-heparin conjugate was synthesized and crosslinked in a water-in-oil emulsion with glutaraldehyde to form microspheres in the same manner as for albumin microsphere

  13. Binding of disodium cromoglycate to human serum albumin

    Science.gov (United States)

    Ochoa de Aspuru, Eduardo; Zatón, Ana M. L.

    1998-07-01

    The binding of several benzopiranone derivatives to human serum albumin was determined. The antiallergic drug disodium cromoglycate binds weakly to serum albumin. However, its precursors, chromones of smaller size, were able to bind in a hydrophobic pocket in the protein, and are carried by serum albumin in blood.

  14. Drug Delivery Vehicles Based on Albumin-Polymer Conjugates.

    Science.gov (United States)

    Jiang, Yanyan; Stenzel, Martina

    2016-06-01

    Albumin has been a popular building block to create nanoparticles for drug delivery purposes. The performance of albumin as a drug carrier can be enhanced by combining protein with polymers, which allows the design of carriers to encompass a broader spectrum of drugs while features unique to synthetic polymers such as stimuli-responsiveness are introduced. Nanoparticles based on polymer-albumin hybrids can be divided into two classes: one that carries album as a bioactive surface coating and the other that uses albumin as biocompatible, although nonbioactive, building block. Nanoparticles with bioactive albumin surface coating can either be prepared by self-assembly of albumin-polymer conjugates or by postcoating of existing nanoparticles with albumin. Albumin has also been used as building block, either in its native or denatured form. Existing albumin nanoparticles are coated with polymers, which can influence the degradation of albumin or impact on the drug release. Finally, an alternative way of using albumin by denaturing the protein to generate a highly functional chain, which can be modified with polymer, has been presented. These albumin nanoparticles are designed to be extremely versatile so that they can deliver a wide variety of drugs, including traditional hydrophobic drugs, metal-based drugs and even therapeutic proteins and siRNA.

  15. Detecting microalbuminuria by urinary albumin/creatinine concentration ratio

    DEFF Research Database (Denmark)

    Jensen, J S; Clausen, P; Borch-Johnsen, K;

    1997-01-01

    BACKGROUND: Microalbuminuria, i.e. a subclinical increase of the albumin excretion rate in urine, may be a novel atherosclerotic risk factor. This study aimed to test whether microalbuminuria can be identified by measurement of urinary albumin concentration or urinary albumin/creatinine concentra......BACKGROUND: Microalbuminuria, i.e. a subclinical increase of the albumin excretion rate in urine, may be a novel atherosclerotic risk factor. This study aimed to test whether microalbuminuria can be identified by measurement of urinary albumin concentration or urinary albumin/creatinine...... not included. Urinary albumin (Ualb) and creatinine (Ucreat) concentrations were measured in an overnight collected sample by enzyme-linked immunosorbent and colorimetric assays, respectively. Urinary albumin excretion rate (UAER) and urinary albumin/creatinine concentration ratio (Ualb/Ucreat) were calculated......, and 73%, 97%, and 73% for Ualb/Ucreat, respectively. CONCLUSIONS: It is concluded that measurement of the albumin/creatinine concentration ratio is a specific and quite sensitive alternative to measurement of the urinary albumin excretion rate in timed collections, when screening for microalbuminuria....

  16. Aluminium and nickel in human albumin solutions

    DEFF Research Database (Denmark)

    Gammelgaard, Bente; Sandberg, E

    1989-01-01

    Five different brands of commercially available human albumin solutions for infusion were analysed for their aluminium and nickel contents by atomic absorption spectrometry. The aluminium concentrations ranged from 12 micrograms/l to 1109 micrograms/l and the nickel concentrations ranged from 17...... micrograms/l to 77 micrograms/l. Examination of the aluminium and nickel contents of the constituents for the production of one brand showed too low levels to explain the final contamination of the product. By following the aluminium and nickel concentrations of the same brand during the production...... of a batch of albumin solution, filtration was shown to contribute to contamination, although the largest increase in aluminium as well as nickel concentrations appeared during the bulk concentrating process. To avoid health risks to certain patients, regulations should be established requiring aluminium...

  17. 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...... of proteases. The generation of protein-derived radicals also results in an enhancement of photobleaching of the porphyrin, suggesting that protein radical generation is linked to porphyrin photooxidation....

  18. Experimental investigation of the serum albumin fascia microstructure

    Science.gov (United States)

    Buzoverya, M. E.; Shcherbak, Yu. P.; Shishpor, I. V.

    2012-09-01

    The results of theoretical and experimental investigation of biological liquids are reported. Structural effects observed in fascias are considered with account of the molecular features of albumin and the concept of supramolecular organization of polymers. It is revealed that the morphology of human serum albumin fascias depends on the concentration and quality of the solvent. It is shown that the water-salt fascias of albumin are more structured than water solutions with the same concentration.

  19. Interaction of Nicotine and Bovine Serum Albumin

    Institute of Scientific and Technical Information of China (English)

    2000-01-01

    The binding of nicotine to bovine serum albumin (BSA) was studied by UV absorption, fluorescence, and 1H NMR methods. With the addition of nicotine, the absorption band of BSA at about 210 nm decreased gradually, moved to longer wavelengths, and narrowed. BSA fluorescence of tryptophan residue was quenched by nicotine. The 1H NMR peaks of nicotine moved to downfield by the addition of BSA. The experimental results showed that nicotine was capable of binding with BSA to form a 1:1 complex. BSA's high selectivity for nicotine binding suggests a unique role for this protein in the detoxification and/or transport of nicotine.

  20. Solution structure of allergenic 2 S albumins.

    Science.gov (United States)

    Pantoja-Uceda, D; Bruix, M; Santoro, J; Rico, M; Monsalve, R; Villalba, M

    2002-11-01

    The NMR solution structures at different levels of refinement of three different 2 S albumin seed proteins, the recombinant pronapin precursor from Brassica napus, the recombinant RicC3 from Ricinus communis and the methionine-rich protein from sunflower ( Helianthus annuus ), are described. The resulting common structure consists of a bundle of five alpha-helices, folded in a right-handed superhelix. The structure is very similar to that of other plant proteins: the hydrophobic protein from soybean, non-specific lipid transfer proteins and amylase/trypsin inhibitors. Analogies and differences in the structures of these families, as well as their possible relationship to allergenicity, are discussed.

  1. [Microalbuminuria and urinary albumin excretion in clinical practice].

    Science.gov (United States)

    Tagle, Rodrigo; González, Fernando; Acevedo, Mónica

    2012-06-01

    Microalbuminuria is a new tool in the management of patients with diabetes mellitus or hypertension. Microalbuminuria is an easily measured biomarker in a urine sample. Urinary albumin to creatinine ratio in first morning urine sample correlates with 24 hours urinary albumin excretion, but it is easier to obtain, and can identify hypertensive or diabetic patients with high risk for cardiovascular events. Therapeutic interventions such as renin angiotensin system blockade have demonstrated their usefulness in reducing urinary albumin excretion in clinical studies. It would be advisable to incorporate urinary albumin to creatinine ratio to the routine clinical monitoring of patients with cardiovascular risk, such as those with hypertension and diabetes mellitus.

  2. Cubilin Maintains Blood Levels of HDL and Albumin

    OpenAIRE

    Aseem, Obaidullah; Smith, Brian T; Cooley, Marion A.; Wilkerson, Brent A.; Argraves, Kelley M.; Remaley, Alan T.; Argraves, W Scott

    2013-01-01

    Cubilin is an endocytic receptor highly expressed in renal proximal tubules, where it mediates uptake of albumin and filtered forms of apoA-I/HDL. Cubilin deficiency leads to urinary loss of albumin and apoA-I; however, the consequences of cubilin loss on the homeostasis of blood albumin and apoA-I/HDL have not been studied. Using mice heterozygous for cubilin gene deletion (cubilin HT mice), we show that cubilin haploinsufficiency leads to reduced renal proximal tubular uptake of albumin and...

  3. Smartphone based point-of-care detector of urine albumin

    Science.gov (United States)

    Cmiel, Vratislav; Svoboda, Ondrej; Koscova, Pavlina; Provaznik, Ivo

    2016-03-01

    Albumin plays an important role in human body. Its changed level in urine may indicate serious kidney disorders. We present a new point-of-care solution for sensitive detection of urine albumin - the miniature optical adapter for iPhone with in-built optical filters and a sample slot. The adapter exploits smart-phone flash to generate excitation light and camera to measure the level of emitted light. Albumin Blue 580 is used as albumin reagent. The proposed light-weight adapter can be produced at low cost using a 3D printer. Thus, the miniaturized detector is easy to use out of lab.

  4. Schistosome albumin is of host, not parasite, origin.

    Science.gov (United States)

    DeMarco, Ricardo; Mathieson, William; Dillon, Gary P; Wilson, R Alan

    2007-09-01

    Recent work has implicated schistosome albumin as part of a mechanism for neutralizing the oxidative assault by host immune defenses and suggested that the gene had been acquired by horizontal transfer from the mammalian host. In the course of proteomic analyses of Schistosoma mansoni adult worm vomitus and eggs recovered from mice, we identified numerous peptides, largely derived from murine rather than parasite albumin. We therefore conjectured that the supposed S. mansoni albumin sequence deposited on GenBank might be the result of contamination rather than horizontal gene transfer. Based on phylogenetic analysis the most likely source was the Syrian (golden) hamster Mesocricetus auratus. Proteomic analysis of Syrian hamster albumin generated peptide identities to S. mansoni as the top hit, with a high ion score >1,500 and 63% coverage of the translated cDNA sequence. RT-PCR using specific primers permitted amplification of the M. auratus albumin transcript, which is identical to the deposited S. mansoni albumin sequence. PCR amplification of a fragment of the M. auratus albumin gene from genomic DNA suggests a homologous structure to the Mus musculus albumin gene. We were unable to find the S. mansoni albumin gene sequence by in silico searching on either version 3 of the S. mansoni genome assembly or the >3 million shotgun DNA reads. Finally, Southern blotting detected the albumin gene in M. auratus but not in S. mansoni genomic DNA, even when the latter was present in a 10-fold excess. Collectively, our data make the strongest case that the schistosome albumin protein described in previous reports is of host origin and all nucleotide-derived data are the result of contamination with host material. By analogy, we suggest that other reported examples of horizontal gene transfer to schistosomes might similarly be explained by complementary/genomic DNA contamination.

  5. 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...

  6. Effects of glycation on meloxicam binding to human serum albumin

    Science.gov (United States)

    Trynda-Lemiesz, Lilianna; Wiglusz, Katarzyna

    2011-05-01

    The current study reports a binding of meloxicam a pharmacologically important new generation, non-steroidal anti-inflammatory drug to glycated form of the human serum albumin (HSA). The interaction of the meloxicam with nonglycated and glycated albumin has been studied at pH 7.4 in 0.05 M sodium phosphate buffer with 0.1 M NaCl, using fluorescence quenching technique and circular dichroism spectroscopy. Results of the present study have shown that the meloxicam could bind both forms of albumin glycated and nonglycated at a site, which was close to the tryptophan residues. Similarly, how for native albumin glycated form has had one high affinity site for the drug with association constants of the order of 10 5 M -1. The glycation process of the HSA significantly has affected the impact of the meloxicam on the binding of other ligands such as warfarin and bilirubin. The affinity of the glycated albumin for bilirubin as for native albumin has been reduced by meloxicam but observed effect was weaker by half (about 20%) compared with nonglycated albumin. In contrast to the native albumin meloxicam binding to glycated form of the protein only slightly affected the binding of warfarin. It seemed possible that the effects on warfarin binding might be entirely attributable to the Lys 199 modification which was in site I.

  7. Albumin storage in neoplastic astroglial elements of gangliogliomas

    Science.gov (United States)

    Schmitz, Ann Kristin; Grote, Alexander; Raabe, Anna; Urbach, Horst; Friedman, Alon; von Lehe, Marec; Becker, Albert J.; Niehusmann, Pitt

    2013-01-01

    Purpose Low-grade neuroepithelial tumors are frequent neuropathological findings in patients with pharmacoresistant epilepsies. Little is known regarding epileptogenic mechanisms in this group of neoplasms with gangliogliomas (GG) as the most common entity. Presence of hemosiderin deposits in GG points to impairment of the blood-brain barrier (BBB). Therefore, we hypothesized a potential role of BBB dysfunction and astrocytic albumin uptake as potential epileptogenic factor in GG. Methods Prussian blue staining and fluorescent double-immunohistochemistry with antibodies against albumin, GFAP, CD34 and GLUT-1 were used to analyze hemosiderin deposits and astroglial albumin accumulation in tumor and adjacent pre-existing brain tissue of GG (n = 10) and several control groups, i.e. dysembryoplastic neuroepithelial tumors (DNT; n = 5), focal cortical dysplasia with balloon cells (FCD IIb; n = 10), astrocytomas WHO grade II (n = 5) and clear renal cell carcinoma brain metastases (RCCM, n = 6). Results Our results revealed strong hemosiderin deposits in GG. Intriguingly, we noted substantial albumin uptake exclusively in neoplastic glial cell components of GG and DNT, whereas no significant albumin was present in perilesional reactive astrocytes. Strikingly, we did not observe substantial albumin uptake in further controls. Conclusion Glial albumin uptake was restricted to long-term epilepsy associated, vasculature-containing tumors. Intratumoural BBB dysfunction in concert with subsequent accumulation of albumin by neoplastic glial cell elements represent a new putatively epileptogenic mechanism for long-term epilepsy-associated tumors. PMID:23182422

  8. Interaction of coffee compounds with serum albumins. Part II: Diterpenes.

    Science.gov (United States)

    Guercia, Elena; Forzato, Cristina; Navarini, Luciano; Berti, Federico

    2016-05-15

    Cafestol and 16-O-methylcafestol are diterpenes present in coffee, but whilst cafestol is found in both Coffea canephora and Coffea arabica, 16-O-methylcafestol (16-OMC) was reported to be specific of only C. canephora. The interactions of such compounds, with serum albumins, have been studied. Three albumins have been considered, namely human serum albumin (HSA), fatty acid free HSA (ffHSA) and bovine serum albumin (BSA). The proteins interact with the diterpenes at the interface between Sudlow site I and the fatty acid binding site 6 in a very peculiar way, leading to a significant change in the secondary structure. The diterpenes do not displace reference binding drugs of site 2, but rather they enhance the affinity of the site for the drugs. They, therefore, may alter the pharmacokinetic profile of albumin - bound drugs.

  9. Cubilin maintains blood levels of HDL and albumin.

    Science.gov (United States)

    Aseem, Obaidullah; Smith, Brian T; Cooley, Marion A; Wilkerson, Brent A; Argraves, Kelley M; Remaley, Alan T; Argraves, W Scott

    2014-05-01

    Cubilin is an endocytic receptor highly expressed in renal proximal tubules, where it mediates uptake of albumin and filtered forms of apoA-I/HDL. Cubilin deficiency leads to urinary loss of albumin and apoA-I; however, the consequences of cubilin loss on the homeostasis of blood albumin and apoA-I/HDL have not been studied. Using mice heterozygous for cubilin gene deletion (cubilin HT mice), we show that cubilin haploinsufficiency leads to reduced renal proximal tubular uptake of albumin and apoA-I and significantly increased urinary loss of albumin and apoA-I. Moreover, cubilin HT mice displayed significantly decreased blood levels of albumin, apoA-I, and HDL. The levels of albumin and apoA-I protein or mRNA expressed in the liver, kidney, or intestine of cubilin HT mice did not change significantly. The clearance rate of small HDL3 particles (density>1.13 g/ml) from the blood increased significantly in cubilin HT mice. In contrast, the rate of clearance of larger HDL2 particles from the blood did not change significantly, indicating a decreased half-life for HDL particles capable of filtering through the glomerulus. On the basis of these findings, we conclude that cubilin deficiency reduces renal salvage and delivery back to the blood of albumin and apoA-I, which decreases blood levels of albumin and apoA-I/HDL. These findings raise the possibility that therapeutic increase of renal cubilin expression might reduce proteinuria and increase blood levels of albumin and HDL.

  10. 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.

  11. Bilirubin-albumin binding, bilirubin/albumin ratios, and free bilirubin levels: where do we stand?

    Science.gov (United States)

    Hulzebos, Christian V; Dijk, Peter H

    2014-11-01

    Treatment for unconjugated hyperbilirubinemia is predominantly based on one parameter, i.e., total serum bilirubin (TSB) levels. Yet, overt kernicterus has been reported in preterm infants at relatively low TSB levels, and it has been repeatedly shown that free unconjugated bilirubin (freeUCB) levels, or bilirubin/albumin (B/A) ratios for that matter, are more closely associated with bilirubin neurotoxicity. In this article, we review bilirubin-albumin binding, UCBfree levels, and B/A ratios in addition to TSB levels to individualize and optimize treatment especially in preterm infants. Methods to measure bilirubin-albumin binding or UCBfree are neither routinely performed in Western clinical laboratories nor incorporated in current management guidelines on unconjugated hyperbilirubinemia. For bilirubin-albumin binding, this seems justified because several of these methods have been challenged, and sufficiently powered prospective trials on the clinical benefits are lacking. Technological advances in the measurement of UCBfree may provide a convenient means for integrating UCBfree measurements into routine clinical management of jaundiced infants. A point-of-care method, as well as determination of UCBfree levels in various newborn populations, is desirable to learn more about variations in time and how various clinical pathophysiological conditions affect UCBfree levels. This will improve the estimation of approximate UCBfree levels associated with neurotoxicity. To delineate the role of UCBfree in the management of jaundiced (preterm) infants, trials are needed using UCBfree as treatment parameter. The additional use of the B/A ratio in jaundiced preterms has been evaluated in the Bilirubin Albumin Ratio Trial (BARTrial; Clinical Trials: ISRCTN74465643) but failed to demonstrate better neurodevelopmental outcome in preterm infants bilirubin toxicity. Yet, different methodologies for estimating these parameters exist, and sufficiently powered, prospective clinical

  12. Nephroprotective Potential of Human Albumin Infusion: A Narrative Review

    Directory of Open Access Journals (Sweden)

    Christian J. Wiedermann

    2015-01-01

    Full Text Available Albumin infusion improves renal function in cirrhosis; however, mechanisms are incompletely understood. In clinical practice, human albumin is used in various intensive care unit indications to deal with a wide range of problems, from volume replacement in hypovolemic shock, or sepsis, to treatment of ascites in patients with liver cirrhosis. Against the background of the results of recent studies on the use of human albumin in septic patients, the importance of the natural colloid in these critically ill patients is being redefined. In addition to the hemodynamic effects of administration of human albumin impacting on sympathetic tone, attention is being paid to other effects in which its pharmacodynamics is associated with the physiological importance of endogenous albumin. The morbidity and mortality data discussed in this paper support the importance of both the hemodynamic and the pharmacological effects of the administration of human albumin in various indications. The contribution that human albumin could make towards the maintenance of renal function in the course and treatment of severe sepsis and cirrhosis of the liver is the subject of this narrative review.

  13. Atomic structure and chemistry of human serum albumin

    Science.gov (United States)

    He, Xiao M.; Carter, Daniel C.

    1992-01-01

    The three-dimensional structure of human serum albumin has been determined crystallographically to a resolution of 2.8 A. It comprises three homologous domains that assemble to form a heart-shaped molecule. Each domain is a product of two subdomains that possess common structural motifs. The principal regions of ligand binding to human serum albumin are located in hydrophobic cavities in subdomains IIA and ILIA, which exhibit similar chemistry. The structure explains numerous physical phenomena and should provide insight into future pharmacokinetic and genetically engineered therapeutic applications of serum albumin.

  14. Urinary albumin excretion. An independent predictor of ischemic heart disease

    DEFF Research Database (Denmark)

    Borch-Johnsen, K; Feldt-Rasmussen, B; Strandgaard, S

    1999-01-01

    ischemic heart disease (IHD) in a population-based cohort. In 1983, urinary albumin and creatinine levels were measured, along with the conventional atherosclerotic risk factors, in 2085 consecutive participants without IHD, renal disease, urinary tract infection, or diabetes mellitus. The participants......Cross-sectional studies suggest that an increased urinary albumin excretion rate is associated with cardiovascular disease, dyslipidemia, and hypertension. The purpose of this study was to analyze prospectively whether the urinary albumin-to -creatinine (A/C) ratio can independently predict......, 1.3 to 3.9, P=0.002), and the 10-year disease-free survival decreased from 97% to 91% (P

  15. 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 i...... no significant correlation of the reserve binding to the albumin level. This methodology may be useful in studying the variable response of infants with patent ductus arteriosus to indomethacin. Udgivelsesdato: 1983-null...

  16. Interaction between Xanthoxylin and Bovine Serum Albumin

    Institute of Scientific and Technical Information of China (English)

    WEN Maogui; TIAN Jianniao; HUANG Yonglin; BIAN Hedong; CHEN Zhengfeng; LIANG Hong

    2009-01-01

    The interaction between xanthoxylin (XT) and bovine serum albumin (BSA) under simulative physiological conditions has been analyzed in detail by various spectroscopic techniques including fluorescence, circular dichro- ism (CD), and Fourier transform infrared (FT-IR) spectroscopy. Fluorescence quenching data revealed that the quenching constants (K) were 3.31×105, 2.03×105 and 0.94×105 L·mol-1 at 286, 298 and 310 K, respectively. Based on the fluorescence results, the fluorescence quenching mechanism of the interaction between XT and BSA has been found to be combined static and dynamic quenching. Thermodynamic parameters △H0, △S0 and △G0 sug- gested that the hydrophobic force played a main role in binding of XT to BSA. The effect of XT on the conforma- tion of BSA was analyzed by FT-IR spectroscopy and quantitatively calculated from CD spectroscopy with reduc- tion of α-helical content by about 3.9%. In addition, the effect of common ions on the binding constant was also dis- cussed.

  17. KADAR ALBUMIN SERUM DAN FAAL GINJAL ANAK

    Directory of Open Access Journals (Sweden)

    Lydia Kosnadi

    2012-09-01

    Full Text Available Serum albumin concentration (Sa is one of the determinants of single nephron glomerular filtration rate. Hypoalbuminemia is frequently encountered in our country due to protein calory malnutrition, liver function disorders and others. The renal function or glomerular filtration rate (GFR measurement in children suffering from renal diseases would be able to provide information regarding the extent of the renal damage. The aim of this study was to know the interaction between Sa and GFR in children. GFR was measured by standard inulin clearance (Cin and conventional endogenous creatinine clearance (Ccr in 112 children hospitalized with renal diseases. Standard renal function status test, namely IKA-1984 was utilized for the renal function measurement. Result of this study showed a positive correlation between : Sa, Cin and Ccr in pediatric patients with decreased renal function : Cin = 5,23 + 12,14 Sa (r = 0,50; p = 0,007; n = 26 and Cr = 7,10 + 14,47 Sa (r = 0,53; p = 0,005; n = 26, so that the lower Sa level, usually will indicate the lower renal function and the more severe the renal failure.

  18. Review: Glycation of human serum albumin.

    Science.gov (United States)

    Anguizola, Jeanethe; Matsuda, Ryan; Barnaby, Omar S; Hoy, K S; Wa, Chunling; DeBolt, Erin; Koke, Michelle; Hage, David S

    2013-10-21

    Glycation involves the non-enzymatic addition of reducing sugars and/or their reactive degradation products to amine groups on proteins. This process is promoted by the presence of elevated blood glucose concentrations in diabetes and occurs with various proteins that include human serum albumin (HSA). This review examines work that has been conducted in the study and analysis of glycated HSA. The general structure and properties of HSA are discussed, along with the reactions that can lead to modification of this protein during glycation. The use of glycated HSA as a short-to-intermediate term marker for glycemic control in diabetes is examined, and approaches that have been utilized for measuring glycated HSA are summarized. Structural studies of glycated HSA are reviewed, as acquired for both in vivo and in vitro glycated HSA, along with data that have been obtained on the rate and thermodynamics of HSA glycation. In addition, this review considers various studies that have investigated the effects of glycation on the binding of HSA with drugs, fatty acids and other solutes and the potential clinical significance of these effects.

  19. Sodium intake affects urinary albumin excretion especially in overweight subjects

    NARCIS (Netherlands)

    Verhave, J C; Hillege, H L; Burgerhof, J G M; Janssen, W M T; Gansevoort, R T; Navis, G J; de Zeeuw, D; de Jong, P E; Postma, Maarten

    2004-01-01

    Objectives. To examine the relationship between sodium intake and urinary albumin excretion, being an established risk marker for later cardiovascular morbidity and mortality. Design. Cross-sectional cohort study using linear regression analysis. Setting: University hospital outpatient clinic. Subje

  20. Development of FET-type albumin sensor for diagnosing nephritis.

    Science.gov (United States)

    Park, Keun-Yong; Sohn, Young-Soo; Kim, Chang-Kyu; Kim, Hong-Seok; Bae, Young-Seuk; Choi, Sie-Young

    2008-07-15

    An albumin biosensor based on a potentiometric measurement using Biofield-effect-transistor (BioFET) has been designed and fabricated, and its characteristics were investigated. The BioFET was fabricated using semiconductor integrated circuit (IC) technology. The gate surface of the BioFET was chemically modified by newly developed self-assembled monolayer (SAM) synthesized by a thiazole benzo crown ether ethylamine (TBCEA)-thioctic acid to immobilize anti-albumin. SAM formation, antibody immobilization, and antigen-antibody interaction were verified using surface plasmon resonance (SPR). The output voltage changes of the BioFET with respect to various albumin concentrations were obtained. Quasi-reference electrode (QRE) and reference FET (ReFET) has been integrated with the BioFET, and its output characteristic was investigated. The results demonstrate the feasibility of the BioFET as the albumin sensor for diagnosing nephritis.

  1. Palmitate binding to serum albumin, measured by rate of dialysis

    DEFF Research Database (Denmark)

    Brodersen, R; Honoré, B; Andersen, S

    1988-01-01

    with binding of the unsaturated acids is less pronounced. Chloride ions compete with binding of palmitate. Reserve albumin concentration in serum samples from 33 male adults was 420 +/- 59 microM (mean +/- SD), and in 33 females, 351 +/- 50 microM. Umbilical cord sera from ten newborn infants averaged 172......Dialysis experiments were performed with an acetylcellulose membrane between two identical sample solutions; a trace amount of radiolabelled palmitate was added on one side and the rate of dialytic equilibration of the label was measured. By comparison with rates measured in standard experiments......, using pure albumin solutions, we obtained the reserve albumin concentration for binding of palmitate, previously defined as the concentration of a pure standard albumin which binds the labelled ligand as tightly as it is bound in the sample. Two techniques were developed, one for 1-ml sample volumes...

  2. 99M-technetium labeled macroaggregated human serum albumin pharmaceutical

    Science.gov (United States)

    Winchell, Harry S.; Barak, Morton; Van Fleet, III, Parmer

    1977-05-17

    A reagent comprising macroaggregated human serum albumin having dispersed therein particles of stannous tin and a method for instantly making a labeled pharmaceutical therefrom, are disclosed. The labeled pharmaceutical is utilized in organ imaging.

  3. Transport of nitrated albumin across continuous vascular endothelium

    OpenAIRE

    Predescu, Dan; Predescu, Sanda; Malik, Asrar B.

    2002-01-01

    Because modification of plasma albumin on tyrosine residues generates nitrated albumin (NOA) that may function as a mechanism of nitrogen monoxide clearance from microcirculation, we investigated biochemicaly and morphologically the cell surface binding and the transendothelial transport of NOA. An electron microscopic study was carried out with mouse lungs and hearts perfused in situ with NOA and NOA-Au complexes. The results indicate that NOA-Au can bind to the endothelial cell surface, and...

  4. Adsorption of albumin on prosthetic materials: implication for tribological behavior.

    Science.gov (United States)

    Serro, A P; Gispert, M P; Martins, M C L; Brogueira, P; Colaço, R; Saramago, B

    2006-09-01

    The orthopedic prosthesis used to substitute damaged natural joints are lubricated by a pseudosynovial fluid that contains biological macromolecules with potential boundary lubrication properties. Proteins are some of those macromolecules whose role in the lubrication process is not yet completely understood. In a previous work, we investigated the influence of the presence of albumin, the major synovial protein, upon the tribological behavior of three of the most used pairs of artificial joint materials: ultra high molecular weight polyethylene (UHMWPE) against counterfaces of alumina, CoCrMo alloy, and 316L stainless steel. Albumin was found to cause a significant decrease in the friction coefficient when the counterfaces were metallic because transfer of UHMWPE was avoided, but this effect was much weaker in the case of alumina. The objective of the present work was to look for an explanation for these differences in tribological behavior in terms of albumin adsorption. With this goal, studies on adsorption of bovine serum albumin (BSA) on the counterface materials, from a biological model fluid (Hanks' balanced salt solution), were carried out using radiolabeled albumin ((125)I-BSA), X-ray photoelectron spectroscopy, and atomic force microscopy. The conclusion from all techniques is that the driving force for albumin adsorption is higher on the metals than on alumina. These results confirm that the greater the amount of protein adsorbed on the counterface, the more efficient is the protection against the transfer of polymeric film to the counterface.

  5. Mineralisation of two phosphate ceramics in HBSS: role of albumin.

    Science.gov (United States)

    Marques, P A A P; Serro, A P; Saramago, B J; Fernandes, A C; Magalhães, M C F; Correia, R N

    2003-02-01

    The role of albumin in the mineralisation process of commercial hydroxyapatite (HAp) and synthesised biphasic (HAp-tricalcium phosphate) ceramics in a bufferless simulated inorganic plasma (HBSS) was investigated by conventional in vitro tests and static and dynamic wettability measurements. Albumin was either pre-adsorbed or solubilised in HBSS. It was found that calcium complexation by albumin plays a key role in early mineralisation kinetics, so that mineralisation is favoured when albumin is pre-adsorbed and hindered when it is dissolved in HBSS. In the biphasic ceramic this picture is complicated by the fact that albumin, in solution, seems to promote the dissolution of tricalcium phosphate, and simultaneously compete for calcium with the ceramic. It also appears that albumin has a stabilising effect of octacalcium phosphate present in deposits on commercial HAp. The same effect may be present in the case of the biphasic ceramic, at earlier mineralisation times, when octacalcium phosphate appears as a precursor of HAp. Octacalcium phosphate formation on commercial apatite is accompanied by carbonate substitution in phosphate positions.

  6. The Relationship between Albumin-Binding Capacity of Recombinant Polypeptide and Changes in the Structure of Albumin-Binding Domain.

    Science.gov (United States)

    Bormotova, E A; Gupalova, T V

    2015-07-01

    Many bacteria express surface proteins interacting with human serum albumin (HSA). One of these proteins, PAB from anaerobic bacteria, contains an albumin-binding domain consisting of 45 amino acid residues known as GA domain. GA domains are also found in G proteins isolated from human streptococcal strains (groups C and G) and of albumin-binding protein isolated from group G streptococcal strains of animal origin. The GA domain is a left-handed three-helix bundle structure in which amino acid residues of the second and third helixes are involved in albumin binding. We studied the relationship between HSA-binding activity of the recombinant polypeptide isolated from group G streptococcus of animal origin and structure of the GA domain is studied. Structural changes in GA domain significantly attenuated HAS-binding capacity of the recombinant polypeptide. Hence, affinity HSA-binding polypeptide depends on stability of GA domain structure.

  7. 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.

  8. 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

    filtration of albumin in microcirculatory beds with permeable capillaries (splanchnic organs), in between the haemodialysis treatment, and filtration of protein-poor fluid in areas with 'tight' capillaries (skeletal muscle, cutis) resulting in interstitial space protein depletion here. As the patients were...... considered to be in steady state during the measurements, the increased TERalb indicates increased lymph flux of albumin. The interstitial space protein 'wash-down' and increased lymph drainage probably serve as oedema prevention....

  9. 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.

  10. Binding of furosemide to albumin isolated from human fetal and adult serum.

    Science.gov (United States)

    Viani, A; Cappiello, M; Silvestri, D; Pacifici, G M

    1991-01-01

    Albumin was isolated from pooled fetal serum from 58 placentas obtained at normal delivery at term and from pooled adult plasma from 8 individuals. Albumin isolation was carried out by means of PEG precipitation followed by ion-exchange chromatography on DEAE-Sephadex A 50 and then on SP-Sephadex C 50. The electrophoresis on SDS-polyacrylamide gels showed only one spot that comigrated with commercial human albumin. Binding to albumin was measured by equilibrium dialysis of an aliquot of albumin solution (0.7 ml) against the same volume of 0.13 M sodium orthophosphate buffer (pH 7.4). At a total concentration of 2 micrograms/ml (therapeutic range), the unbound fraction of furosemide was 2.71% (fetal albumin) and 2.51% (adult albumin). Two classes of binding sites for furosemide were observed in fetal and adult albumin. The number of binding sites (moles of furosemide per mole of albumin) was 1.22 (fetal albumin) and 1.58 (adult albumin) for the high-affinity site and 2.97 (fetal albumin) and 3.25 (adult albumin) for the low-affinity site. The association constants (M-1) were 3.1 X 10(4) (fetal albumin) and 2.6 X 10(4) (adult albumin) for the high-affinity set of sites and 0.83 X 10(4) (fetal albumin) and 1.0 X 10(4) (adult albumin) low-affinity site. The displacement of furosemide from albumin was studied with therapeutic concentrations of several drugs. Valproic acid, salicylic acid, azapropazone and tolbutamide had the highest displacing effects which were significantly higher with fetal than with adult albumin.

  11. Using egg albumin foam to extinguish fires

    Directory of Open Access Journals (Sweden)

    Hytham A. Alsaati

    2003-12-01

    Full Text Available Oil, coal and chemical fires are often difficult to put out using water. In certain hydrocarbon fires, protein foam can extinguish fires better than water by keeping air (oxygen away from the flames and by ''blowing'' the flame away from its fuel source. Egg albumin is a relatively inexpensive protein and is representative of foaming proteins, which are candidates for use as fire suppression agents. This paper begins to deal with the effect of the foam bulk pH, foam protein concentration and generating air flow rate into the foam on the fire extinguishing time in laboratory experiments. A Bunsen burner was used to generate a small, controlled laboratory fire within a plastic container, which represented a point source in a partially open room in the experiments. The Bunsen burner represents a gaseous hydrocarbon fire, which can be difficult to extinguish. Both a low pH foam and one made with a high air flow rate favor a reduction in time required to put out the Bunsen burner flame.Chamas produzidas por óleo, carvão e produtos químicos (incêndios provocados são difíceis de ser extinguidos com água. Algumas chamas de hidrocarbonetos podem ser extinguidas por espumas protéicas melhor do que a manutenção de ar (oxigênio fora do alcance das chamas ou pelo sopramento da chama para longe da sua fonte. Albumina de ovo é uma proteína relativamente barata e é representativa dentre as proteínas usadas como espuma para a (supressão extinção de agentes causadores de incêndio. Este artigo trata do estudo do efeito do pH e concentração da espuma protéica, além da geração de ar no interior da espuma, sobre o tempo de extinção de incêndio em experimentos laboratoriais. Nos experimentos um bico de Bunsen foi usado para gerar uma pequena chama, controlada em um container de plástico, representando uma fonte pontual em um ambiente parcialmente aberto. A chama do bico de Bunsen representa uma chama gasosa de hidrocarbonetos, que são dif

  12. EVALUATION OF SERUM ALBUMIN LEVELS IN ACUTE MYOCARDIAL INFARCTION

    Directory of Open Access Journals (Sweden)

    Shilpa

    2015-10-01

    Full Text Available BACKGROUND : Acute myocardial infarction (AMI is one of the major causes of mortality and morbidity in the world. Serum albumin levels are inversely related with age, smoking, blood pressure and obesity. It is not clear whether low serum albumin level is a nonspecific , prognostic variable, a marker of subclinical disease, or whether it is a part of causal mechanism leading to death due to cardiovascular disease. Some studies have reported an inverse association between serum albumin and cardiovascular mortality but oth ers have not . 1 The association between serum albumin and cardiovascular mortality remains controversial. This study was done to evaluate the serum albumin levels in patients with ST segment elevation Myocardial infarction (STEMI over a period of three days from the date of admission and whether the changes had any relationship with the prognosis of the patient. AIM: to associate changes in serum albumin levels in AMI patients over a period of three days i.e., day zero - at the time of admission, day+1 - the following day(12 to 30hrs after collecting first sample, day +2(32 to 54 hrs after collecting first sample with the clinical prognosis of the patient. SETTINGS AND DESIGN : Prospective follow up study in patents admitted with AMI in a tertiary care hospital. METHODS: 30 pati ents admitted with STEMI were included in the study and serum albumin levels were estimated in them on admission and for two days thereafter. Statistical analysis used. The data was analysed using SPSS 15.0, STATA 8.0, MEDLAC 9.0.1, And SYSTAT 11 softwares. Repeated measures analysis of variance and student t test was used to find the significance in changes of serum albumin levels and prognosis of the patient on different days. RESULTS AND CONCLUSION: This study found that there was fall in serum albumin le vels in patients with AMI in the course of three days compared with the day of admission and it was significantly associated with bad prognosis.

  13. Quantification of osmotic water transport in vivo using fluorescent albumin.

    Science.gov (United States)

    Morelle, Johann; Sow, Amadou; Vertommen, Didier; Jamar, François; Rippe, Bengt; Devuyst, Olivier

    2014-10-15

    Osmotic water transport across the peritoneal membrane is applied during peritoneal dialysis to remove the excess water accumulated in patients with end-stage renal disease. The discovery of aquaporin water channels and the generation of transgenic animals have stressed the need for novel and accurate methods to unravel molecular mechanisms of water permeability in vivo. Here, we describe the use of fluorescently labeled albumin as a reliable indicator of osmotic water transport across the peritoneal membrane in a well-established mouse model of peritoneal dialysis. After detailed evaluation of intraperitoneal tracer mass kinetics, the technique was validated against direct volumetry, considered as the gold standard. The pH-insensitive dye Alexa Fluor 555-albumin was applied to quantify osmotic water transport across the mouse peritoneal membrane resulting from modulating dialysate osmolality and genetic silencing of the water channel aquaporin-1 (AQP1). Quantification of osmotic water transport using Alexa Fluor 555-albumin closely correlated with direct volumetry and with estimations based on radioiodinated ((125)I) serum albumin (RISA). The low intraperitoneal pressure probably accounts for the negligible disappearance of the tracer from the peritoneal cavity in this model. Taken together, these data demonstrate the appropriateness of pH-insensitive Alexa Fluor 555-albumin as a practical and reliable intraperitoneal volume tracer to quantify osmotic water transport in vivo.

  14. Biocompatibility of electrospun human albumin: a pilot study.

    Science.gov (United States)

    Noszczyk, B H; Kowalczyk, T; Łyżniak, M; Zembrzycki, K; Mikułowski, G; Wysocki, J; Kawiak, J; Pojda, Z

    2015-03-02

    Albumin is rarely used for electrospinning because it does not form fibres in its native globular form. This paper presents a novel method for electrospinning human albumin from a solution containing pharmaceutical grade protein and 25% polyethylene oxide (PEO) used as the fibre-forming agent. After spontaneous cross-linking at body temperature, with no further chemicals added, the fibres become insoluble and the excess PEO can be washed out. Albumin deposited along the fibres retains its native characteristics, such as its non-adhesiveness to cells and its susceptibility for degradation by macrophages. To demonstrate this we evaluated the mechanical properties, biocompatibility and biodegradability of this novel product. After subcutaneous implantation in mice, albumin mats were completely resorbable within six days and elicited only a limited local inflammatory response. In vitro, the mats suppressed cell attachment and migration. As this product is inexpensive, produced from human pharmaceutical grade albumin without chemical modifications, retains its native protein properties and fulfils the specific requirements for anti-adhesive dressings, its clinical use can be expedited. We believe that it could specifically be used when treating paediatric patients with epidermolysis bullosa, in whom non-healing wounds occur after minor hand injuries which lead to rapid adhesions and devastating contractures.

  15. Anionic Calixarene-Capped Silver Nanoparticles Show Species-Dependent Binding to Serum Albumins

    Directory of Open Access Journals (Sweden)

    Anthony W. Coleman

    2013-05-01

    Full Text Available The anionic calixarenes para-sulphonatocalix[4]arene and 1,3-di-Ophosphonatocalix[ 4]arene, have been used to cap silver nanoparticles. The binding of these functional particles with regard to various serum albumins (bovine serum albumin, human serum albumin, porcine serum albumin and sheep serum albumin has been studied by variable temperature fluorescence spectroscopy. The quenching of the fluorescence of the proteins was shown to vary as a function of the anionic calixarene capping molecule and also as a function of the origin of the serum albumin. It is thus possible to discriminate between the different species.

  16. Anionic calixarene-capped silver nanoparticles show species-dependent binding to serum albumins.

    Science.gov (United States)

    Tauran, Yannick; Brioude, Arnaud; Kim, Beomjoon; Perret, Florent; Coleman, Anthony W

    2013-05-21

    The anionic calixarenes para-sulphonatocalix[4]arene and 1,3-di-O-phosphonatocalix[ 4]arene, have been used to cap silver nanoparticles. The binding of these functional particles with regard to various serum albumins (bovine serum albumin, human serum albumin, porcine serum albumin and sheep serum albumin) has been studied by variable temperature fluorescence spectroscopy. The quenching of the fluorescence of the proteins was shown to vary as a function of the anionic calixarene capping molecule and also as a function of the origin of the serum albumin. It is thus possible to discriminate between the different species.

  17. Renal catabolism of albumin – current views and controversies

    Directory of Open Access Journals (Sweden)

    Jakub Gburek

    2011-10-01

    Full Text Available Albumin is the main protein of blood plasma, lymph, cerebrospinal fluid and interstitial fluid. The protein assists in many important body functions, including maintenance of proper colloidal osmotic pressure, transport of important metabolites and antioxidant action. Synthesis of albumin takes place mainly in the liver, and its catabolism occurs mostly in vascular endothelium of muscle, skin and liver as well as in the kidney tubular epithelium. Renal catabolism of albumin consists of glomerular filtration and tubular reabsorption. The tubular processes include endocytosis via the multiligand scavenger receptor tandem megalin and cubilin-amnionless complex. Possible ways of further catabolism of this protein are lysosomal proteolysis to amino acids and short peptides, recycling of degradation products into the bloodstream and tubular lumen or transcytosis of whole molecules. The article discusses the molecular aspects of these processes and presents the controversies arising in the light of the last decade of research.

  18. On-Chip Immunoassay for Determination of Urinary Albumin

    Directory of Open Access Journals (Sweden)

    Adisorn Tuantranont

    2009-12-01

    Full Text Available An immunoassay performed on a portable microfluidic device was evaluated for the determination of urinary albumin. An increase in absorbance at 500 nm resulting from immunoagglutination was monitored directly on the poly(dimethylsiloxane (PDMS microchip using a portable miniature fibre-optic spectrometer. A calibration curve was linear up to 10 mg L–1 (r2 = 0.993, with a detection limit of 0.81 mg L–1 (S/N = 3. The proposed system showed good precision, with relative standard deviations (RSDs of 5.1%, when evaluated with 10 mg L–1 albumin (n = 10. Determination of urinary albumin with the proposed system gave results highly similar to those determined by the conventional spectrophotometric method using immunoturbidimetric detection (r2 = 0.995; n = 15.

  19. Adherence of platelets to in situ albumin-binding surfaces under flow conditions: role of surface-adsorbed albumin.

    Science.gov (United States)

    Guha Thakurta, Sanjukta; Miller, Robert; Subramanian, Anuradha

    2012-08-01

    Surfaces that preferentially bind human serum albumin (HSA) were generated by grafting albumin-binding linear peptide (LP1) onto silicon surfaces. The research aim was to evaluate the adsorption pattern of proteins and the adhesion of platelets from platelet-poor plasma and platelet-rich plasma, respectively, by albumin-binding surfaces under physiological shear rate (96 and 319 s(-1)) conditions. Bound proteins were quantified using enzyme-linked immunosorbent assays (ELISAs) and two-dimensional gel electrophoresis. A ratio of ∼1000:100:1 of adsorbed HSA, human immunoglobulin (HIgG) and human fibrinogen (HFib) was noted, respectively, on LP1-functionalized surfaces, and a ratio of ∼5:2:1 of the same was noted on control surfaces, as confirmed by ELISAs. The surface-adsorbed von Willebrand factor was undetectable by sensitive ELISAs. The amount of adhered platelets correlated with the ratio of adsorbed HSA/HFib. Platelet morphology was more rounded on LP1-functionalized surfaces when compared to control surfaces. The platelet adhesion response on albumin-binding surfaces can be explained by the reduction in the co-adsorption of other plasma proteins in a surface environment where there is an excess of albumin molecules, coupled with restrictions in the conformational transitions of other surface-adsorbed proteins into hemostatically active forms.

  20. Radiation-modified albumin in type 2 diabetic patients

    Directory of Open Access Journals (Sweden)

    Galina Gorbenko

    2013-02-01

    Full Text Available Objectives: Diabetes mellitus has been one of the most crippling diseases that man has seen, and its prevalence has risen dramatically over the past two decades. Currently, there are over 150 million diabetics worldwide and this number is likely to increase to 300 million or more by the year 2025. Diabetes mellitus increases the risk of many disorders including cardiovascular diseases. Understanding the molecular properties of diabetic progression is a big challenge in the system biology era. The aim of this study is to determine association in albumin modifications between Chernobyl clean-up workers with and without type 2 diabetes mellitus. Methods: ABM (3-aminobenzanthrone derivative developed in Daugavpils University, Latvia has been previously shown as a potential biomarker for determination of the immune state of patients with different pathologies. In this study several aspects of plasma albumin alterations in the group of Chernobyl clean-up workers with diabetes mellitus in relation to the group of workers without diabetes mellitus and people having no professional contact with radioactivity were determined. The following parameters were examined: (1 spectral characteristics of ABM in blood plasma; (2 effective and total albumin concentration in blood plasma; and (3 quantitative parameters of albumin auto-fluorescence. Results: Screening of individuals with diabetes mellitus 25-26 years after their work in Chernobyl revealed two groups of patients differing in structural and functional properties of membrane. The revealed structural modifications of membrane are dependent on radiation-induced factors. Concomitant diseases (diabetes mellitus, cardiovascular diseases reinforce radiation-induced effects. Conclusion: ABM is a sensitive probe of albumin alterations; it can be used to elucidate the changes in protein systems. Significant differences in albumin dynamics exist between the control group (donors and that of diabetics and non

  1. Preparation and characterization of 125 I labeled bovine serum albumin

    Directory of Open Access Journals (Sweden)

    K S Ashwitha Rai

    2015-01-01

    Full Text Available Bovine serum albumin is a model protein, which has been conventionally used as protein standard and in many areas of biochemistry, pharmacology and medicine. Radioiodination procedure for bovine serum albumin employing chloramine-T as an oxidant with slight modification was evaluated critically to establish the optimal conditions for the preparation of radiolabeled tracer ( 125 I-BSA with required specific activity without impairing the immune reactivity and biological activity. Optimized radioiodination procedure involving 10 µg of chloramine-T along with 20 µg of sodium metabisulphite with 60 seconds incubation at 2° yielded 125 I-BSA with high integrity.

  2. Recent Topics in Chemical and Clinical Research on Glycated Albumin

    OpenAIRE

    Ueda, Yuki; Matsumoto, Hideyuki

    2015-01-01

    The measuring method for glycated albumin (GA) has been developed as a new glycemic control marker since the beginning of the 21st century. Since GA has an advantage in reflecting glycemic status over a shorter period than hemoglobin A1c (HbA1c), much research and many reviews have been reported. However, so far there have been few reports on glycation sites based on the tertiary structure of human serum albumin (HSA) and the comparison of glycation rates between GA and HbA1c in detail. The p...

  3. Stabilization of Tyrosinase-Bovine Serum Albumin Crystals by Glutaraldehyde

    Directory of Open Access Journals (Sweden)

    D. Norouzian

    2007-01-01

    Full Text Available Tyrosinase and bovine serum albumin were co-crystallized by saturated ammonium sulfate solution(65% and 20% polyethylene glycol ( PEG 6000 and n-propanol as co-solvents .The obtained crystals were cross linked by glutaraldehyde solution(1% v/v.Polyethylene glycol 6000 was found to be better co-solvent than n-propanol. The developed biocatalyst could be recycled 6 times without further loss of tyrosinase activity. No loss of activity of cross linked tyrosinase -bovine serum albumin crystals was observed upon storage of the developed CLECs at refrigerator for six months.

  4. Measurements of neonatal bilirubin and albumin concentrations: a need for improvement and quality control

    NARCIS (Netherlands)

    Imhoff, D.E. van; Dijk, P.H.; Weykamp, C.W.; Cobbaert, C.M.; Hulzebos, C.V.; Liem, K.D.

    2011-01-01

    Accurate and precise bilirubin and albumin measurements are essential for proper management of jaundiced neonates. Data hereon are lacking for Dutch laboratories. We aimed to determine variability of measurements of bilirubin and albumin concentrations typical for (preterm) neonates. Aqueous, human

  5. Measurements of neonatal bilirubin and albumin concentrations : a need for improvement and quality control

    NARCIS (Netherlands)

    van Imhoff, Deirdre E.; Dijk, Peter H.; Weykamp, Cas W.; Cobbaert, Christa M.; Hulzebos, Christian V.

    2011-01-01

    Accurate and precise bilirubin and albumin measurements are essential for proper management of jaundiced neonates. Data hereon are lacking for Dutch laboratories. We aimed to determine variability of measurements of bilirubin and albumin concentrations typical for (preterm) neonates. Aqueous, human

  6. Water-phase palmitate concentrations in equilibrium with albumin-bound palmitate in a biological system

    DEFF Research Database (Denmark)

    Bojesen, Inge Norby; Bojesen, Eigil

    1992-01-01

    Biokemi, erythrocyte ghosts, pamitate, bovine serum albumin, long-chain fatty acids, equilibrium constants......Biokemi, erythrocyte ghosts, pamitate, bovine serum albumin, long-chain fatty acids, equilibrium constants...

  7. Conjugation of Chitooligosaccharide-5-fluorouracil with Bovine Serum Albumin

    Institute of Scientific and Technical Information of China (English)

    Rong Min WANG; Jing Feng SONG; Yu Feng HE; Juan Juan MAO; Yan LI

    2006-01-01

    The interaction between chitooligosaccharide-5-fluorouracil (COS-5FU) and bovine serum albumin (BSA) was studied by fluorescence spectroscopy. It was found that an energy transfer between COS-5FU and BSA had been occurred. The binding constants were calculated,between the donor and acceptor, the distance between BSA and COS-5FU was determined.

  8. 2S Albumin Storage Proteins: What Makes them Food Allergens?

    Science.gov (United States)

    Moreno, F. Javier; Clemente, Alfonso

    2008-01-01

    2S albumin storage proteins are becoming of increasing interest in nutritional and clinical studies as they have been reported as major food allergens in seeds of many mono- and di-cotyledonous plants. This review describes the main biochemical, structural and functional properties of these proteins thought to play a role in determining their potential allergenicity. 2S albumins are considered to sensitize directly via the gastrointestinal tract (GIT). The high stability of their intrinsic protein structure, dominated by a well-conserved skeleton of cysteine residues, to the harsh conditions present in the GIT suggests that these proteins are able to cross the gut mucosal barrier to sensitize the mucosal immune system and/or elicit an allergic response. The flexible and solvent-exposed hypervariable region of these proteins is immunodominant and has the ability to bind IgE from allergic patients´ sera. Several linear IgE-binding epitopes of 2S albumins spanning this region have been described to play a major role in allergenicity; the role of conformational epitopes of these proteins in food allergy is far from being understood and need to be investigated. Finally, the interaction of these proteins with other components of the food matrix might influence the absorption rates of immunologically reactive 2S albumins but also in their immune response. PMID:18949071

  9. Binding of straight-chain saturated dicarboxylic acids to albumin.

    Science.gov (United States)

    Tonsgard, J H; Mendelson, S A; Meredith, S C

    1988-11-01

    Dicarboxylic acids are prominent features of several diseases, including Reye's syndrome. Long-chain dicarboxylic acids have profound effects on the function and structure of isolated mitochondria, suggesting that they could contribute to the mitochondrial dysfunction in Reye's syndrome. Binding of fatty acids to albumin and the intracellular fatty acid-binding proteins is important in regulating the transport and metabolism of fatty acids and protects against the toxic effects of unbound fatty acids. We studied the binding of dicarboxylic acids to defatted albumin using equilibrium dialysis to assess to what extent dicarboxylic acids are likely to be bound in the plasma of patients. Dicarboxylic acids bind weakly to albumin in a molar ratio of 3.8, 4.2, 1.6, 0.8, and 0.7 to 1 for octadecanedioic, hexadecanedioic, tetradecanedioic, dodecanedioic, and decanedioic acid, respectively. The dissociation constants for long-chain dicarboxylic acids are 100-1,000-fold larger than those of comparable monocarboxylic acids. Oleate competes with dicarboxylic acid and reduces the moles of dicarboxylic acid bound per mol of albumin to less than 1. Octanoate inhibits dicarboxylic acid binding. Our observations indicate that in Reye's syndrome, substantial concentrations of dicarboxylic acids of patients may be free and potentially toxic to mitochondria and other cellular processes.

  10. Isolation of bovine serum albumin from whey using affinity chromatography

    NARCIS (Netherlands)

    Besselink, T.; Janssen, A.E.M.; Boom, R.M.

    2015-01-01

    The adsorption of bovine serum albumin (BSA) to a chromatography resin with immobilised llama antibody fragments as affinity ligands was investigated. The maximum adsorption capacity of the affinity resin was 21.6 mg mL-1 with a Langmuir equilibrium constant of 20.4 mg mg-1. Using packed bed chromat

  11. Spontaneous formation of small sized albumin/acacia coacervate particles.

    Science.gov (United States)

    Burgess, D J; Singh, O N

    1993-07-01

    Microgel coacervate particles form spontaneously on mixing aqueous solutions of oppositely charged albumin and acacia, under specific conditions of pH, ionic strength, and polyion concentration, close to but not at the optimum conditions for maximum coacervate yield. The mean particle diameter of these coacervate particles is approximately 6 microns when suspended in aqueous media, as determined by HIAC/Royco particle analysis. The geometric standard deviation of the particles falls in the range 1.2-1.9 microns. The particle size was not dependent on the method of emulsification of the coacervate in the equilibrium phase, or on the stirring speed applied during the manufacturing process. The microgel particles were stable on storage, for periods up to forty-six days, without the addition of a chemical cross-linking agent, or the application of heat. Stability was measured with respect to the change in particle size of samples stored at different temperatures. The non-cross-linked microcapsules were also shown to be stable on pH change, to pH values outside the coacervation pH range. At the optimum conditions for maximum coacervate yield the albumin/acacia system formed a very viscous coacervate phase, which was unsuitable for microcapsule preparation. The rheological properties of albumin/acacia and gelatin/acacia complex coacervates optimized for maximum coacervate yield were compared. The albumin/acacia coacervate was shown to be three orders of magnitude more viscous than the gelatin/acacia system.

  12. Interaction of Tannin with Bovine Serum Albumin by Fluorescence Spectrometry

    CERN Document Server

    Dong-Il, Kim; Kye-Ryong, Sin

    2016-01-01

    Interaction between tannin and bovine serum albumin (BSA) was examined by the fluorescent quenching. The process of elimination between BSA and tannin was the one of a stationary state, and the coupling coefficient was one. The working strength between the tannin and the beef serum was hydrophobic one.

  13. Albumin-heparin microspheres as carriers for cytostatic agents

    NARCIS (Netherlands)

    Cremers, H.F.M.; Feijen, J.; Kwon, G.; Bae, Y.H.; Kim, S.W.; Noteborn, H.P.J.M.; McVie, J.G.

    1990-01-01

    Much work has been done on adriamycin-loaded albumin microspheres (Alb-MS) for chemoembolization [1–4], the rationale being that site-specific drug delivery may increase the therapeutic efficacy of the drug. Alb-Ms are being investigated because of their biocompatibility and because the degradation

  14. 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 Food and Drugs FOOD AND DRUG ADMINISTRATION, DEPARTMENT OF HEALTH AND HUMAN SERVICES (CONTINUED) MEDICAL DEVICES CLINICAL CHEMISTRY AND CLINICAL TOXICOLOGY DEVICES Clinical Chemistry Test Systems §...

  15. A single food bolus stimulates albumin synthesis in growing piglets

    NARCIS (Netherlands)

    de Meer, K; Smolders, HC; Meesterburrie, J; de Sain-van der Velden, M; Voorbij, HAM; Okken, A; Reijngoud, DJ; Kulik, W

    2000-01-01

    Background: A stable isotope tracer method to quantify the synthesis of proteins of hepatic origin in response to feeding is described. The response of albumin synthesis on one mixed meal in a piglet model was investigated and the intragastric and intravenous administration modes of C-13-valine were

  16. Pharmacokinetics and anti-HIV-1 efficacy of negatively charged human serum albumins in mice

    NARCIS (Netherlands)

    Kuipers, M E; Swart, P J; Schutten, M; Smit, C; Proost, J H; Osterhaus, A D; Meijer, D K

    1997-01-01

    Negatively charged albumins (NCAs, with the prototypes succinylated human serum albumin (Suc-HSA) and aconitylated human serum albumin (Aco-HSA)), modified proteins with a potent anti-human immunodeficiency virus type 1 (anti-HIV-1) activity in vitro, were studied for their pharmacokinetic behaviour

  17. Studies on Interactions of Antibiotics with Serum Albumin by Surface Plasmon Resonance Biosensor

    Institute of Scientific and Technical Information of China (English)

    2006-01-01

    Characterizing how chemical compounds binding to serum albumin is essential in evaluating drug candidates and is the focus of this study. A surface plasmon resonance biosensor developed in this laboratory was used to determine the binding constants of antibiotics with serum albumin. The binding constants of five antibiotics(azithromycin, spectinomycin, gentamycin, metacycline and kanamycin) with serum albumins were obtained.

  18. Albumin testing in urine using a smart-phone.

    Science.gov (United States)

    Coskun, Ahmet F; Nagi, Richie; Sadeghi, Kayvon; Phillips, Stephen; Ozcan, Aydogan

    2013-11-07

    We demonstrate a digital sensing platform, termed Albumin Tester, running on a smart-phone that images and automatically analyses fluorescent assays confined within disposable test tubes for sensitive and specific detection of albumin in urine. This light-weight and compact Albumin Tester attachment, weighing approximately 148 grams, is mechanically installed on the existing camera unit of a smart-phone, where test and control tubes are inserted from the side and are excited by a battery powered laser diode. This excitation beam, after probing the sample of interest located within the test tube, interacts with the control tube, and the resulting fluorescent emission is collected perpendicular to the direction of the excitation, where the cellphone camera captures the images of the fluorescent tubes through the use of an external plastic lens that is inserted between the sample and the camera lens. The acquired fluorescent images of the sample and control tubes are digitally processed within one second through an Android application running on the same cellphone for quantification of albumin concentration in the urine specimen of interest. Using a simple sample preparation approach which takes ~5 min per test (including the incubation time), we experimentally confirmed the detection limit of our sensing platform as 5-10 μg mL(-1) (which is more than 3 times lower than the clinically accepted normal range) in buffer as well as urine samples. This automated albumin testing tool running on a smart-phone could be useful for early diagnosis of kidney disease or for monitoring of chronic patients, especially those suffering from diabetes, hypertension, and/or cardiovascular diseases.

  19. Optimalisasi Pengikatan Tanin Daun Nangka dengan Protein Bovine Serum Albumin (Optimalisation Binding of Jackfruit Leaves Tannin with Bovine Serum Albumin Protein)

    OpenAIRE

    Wahidin Teguh Sasongko; Lies Mira Yusiati; Zaenal Bachruddin; (Mugiono), Mugiono

    2012-01-01

    Tannins are high molecular weight polyphenol compounds with ability to bind proteins. Based on the structure, albumin are simple globular molecule protein. Optimalisation binding of jackfruit leave tannins to bovine serum (BSA) albumin was done in two stages. The first stage was to determine levels of tannins and condensed tannins in jackfruit leaves grown in mediterranean soil types. Second research was optimalisation binding of jackfruit leaf tannins with bovine serum albumin. In t...

  20. Renal type a intercalated cells contain albumin in organelles with aldosterone-regulated abundance.

    Directory of Open Access Journals (Sweden)

    Thomas Buus Jensen

    Full Text Available Albumin has been identified in preparations of renal distal tubules and collecting ducts by mass spectrometry. This study aimed to establish whether albumin was a contaminant in those studies or actually present in the tubular cells, and if so, identify the albumin containing cells and commence exploration of the origin of the intracellular albumin. In addition to the expected proximal tubular albumin immunoreactivity, albumin was localized to mouse renal type-A intercalated cells and cells in the interstitium by three anti-albumin antibodies. Albumin did not colocalize with markers for early endosomes (EEA1, late endosomes/lysosomes (cathepsin D or recycling endosomes (Rab11. Immuno-gold electron microscopy confirmed the presence of albumin-containing large spherical membrane associated bodies in the basal parts of intercalated cells. Message for albumin was detected in mouse renal cortex as well as in a wide variety of other tissues by RT-PCR, but was absent from isolated connecting tubules and cortical collecting ducts. Wild type I MDCK cells showed robust uptake of fluorescein-albumin from the basolateral side but not from the apical side when grown on permeable support. Only a subset of cells with low peanut agglutinin binding took up albumin. Albumin-aldosterone conjugates were also internalized from the basolateral side by MDCK cells. Aldosterone administration for 24 and 48 hours decreased albumin abundance in connecting tubules and cortical collecting ducts from mouse kidneys. We suggest that albumin is produced within the renal interstitium and taken up from the basolateral side by type-A intercalated cells by clathrin and dynamin independent pathways and speculate that the protein might act as a carrier of less water-soluble substances across the renal interstitium from the capillaries to the tubular cells.

  1. Binding of diazepam, salicylic acid and digitoxin to albumin isolated from fetal and adult serum.

    Science.gov (United States)

    Viani, A; Cappiello, M; Pacifici, G M

    1991-01-01

    Albumin was isolated from pooled fetal serum obtained at normal delivery at term and from pooled adult plasma. Albumin isolation was carried out by means of PEG precipitation followed by ion exchange chromatography on DEAE-Sephadex A 50 and then on SP-Sephadex C 50. The binding of diazepam (1 microM), salicylic acid (2 mM) and digitoxin (6 nM) to albumin (40 g/l) was measured by equilibrium dialysis at 37 degrees C. The unbound fraction (mean +/- SD) for fetal and adult albumin of diazepam was 1.86 +/- 0.24 and 1.82 +/- 0.15% (NS), that of digitoxin was 3.18 +/- 0.27 and 3.36 +/- 0.04% (NS) and that of salicylic acid was 11.65 +/- 0.99 and 9.47 +/- 0.75% (p less than 0.05), respectively. With both fetal and adult albumin, a single class of binding sites was observed for diazepam and digitoxin, whereas two classes of binding sites were observed for salicylic acid. The number of binding sites (n, moles of drug per mole of albumin) for fetal and adult albumin was 0.83 and 1.02 for diazepam and 0.014 and 0.018 for digitoxin, respectively. For salicylic acid, n was 1.45 (fetal albumin) and 1.55 (adult albumin) for the higher affinity site, and 3.06 (fetal albumin) and 3.27 (adult albumin) for the lower affinity site. The association constant (Ka, M-1) for diazepam was 1.36 x 10(5) (fetal albumin) and 1.00 x 10(5) (adult albumin) and that for digitoxin was 4.12 x 10(6) (fetal albumin) and 2.7 x 10(6) (adult albumin). For salicylic acid, Ka was 38.4 x 10(3) (fetal albumin) and 35.8 x 10(3) (adult albumin) for the higher affinity site, and 2.7 x 10(3) (fetal albumin) and 4.3 x 10(3) (adult albumin) for the lower affinity site. This work shows that fetal and adult albumin have similar binding properties and corroborates our previous findings with furosemide.

  2. [Excess mortality in critically ill patients after treatment with human albumin].

    Science.gov (United States)

    Offringa, M; Gemke, R J; Henny, C P

    1998-08-15

    According to the results of a systematic review of randomized clinical studies administration of human albumin to critically ill patients is associated with excess mortality, compared with withholding albumin or administration of crystalloid fluids. The study appears to be well done. Also, there are various explanatory pathophysiological mechanisms supporting the association. However, a favourable effect of albumin in certain patient groups cannot be excluded. Alternatives to albumin are available in most clinical situations, but unfortunately, they are not completely without drawbacks. The use of albumin has to be limited; it might only be abolished when a better effect of other fluids, such as synthetic solutions, is demonstrated.

  3. Vanillin restrains non-enzymatic glycation and aggregation of albumin by chemical chaperone like function.

    Science.gov (United States)

    Awasthi, Saurabh; Saraswathi, N T

    2016-06-01

    Vanillin a major component of vanilla bean extract is commonly used a natural flavoring agent. Glycation is known to induce aggregation and fibrillation of globular proteins such as albumin, hemoglobin. Here we report the inhibitory potential of vanillin toward early and advanced glycation modification and amyloid like aggregation of albumin based on the determination of both early and advanced glycation and conformational changes in albumin using circular dichroism. Inhibition of aggregation and fibrillation of albumin was determined based on amyloid specific dyes i.e., Congo red and Thioflavin T and microscopic imaging. It was evident that vanillin restrains glycation of albumin and exhibits protective effect toward its native conformation.

  4. Buoyancy-activated cell sorting using targeted biotinylated albumin microbubbles.

    Directory of Open Access Journals (Sweden)

    Yu-Ren Liou

    Full Text Available Cell analysis often requires the isolation of certain cell types. Various isolation methods have been applied to cell sorting, including fluorescence-activated cell sorting and magnetic-activated cell sorting. However, these conventional approaches involve exerting mechanical forces on the cells, thus risking cell damage. In this study we applied a novel isolation method called buoyancy-activated cell sorting, which involves using biotinylated albumin microbubbles (biotin-MBs conjugated with antibodies (i.e., targeted biotin-MBs. Albumin MBs are widely used as contrast agents in ultrasound imaging due to their good biocompatibility and stability. For conjugating antibodies, biotin is conjugated onto the albumin MB shell via covalent bonds and the biotinylated antibodies are conjugated using an avidin-biotin system. The albumin microbubbles had a mean diameter of 2 μm with a polydispersity index of 0.16. For cell separation, the MDA-MB-231 cells are incubated with the targeted biotin-MBs conjugated with anti-CD44 for 10 min, centrifuged at 10 g for 1 min, and then allowed 1 hour at 4 °C for separation. The results indicate that targeted biotin-MBs conjugated with anti-CD44 antibodies can be used to separate MDA-MB-231 breast cancer cells; more than 90% of the cells were collected in the MB layer when the ratio of the MBs to cells was higher than 70:1. Furthermore, we found that the separating efficiency was higher for targeted biotin-MBs than for targeted avidin-incorporated albumin MBs (avidin-MBs, which is the most common way to make targeted albumin MBs. We also demonstrated that the recovery rate of targeted biotin-MBs was up to 88% and the sorting purity was higher than 84% for a a heterogenous cell population containing MDA-MB-231 cells (CD44(+ and MDA-MB-453 cells (CD44-, which are classified as basal-like breast cancer cells and luminal breast cancer cells, respectively. Knowing that the CD44(+ is a commonly used cancer

  5. Insulin Is Required to Maintain Albumin Expression by Inhibiting Forkhead Box O1 Protein.

    Science.gov (United States)

    Chen, Qing; Lu, Mingjian; Monks, Bobby R; Birnbaum, Morris J

    2016-01-29

    Diabetes is accompanied by dysregulation of glucose, lipid, and protein metabolism. In recent years, much effort has been spent on understanding how insulin regulates glucose and lipid metabolism, whereas the effect of insulin on protein metabolism has received less attention. In diabetes, hepatic production of serum albumin decreases, and it has been long established that insulin positively controls albumin gene expression. In this study, we used a genetic approach in mice to identify the mechanism by which insulin regulates albumin gene transcription. Albumin expression was decreased significantly in livers with insulin signaling disrupted by ablation of the insulin receptor or Akt. Concomitant deletion of Forkhead Box O1 (Foxo1) in these livers rescued the decreased albumin secretion. Furthermore, activation of Foxo1 in the liver is sufficient to suppress albumin expression. These results suggest that Foxo1 acts as a repressor of albumin expression.

  6. Albumin Suppresses Human Hepatocellular Carcinoma Proliferation and the Cell Cycle

    Directory of Open Access Journals (Sweden)

    Shunsuke Nojiri

    2014-03-01

    Full Text Available Many investigations have revealed that a low recurrence rate of hepatocellular carcinoma (HCC is associated with high serum albumin levels in patients; therefore, high levels of serum albumin are a major indicator of a favorable prognosis. However, the mechanism inhibiting the proliferation of HCC has not yet been elucidated, so we investigated the effect of serum albumin on HCC cell proliferation. Hep3B was cultured in MEM with no serum or containing 5 g/dL human albumin. As control samples, Prionex was added to generate the same osmotic pressure as albumin. After 24-h incubation, the expressions of α-fetoprotein (AFP, p53, p21, and p57 were evaluated with real-time PCR using total RNA extracted from the liver. Protein expressions and the phosphorylation of Rb (retinoblastoma were determined by Western blot analysis using total protein extracted from the liver. For flow cytometric analysis of the cell cycle, FACS analysis was performed. The percentages of cell cycle distribution were evaluated by PI staining, and all samples were analyzed employing FACScalibur (BD with appropriate software (ModFit LT; BD. The cell proliferation assay was performed by counting cells with using a Scepter handy automated cell counter (Millipore. The mRNA levels of AFP relative to Alb(−: Alb(−, Alb(+, and Prionex, were 1, 0.7 ± 0.2 (p < 0.001 for Alb(−, and 1 ± 0.3, respectively. The mRNA levels of p21 were 1, 1.58 ± 0.4 (p = 0.007 for Alb(− and p = 0.004 for Prionex, and 0.8 ± 0.2, respectively. The mRNA levels of p57 were 1, 4.4 ± 1.4 (p = 0.002 for Alb(− and Prionex, and 1.0 ± 0.1, respectively. The protein expression levels of Rb were similar in all culture media. The phosphorylation of P807/811 and P780 of Rb protein was reduced in Alb(+. More cells in the G0/G1 phase and fewer cells in S and G2/M phases were obtained in Alb(+ than in Alb(− (G0/G1: 60.9%, 67.7%, 61.5%; G2/M: 16.5%, 13.1%, 15.6%; S: 22.6%, 19.2%, 23.0%, Alb(−, Alb

  7. Albumin-mediated delivery of siRNA

    DEFF Research Database (Denmark)

    Bienk, Konrad

    2015-01-01

    . The human body, however, possesses several natural transport mechanisms for active transport of molecules. Amongst these is albumin, which is the most abundant plasma protein and has a circulatory half-life of ~21 days, partially due to engagement and recycling by the neonatal Fc receptor (FcRn). Albumin......The recent development of protein, peptide and nucleotide therapeutics is an important step towards the successful treatment of many severe diseases caused by altered gene expression. Small interfering RNA (siRNA) can be used for regulation of cellular gene expression to revert pathologic states...... vehicle. This proof of concept silencing showed that siRNA can be used for therapeutic purposes without the use of non-biocompatible polymer or lipid materials. This work, therefore, provides a novel technology platform for the safe delivery of siRNA therapeutics....

  8. Raman microspectroscopy of nanodiamond-induced structural changes in albumin.

    Science.gov (United States)

    Svetlakova, Anastasiya S; Brandt, Nikolay N; Priezzhev, Alexander V; Chikishev, Andrey Yu

    2015-04-01

    Nanodiamonds (NDs) are promising agents for theranostic applications due to reported low toxicity and high biocompatibility, which is still being extensively tested on cellular, tissue, and organism levels. It is presumed that for experimental and future clinical applications, NDs will be administered into the organism via the blood circulation system. In this regard, the interaction of NDs with blood components needs to be thoroughly studied. We studied the interaction of carboxylated NDs (cNDs) with albumin, one of the major proteins of blood plasma. After 2-h long in vitro incubation in an aqueous solution of the protein, 100-nm cNDs were dried and the dry samples were studied with the aid of Raman microspectroscopy. The spectroscopic data indicate significant conformational changes that can be due to cND–protein interaction. A possible decrease in the functional activity of albumin related to the conformational changes must be taken into account in the in vivo applications.

  9. Raman microspectroscopy of nanodiamond-induced structural changes in albumin

    Science.gov (United States)

    Svetlakova, Anastasiya S.; Brandt, Nikolay N.; Priezzhev, Alexander V.; Chikishev, Andrey Yu.

    2015-04-01

    Nanodiamonds (NDs) are promising agents for theranostic applications due to reported low toxicity and high biocompatibility, which is still being extensively tested on cellular, tissue, and organism levels. It is presumed that for experimental and future clinical applications, NDs will be administered into the organism via the blood circulation system. In this regard, the interaction of NDs with blood components needs to be thoroughly studied. We studied the interaction of carboxylated NDs (cNDs) with albumin, one of the major proteins of blood plasma. After 2-h long in vitro incubation in an aqueous solution of the protein, 100-nm cNDs were dried and the dry samples were studied with the aid of Raman microspectroscopy. The spectroscopic data indicate significant conformational changes that can be due to cND-protein interaction. A possible decrease in the functional activity of albumin related to the conformational changes must be taken into account in the in vivo applications.

  10. 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...... approach to half-life extension is conjugation of molecules to HSA. In this part of the thesis, novel GLP-1-albumin conjugates developed by Albumedix A/S where examined by a combined approach of pharmacokinetic studies and solution structure determination with SAXS. GLP-1 was conjugated to Cys34...... of recombinant HSA (rHSA) and two rHSA variants with lower (NB) and higher binding (HB) affinity to the neonatal Fc receptor (FcRn). Binding kinetics showed that the conjugation had limited effect on the binding properties of the conjugates to FcRn compared to the respective rHSA variants. Increased in-vivo half...

  11. Recent advancements in erythrocytes, platelets, and albumin as delivery systems.

    Science.gov (United States)

    Xu, Peipei; Wang, Ruju; Wang, Xiaohui; Ouyang, Jian

    2016-01-01

    In the past few years, nanomaterial-based drug delivery systems have been applied to enhance the efficacy of therapeutics and to alleviate negative effects through the controlled delivery of targeting and releasing agents. However, few drug carriers can achieve high targeting efficacy, even when targeting modalities and surface markers are introduced. Immunological problems have also limited their wide applications. Biological drug delivery systems, such as erythrocytes, platelets, and albumin, have been extensively investigated because of their unique properties. In this review, erythrocytes, platelets, and albumin are described as efficient drug delivery systems. Their properties, applications, advantages, and limitations in disease treatment are explained. This review confirms that these systems can be used to facilitate a specific, biocompatible, and smart drug delivery.

  12. [Reaction mechanism of cefotaxime with human serum albumin].

    Science.gov (United States)

    Liu, Luo-sheng; Wang, Xing-po; Zhao, Quan-qin; Zhang, Yu-yi

    2006-06-01

    The reaction mechanism of cefotaxime with human serum albumin (HSA) and the affinity between cefotaxime and beta-lactamase were investigated by spectrometry and spectrofluorimetry. The interaction dissociation constants of human serum albumin and cefotaxime were determined from a double reciprocal Lineweaver-Burk plot. The binding distance and transfer efficiency between cefotaxime and HSA were also obtained according to the theory of Förster non-radiation energy transfer. The result suggested that the main binding force between cefotaxime and HSA is electrostatic force interaction. The high beta-lactamase stability of cefotaxime may be correlative with its molecular structure. The antibiotic activity and valence are connected with transfer efficiency and dissociation constant. The effect of cefotaxime on the conformation of HSA was also analyzed using synchronous fluorescence spectrometry.

  13. Low urinary albumin excretion in astronauts during space missions

    DEFF Research Database (Denmark)

    Cirillo, Massimo; De Santo, Natale G; Heer, Martina

    2003-01-01

    BACKGROUND: Physiological changes occur in man during space missions also at the renal level. Proteinuria was hypothesized for space missions but research data are missing. METHODS: Urinary albumin, as an index of proteinuria, and other variables were analyzed in 4 astronauts during space missions...... onboard the MIR station and on the ground (control). Mission duration before first urine collection in the four astronauts was 4, 26, 26, and 106 days, respectively. On the ground, data were collected 2 months before mission in two astronauts, 6 months after in the other astronauts. A total of twenty......-two 24-hour urine collections were obtained in space (n per astronaut = 1-14) and on the ground (n per astronaut = 2-12). Urinary albumin was measured by radioimmunoassay. For each astronaut, mean of data in space and on the ground was defined as individual average. RESULTS: The individual averages of 24...

  14. Binding of straight-chain saturated dicarboxylic acids to albumin.

    OpenAIRE

    Tonsgard, J H; Mendelson, S A; Meredith, S C

    1988-01-01

    Dicarboxylic acids are prominent features of several diseases, including Reye's syndrome. Long-chain dicarboxylic acids have profound effects on the function and structure of isolated mitochondria, suggesting that they could contribute to the mitochondrial dysfunction in Reye's syndrome. Binding of fatty acids to albumin and the intracellular fatty acid-binding proteins is important in regulating the transport and metabolism of fatty acids and protects against the toxic effects of unbound fat...

  15. Occupational asthma caused by inhalation of bovine serum albumin powder

    OpenAIRE

    Choi, Gil-Soon; Kim, Joo-Hee; Lee, Haet-Nim; Sung, Jun-Mo; Lee, Jin-Woo; Park, Hae-Sim

    2009-01-01

    Bovine serum albumin (BSA), which is present in bovine plasma, is one of the major allergens affecting patients with food allergies induced by milk and meat. It is also commonly used in research laboratories. Although some reports have documented food allergies associated with BSA, BSA-induced occupational asthma has not been reported. We report a case of occupational asthma and rhinitis in a laboratory worker caused by the inhalation of BSA powder, in which an IgE-mediated response was sugge...

  16. Binding of several benzodiazepines to bovine serum albumin: Fluorescence study

    Science.gov (United States)

    Machicote, Roberta G.; Pacheco, María E.; Bruzzone, Liliana

    2010-10-01

    The interactions of lorazepam, oxazepam and bromazepam with bovine serum albumin (BSA) were studied by fluorescence spectrometry. The Stern-Volmer quenching constants and corresponding thermodynamic parameters Δ H, Δ G and Δ S were calculated. The binding constants and the number of binding sites were also investigated. The distances between the donor (BSA) and the acceptors (benzodiazepines) were obtained according to fluorescence resonance energy transfer and conformational changes of BSA were observed from synchronous fluorescence spectra.

  17. Albumin-bound fatty acids induce mitochondrial oxidant stress and impair antioxidant responses in proximal tubular cells

    NARCIS (Netherlands)

    Ishola, D. A.; Post, J. A.; van Timmeren, M. M.; Bakker, S. J. L.; Goldschmeding, R.; Koomans, H. A.; Braam, B.; Joles, J. A.

    2006-01-01

    Albumin induces oxidative stress and cytokine production in proximal tubular cells (PTECs). Albumin-bound fatty acids (FAs) enhance tubulopathic effects of albumin in vivo. We proposed that FA aggravation of albumin-induced oxidative stress in PTECs might be involved. We hypothesized that mitochondr

  18. [Sero-ascitic gradient of albumin: usefulness and diagnostic limitations].

    Science.gov (United States)

    Alba, D; Torres, E; Vázquez, J J

    1995-08-01

    The serum-ascites albumin (SAA) gradient has been defined as the serum albumin concentration minus the ascitic fluid albumin concentration. The SAA gradient is superior to the exudate-transudate concept to classify ascites, being a exact portal hypertension (PH) marker. An elevated SAA gradient (1.1 g/L or greater) correlates with PH, whereas a low gradient indicates no PH. The SAA gradient correlates well with PH in cirrhotic patients. It is also of particular utility to differentiate between congestive heart failure and malignant ascites without liver metastases (both of them with elevated ascites fluid proteins -AFP-). However, a low SAA gradient do not differentiate between tuberculous and malignant ascites. Consequently, there are still need for tests a cytology, culture for mycobacteria or ascites fluid polymorphonuclear cell count in some cases. The level of AFP, apart from the exudate-transudate concept, has some value for certain cases (a low level of AFP implicates a high risk of spontaneous bacterial peritonitis). The SAA gradient should replace the AFP concentration as the initial test to classify ascites.

  19. Superior serum half life of albumin tagged TNF ligands

    Energy Technology Data Exchange (ETDEWEB)

    Mueller, Nicole [Division of Molecular Internal Medicine, Department of Internal Medicine II, University Hospital Wuerzburg, Roentgenring 11, 97070 Wuerzburg (Germany); Schneider, Britta; Pfizenmaier, Klaus [Institute of Cell Biology and Immunology, University of Stuttgart, Allmandring 31, 70569 Stuttgart (Germany); Wajant, Harald, E-mail: harald.wajant@mail.uni-wuerzburg.de [Division of Molecular Internal Medicine, Department of Internal Medicine II, University Hospital Wuerzburg, Roentgenring 11, 97070 Wuerzburg (Germany)

    2010-06-11

    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.

  20. Hydrophobic interactions of phenoxazine modulators with bovine serum albumin

    Indian Academy of Sciences (India)

    H N Kalpana; B C Channu; Chhabil Dass; P J Houghton; K N Thimmaiah

    2000-02-01

    The interaction of 10-(3’-N-morpholinopropyl)phenoxazine [MPP], 10-(4’-N-morpholinobutyl)phenoxazine [MBP], 10-(3’-N-morpholinopropyl)-2-chlorophenoxazine [MPCP], 10-(3’-N-piperidinopropyl)-2-chlorophenoxazine [PPCP] or 10-(3’-N-morpholinopropyl)-2-trifluoromethylphenoxazine [MPTP] with bovine serum albumin (BSA) has been studied by gel filtration and equilibrium dialysis methods. The binding of these modulators, based on dialysis experiments, has been characterized using the following parameters: percentage of bound drug (), the association constant (1), the apparent binding constant () and the free energy change ( °). The binding of phenoxazine derivatives to serum transporter protein, BSA, is correlated with their octanol-water partition coefficient, log10 ~ . In addition, effect of the displacing activities of hydroxyzine and acetylsalicylic acid on the binding of phenoxazine derivatives to albumin has been studied. Results of the displacement experiments show that phenoxazine benzene rings and tertiary amines attached to the side chain of the phenoxazine moiety are bound to a hydrophobic area on the albumin molecule.

  1. Effect of tribology processes on adsorption of albumin

    Science.gov (United States)

    Yan, Yu; Yang, Hongjuan; Wang, Linghe; Su, Yanjing; Qiao, Lijie

    2016-03-01

    As soon as artificial joint replacements are implanted into patients, the adsorption of proteins can occur. Joint implants operate in a protein-rich and relatively corrosive environment under tribological contact. The contacted area acted as an anodic part and the rest of the surface was more cathodic. Therefore, the adsorption of proteins is different in and outside the wear track. Adsorbed proteins would denature during rubbing and a tribofilm could form. The tribofilm can lubricate the surface and act as a barrier to corrosion damage. However, to observe the adsorption of proteins in situ has always been a challenge. Scanning Kelvin probe force microscope (SKPFM) was used to study the adsorption of albumin on the surface of CoCrMo alloy under simulated tribology movement. Fluorescence microscopy (FM) was employed to reveal the protein molecules in the wear scar. It was found that albumin molecules can decrease the surface potential and accelerate the corrosion process. In the wear track, albumin denatured and changed the surface potential as time progressed.

  2. Non-enzymatic glucosylation induced neo-epitopes on human serum albumin: A concentration based study

    Science.gov (United States)

    Neelofar, Km; Arif, Zarina; Ahmad, Jamal; Alam, Khursheed

    2017-01-01

    Hyperglycaemia induced non enzymatic glycation is accelerated in diabetic patients and aggressively involved in diabetes progression. Human serum albumin (HSA) is the most abundant protein in blood circulation. In hyperglycaemia, it undergoes fast glycation and results in the impairment of structure. Our previous study has demonstrated structural alterations in Amadori-albumin modified with different glucose concentrations from physiological to pathophysiological range. Here, we focused on immunological characterization of Amadori-albumin. Immunogenicity of Amadori-albumin was analysed by direct binding and competitive ELISA. Amadori-albumin was found to be highly immunogenic (expect albumin modified with 5mM) and induced high titre antibodies depending upon the extent of modification. Very high titre antibodies were obtained with albumin modified with 75mM glucose as compared to native albumin. Anti-Amadori-albumin-IgG from rabbit sera exhibited increased recognition of Amadori-albumin than native albumin in competitive immunoassay. Alteration induced in albumin after glucosylation has made it highly immunogenic. Induced antibodies were quite specific for respective immunogens but showed cross-reaction with other Amadori/native proteins. It suggests that glucosylation has generated highly immunogenic epitopes on albumin. Formation of high molecular weight immune complex with retarded mobility further supports specificity of anti-Amadori-albumin-IgG towards Amadori-albumin. It may be concluded that due to early glycation, an array of modification occurred in HSA structure. Such gross structural changes might favour polymerization of most of the native epitopes into potent immunogenic neo-epitopes, but some original epitopes were still active and has contributed in the immunogenicity. It could be concluded that induction of anti-Amadori-albumin antibodies may be due to protection of glucose modified albumin from protiolytic breakdown. We assumed that this type of

  3. Plasma-to-ascitic fluid transport rate of albumin in patients with decompensated cirrhosis. Relation to intraperitoneal albumin

    DEFF Research Database (Denmark)

    Henriksen, Jens Henrik Sahl; Ring-Larsen, H; Lassen, N A;

    1983-01-01

    Albumin-kinetics and haemodynamic studies were performed in 20 patients with decompensated liver cirrhosis in order to improve the knowledge on genesis and perpetuation of hepatic ascites, especially with respect to determinants of intraperitoneal protein. A positive relationship was found betwee...... in the 'lymph-imbalance' theory of ascites formation, whereas a 'fluid equilibrium' theory seems to be too simple, especially with respect to explain protein sequestration in the peritoneal cavity....

  4. Albumin Utilization in a Teaching Hospital in Tehran: Time to Revise the Prescribing Strategies

    Directory of Open Access Journals (Sweden)

    Yokabed Kazemi

    2015-10-01

    Full Text Available Background: Since albumin imposes a relatively high cost to a healthcare system, drug use evaluation for this drug is much more important. This study wants to evaluate pattern of albumin use in a large university affiliated hospital in Tehran, Iran.Methods: A concurrent, cross-sectional study was performed in “Shaheed Rajaei” Cardiovascular, Medical and Research Center. All inpatient adults that were prescribed albumin during the study period were evaluated to register the indications for albumin usage according to the evidence-based guidelines.Results: Only for five patients (4% the albumin prescriptions were justifiable. Of these cases, intractable edema was the leading cause of albumin misuse (73 patients; 60.8%. The total 1468 vials of Albumin were prescribed for 120 patients during the study period. The most common reasons to prescribe albumin were acute normovolemic (34%, cardiac failure (0.83%, resistance edema with Albumin>2g/dL (61%, nephrotic syndrome (0.83%, plasmapheresis (1.67%, ascetic (1.67%.Conclusion: These data, together with previous national studies highly suggest a mandatory need for educational measures for practicing physicians along with strict regulations for prescription strategies regarding expensive drugs such as albumin.

  5. Long term alterations of blood plasma albumin in Chernobyl clean-up workers

    Directory of Open Access Journals (Sweden)

    Inta Kalnina

    2014-09-01

    Full Text Available Albumin is the most generously represented protein in human blood plasma. Therefore it is important to follow and assess the transport function of albumin in clinic researches. Disturbances in structural/functional properties of albumin play an important role in the pathogenesis of various diseases and immune state in patients. Changes in albumin transformation can serve as a diagnostic and prognostic criterion in pathologies. ABM (3-aminobenzanthrone derivative developed at the Daugavpils University, Latvia has been previously shown as a potential biomarker for determination of the immune state of patients with different pathologies. The aim of this study was to determine the several aspects of plasma albumin alterations in the group of Chernobyl clean-up workers in long term period in relation with humans having no professional contact with radioactivity. The following parameters were examined: (1 spectral characteristics of ABM in blood plasma; (2 and #8216;effective and #8217; and total albumin (EA and TA concentration in blood plasma; (3 quantitative parameters of albumin auto-fluorescence; (4 albumin binding site characteristics. Screening of the individuals with a period of 25-26 years after the work in Chernobyl revealed two groups of patients differing in structural and functional albumin properties; first on conformations of plasma albumin, and second characteristics of tryptophanyl region of the molecule. The revealed structural modifications of albumin are dependent on radiation-induced factors. Concomitant diseases such as diabetes mellitus or cardio-vascular diseases reinforce radiation-induced effects. In conclusion, ABM is a sensitive probe for albumin alterations and can be used to elucidate the changes in protein systems. Significant differences in albumin dynamics exist between control (donors and groups of Chernobyl clean-up workers. [J Exp Integr Med 2014; 4(3.000: 165-170

  6. The preparation of albumin as a biological drug from human plasma by fiber filtration

    Directory of Open Access Journals (Sweden)

    Mousavi Hosseini K

    2011-08-01

    Full Text Available "nBackground: In recent years, consumption of whole-blood for the treatment of patients has decreased but use of biological plasma-derived medicines such as albumin, immunoglobulin and coagulation factors have increased instead. Paying attention to albumin molecular structure is important for its isolation from human plasma. Albumin is a single-chain protein consisting of about 585 amino acids and a molecular weight of 66500 Daltons. Albumin is a stable molecule and it is spherical in shape. There are different methods for human albumin preparation. Considering the large consumption of this biological drug in clinical settings, methods with fewer steps in production line are of big advantage in saving time and manufacturing more products."n "nMethods: In this project, we prepared human albumin using hollow fiber cartridges in order to omit the rework on fraction V+VI. Human albumin is usually produced by the application of cold ethanol method, where albumin is obtained from fraction V by doing a rework on fraction V+VI to separate fraction V."n "nResults: In the current work, human albumin was prepared from fraction V+VI by the help of hollow fiber cartridges. With a concentration of 20%, the obtained albumin had 96.5% of monomer and 3.5% of polymer and polymer aggregate."n "nConclusion: Comparing the obtained human albumin with a number of commercial human albumin samples by the use of SDS-page, the results were satisfactory regarding the 3.5 percent polymer and aggregate rate for the prepared albumin.

  7. An inhibitor to rubella hemagglutination present in bovine albumin preparations: its removal by treatment with kaolin.

    Science.gov (United States)

    Campbell, J B; Ellins, M L; Tasios, C

    1977-07-18

    Certain commercial preparations of bovine albumin, fraction V, show inhibitory activity in the rubella hemagglutination (HA) and hemagglutination-inhibition (HI) tests. This does not appear to be due to albumin per se, but instead to a contaminant (or contaminants) with the properties of a lipoprotein. All inhibitory activity can be removed from albumin preparations by treatment with kaolin, gel filtration, or flotation ultracentrifugation. We have found that, even when there was no inhibition of HA titers, kaolin treatment of the albumins prior to their incorporation into the test diluent resulted in more clearly defined agglutination patterns. Reasons for and against including albumin in the test diluent are discussed. It is concluded that, although not essential, it is a worthwhile additive. Our data suggest, however, that each batch of albumin used for this purpose should be checked for the presence of inhibitor, and that treatment with kaolin might be considered as a routine step prior to its incorporation into the test diluent.

  8. Characterization of anticancer, DNase and antifungal activity of pumpkin 2S albumin.

    Science.gov (United States)

    Tomar, Prabhat Pratap Singh; Nikhil, Kumar; Singh, Anamika; Selvakumar, Purushotham; Roy, Partha; Sharma, Ashwani Kumar

    2014-06-13

    The plant 2S albumins exhibit a spectrum of biotechnologically exploitable functions. Among them, pumpkin 2S albumin has been shown to possess RNase and cell-free translational inhibitory activities. The present study investigated the anticancer, DNase and antifungal activities of pumpkin 2S albumin. The protein exhibited a strong anticancer activity toward breast cancer (MCF-7), ovarian teratocarcinoma (PA-1), prostate cancer (PC-3 and DU-145) and hepatocellular carcinoma (HepG2) cell lines. Acridine orange staining and DNA fragmentation studies indicated that cytotoxic effect of pumpkin 2S albumin is mediated through induction of apoptosis. Pumpkin 2S albumin showed DNase activity against both supercoiled and linear DNA and exerted antifungal activity against Fusarium oxysporum. Secondary structure analysis by CD showed that protein is highly stable up to 90°C and retains its alpha helical structure. These results demonstrated that pumpkin 2S albumin is a multifunctional protein with host of potential biotechnology applications.

  9. The evidence for small-volume resuscitation with hyperoncotic albumin in critical illness

    OpenAIRE

    Myburgh, John A

    2008-01-01

    Small-volume resuscitation of critically ill patients with hyperoncotic albumin offers a number of theoretical advantages, such as increasing intravascular volume in excess of the volume of fluid administered and reducing interstitial edema. Whilst iso-oncotic albumin has been shown to be equi-effective to isotonic saline for the resuscitation of critically ill patients without associated traumatic brain injury, the efficacy of hyperoncotic albumin for resuscitation has not been evaluated in ...

  10. Caveolae-dependent and -independent uptake of albumin in cultured rodent pulmonary endothelial cells.

    Directory of Open Access Journals (Sweden)

    Hui-Hua Li

    Full Text Available Although a critical role for caveolae-mediated albumin transcytosis in pulmonary endothelium is well established, considerably less is known about caveolae-independent pathways. In this current study, we confirmed that cultured rat pulmonary microvascular (RPMEC and pulmonary artery (RPAEC endothelium endocytosed Alexa488-labeled albumin in a saturable, temperature-sensitive mode and internalization resulted in co-localization by fluorescence microscopy with cholera B toxin and caveolin-1. Although siRNA to caveolin-1 (cav-1 in RPAEC significantly inhibited albumin uptake, a remnant portion of albumin uptake was cav-1-independent, suggesting alternative pathways for albumin uptake. Thus, we isolated and cultured mouse lung endothelial cells (MLEC from wild type and cav-1(-/- mice and noted that ~ 65% of albumin uptake, as determined by confocal imaging or live cell total internal reflectance fluorescence microscopy (TIRF, persisted in total absence of cav-1. Uptake of colloidal gold labeled albumin was evaluated by electron microscopy and demonstrated that albumin uptake in MLEC from cav-1(-/- mice was through caveolae-independent pathway(s including clathrin-coated pits that resulted in endosomal accumulation of albumin. Finally, we noted that albumin uptake in RPMEC was in part sensitive to pharmacological agents (amiloride [sodium transport inhibitor], Gö6976 [protein kinase C inhibitor], and cytochalasin D [inhibitor of actin polymerization] consistent with a macropinocytosis-like process. The amiloride sensitivity accounting for macropinocytosis also exists in albumin uptake by both wild type and cav-1(-/- MLEC. We conclude from these studies that in addition to the well described caveolar-dependent pulmonary endothelial cell endocytosis of albumin, a portion of overall uptake in pulmonary endothelial cells is cav-1 insensitive and appears to involve clathrin-mediated endocytosis and macropinocytosis-like process.

  11. Importance of albumin in cross-reactivity among cat, dog and horse allergens.

    Science.gov (United States)

    Cabañas, R; López-Serrano, M C; Carreira, J; Ventas, P; Polo, F; Caballero, M T; Contreras, J; Barranco, P; Moreno-Ancillo, A

    2000-01-01

    Different allergenic proteins have been involved in cross-reactivity among animals. Albumins seem to be cross-sensitizing allergenic components. The aim of this study was to assess the importance of albumin as a cross-reactive allergen in patients sensitized to cat, dog and horse. One hundred and seventeen patients sensitized to cat were tested for IgE reactivity using skin prick tests and RAST assays with cat, dog and horse hair/dander extracts and their purified albumin extracts. RAST-inhibition studies were carried out to assess cross-reactivity among cat, dog and horse and among their purified albumins. It was found that 22% of patients exhibited specific IgE to cat albumin; 41% of patients sensitized to cat were also sensitized to dog and horse. Out of these patients, 21% had IgE to three albumins and 17% to two. Reciprocal inhibitions were observed among cat, dog and horse albumins and also among cat, dog and horse hair/dander extracts, using in the latter experiment sera from patients not sensitized to albumins. IgE binding to horse extract was inhibited 30% by its homologous albumin and IgE binding to cat and dog extracts in almost 15% by their respective albumins. It was concluded that albumins from these three animals share some epitopes that account for the cross-reactivity observed in around one-third of patients sensitized to cat, dog and horse. Nevertheless, more than 50% of specific IgE that cross-reacts among these three animals is directed to allergens other than albumin.

  12. 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

  13. Stability, accumulation and cytotoxicity of an albumin-cisplatin adduct

    DEFF Research Database (Denmark)

    Møller, Charlotte; Tastesen, Hanne Sørup; Gammelgaard, Bente

    2010-01-01

    The accumulation and cytotoxicity of a 10 µmol L¿¹ equimolar human serum albumin-cisplatin adduct (HSA-Pt) was investigated in suspension Ehrlich Ascites Tumor Cells (EATC) and adherent Ehrlich Lettré Ascites Cells (Lettré). HSA-Pt did not induce apoptosis nor was it taken up by the cells to any...... significant amount within 24 h incubation. The accumulation and cytotoxicity of HSA-Pt was compared to 10 µmol L¿¹ cisplatin for which a larger accumulation and cytotoxicity were observed in EATC compared to Lettré. The experiment was performed with cell medium exchange every fourth hour as HSA...

  14. Elucidation of structural and functional properties of albumin bound to gold nanoparticles.

    Science.gov (United States)

    Mariam, Jessy; Sivakami, S; Dongre, P M

    2017-02-01

    Nanoparticle-albumin complexes are being designed for targeted drug delivery and imaging. However, the changes in the functional properties of albumin due to adsorption on nanoparticles remain elusive. Thus, the objective of this work was to elucidate the structural and functional properties of human and bovine serum albumin bound to negatively charged gold nanoparticles (GNPs). Fluorescence data demonstrated static quenching of albumin by GNP with the quenching of buried as well as surface tryptophan in BSA. The binding process was enthalpy and entropy-driven in HSA and BSA, respectively. At lower concentrations of GNP there was a higher affinity for tryptophan, whereas at higher concentrations both tryptophan and tyrosine participated in the interaction. Synchronous fluorescence spectra revealed that the microenvironment of tryptophan in HSA turned more hydrophilic upon exposure to GNP. The α-helical content of albumin was unaltered by GNP. Approximately 37 and 23% reduction in specific activity of HSA and BSA was observed due to GNP binding. In presence of warfarin and ibuprofen the binding constants of albumin-GNP complexes were altered. A very interesting observation not reported so far is the retained antioxidant activity of albumin in presence of GNP i.e. we believe that GNPs did not bind to the free sulfhydryl groups of albumin. However enhanced levels of copper binding were observed. We have also highlighted the differential response in albumin due to gold and silver nanoparticles which could be attributed to differences in the charge of the nanoparticle.

  15. Conformational Transitions and Glycation of Serum Albumin in Patients with Minimal-Change Glomerulopathy

    Science.gov (United States)

    Hong, Sae Yong; Lee, Eun Young; Yang, Jong Oh; Kim, Tae Yeong; Kim, Eun Hee; Cheong, Mi Young; Kim, Soo Hyun; Cheong, Chae Joon

    2004-01-01

    Background There has been a lack of study on the structural changes of serum albumin in patients with minimal change disease (MCD). To determine whether glycation and/or conformational transitions of albumin are involved in the pathogenesis of albuminuria, nine patients with MCD were enrolled in a prospective follow-up study for comparison of these parameters in serum albumin during the remission and relapse of nephrotic syndrome. Methods Circular dichroism measurements were made with purified albumin. Ellipticities at each wavelength were transformed to mean residue ellipticity. Monosaccharide composition was analyzed by high-pH anion-exchange chromatography with pulsed amperometric detection. Results There was no difference in the proportions of α-helix, β-conformation, and β-turn of albumin between the sera of control patients and those with nephrotic syndrome. However, the proportion of the random configuration was slightly higher in the plasma albumin of patients in relapse than in those in remission. The proportion of the random configuration was lower in the albumin of the serum than in the urine of patients with nephrotic syndrome, but there was no difference in the proportions of α-helix, β-conformation, and β-turn of albumin between their plasma and urine. Conclusion Our results suggest that conformational changes in albumin are involved in albuminuria in patients with MCD. PMID:15481604

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

    Energy Technology Data Exchange (ETDEWEB)

    Naveenraj, Selvaraj [Nanomaterials and Solar Energy Conversion Lab, Department of Chemistry, National Institute of Technology, Tiruchirappalli 620015 (India); Solomon, Rajadurai Vijay; Venuvanalingam, Ponnambalam [School of Chemistry, Bharathidasan University, Tiruchirappalli 620024 (India); Asiri, Abdullah M. [The Center of Excellence for Advanced Materials Research, King Abdulaziz University, Jeddah 21413, P.O. Box 80203 (Saudi Arabia); Anandan, Sambandam, E-mail: sanand@nitt.edu [Nanomaterials and Solar Energy Conversion Lab, Department of Chemistry, National Institute of Technology, Tiruchirappalli 620015 (India)

    2013-11-15

    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.

  17. Cellular Specificity of the Blood-CSF Barrier for Albumin Transfer across the Choroid Plexus Epithelium

    DEFF Research Database (Denmark)

    Liddelow, Shane A; Dzięgielewska, Katarzyna M; Møllgård, Kjeld

    2014-01-01

    in albumin transport into developing brain, however the exact mechanism remains unknown. We postulate that SPARC is a docking site for albumin, mediating its uptake and transfer by choroid plexus epithelial cells from blood into cerebrospinal fluid (CSF). We used in vivo physiological measurements...... the mouse blood-CSF barrier to the same extent as endogenous mouse albumin, confirming results from in situ PLA. During postnatal development Sparc gene expression was higher in early postnatal ages than in the adult and changed in response to altered levels of albumin in blood plasma in a differential...

  18. 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.

  19. Plasma-to-ascitic fluid transport rate of albumin in patients with decompensated cirrhosis. Relation to intraperitoneal albumin

    DEFF Research Database (Denmark)

    Henriksen, J H; Ring-Larsen, Helmer; Lassen, N A

    1983-01-01

    Albumin-kinetics and haemodynamic studies were performed in 20 patients with decompensated liver cirrhosis in order to improve the knowledge on genesis and perpetuation of hepatic ascites, especially with respect to determinants of intraperitoneal protein. A positive relationship was found between...... (plasma minus ascitic fluid) oncotic pressure (rlin = 0.74, P less than 0.001) but significantly higher than that (P less than 0.005), indicating a 'non-equilibrium' in the splanchnic Starling forces. The results point to a multivariate genesis and perpetuation of cirrhotic ascites as laid down...

  20. Systematic targeted integration to study Albumin gene control elements.

    Directory of Open Access Journals (Sweden)

    Sanchari Bhattacharyya

    Full Text Available To study transcriptional regulation by distant enhancers, we devised a system of easily modified reporter plasmids for integration into single-copy targeting cassettes in clones of HuH7, a human hepatocellular carcinoma. The plasmid constructs tested transcriptional function of a 35-kb region that contained the rat albumin gene and its upstream flanking region. Expression of integrants was analyzed in two orientations, and compared to transient expression of non-integrated plasmids. Enhancers were studied in their natural positions relative to the promoter and localized by deletion. All constructs were also analyzed by transient transfection assays. In addition to the known albumin gene enhancer (E1 at -10 kb, we demonstrated two new enhancers, E2 at -13, and E4 at +1.2 kb. All three enhancers functioned in both transient assays and integrated constructs. However, chromosomal integration demonstrated several differences from transient expression. For example, analysis of E2 showed that enhancer function within the chromosome required a larger gene region than in transient assays. Another conserved region, E3 at -0.7 kb, functioned as an enhancer in transient assays but inhibited the function of E1 and E2 when chromosomally integrated. The enhancers did not show additive or synergistic behavior,an effect consistent with competition for the promoter or inhibitory interactions among enhancers. Growth arrest by serum starvation strongly stimulated the function of some integrated enhancers, consistent with the expected disruption of enhancer-promoter looping during the cell cycle.

  1. Release of proteins via ion exchange from albumin-heparin microspheres

    NARCIS (Netherlands)

    Kwon, Glen S.; Bae, You Han; Cremers, Harry; Feijen, Jan; Kim, Sung Wan

    1992-01-01

    Albumin-heparin and albumin microspheres were prepared as ion exchange gels for the controlled release of positively charged polypeptides and proteins. The adsorption isotherms of chicken egg and human lysozyme, as model proteins, on microspheres were obtained. An adsorption isotherm of chicken egg

  2. Effect of low-dose heparin on urinary albumin excretion in insulin-dependent diabetes mellitus

    DEFF Research Database (Denmark)

    Myrup, B; Hansen, P M; Jensen, T;

    1995-01-01

    We investigated the effect of heparin on urinary albumin excretion in patients with insulin-dependent diabetes mellitus. 39 patients with persistent urinary albumin excretion of 30-300 mg/24 h were randomly treated for 3 months with subcutaneous injections twice daily of isotonic saline, 5000 IU ...

  3. Inhibition of surface induced coagulation by preadsorption of albumin-heparin conjugates

    NARCIS (Netherlands)

    Hennink, W.E.; Kim, S.W.; Feijen, J.

    1984-01-01

    Surface coatings of the albumin-heparin conjugates were developed to improve the blood compatibility of polymeric materials. Glass, PVC, Biomer and cellulose acetate were coated with albumin-heparin conjugate and its adsorption and desorption behavior on glass in particular was studied using 3H and

  4. Urinary albumin excretion predicts cardiovascular and noncardiovascular mortality in general population

    NARCIS (Netherlands)

    Hillege, HL; Fidler, [No Value; Diercks, GFH; van Gilst, WH; de Zeeuw, D; van Veldhuisen, DJ; Gans, ROB; Janssen, WMT; Grobbee, DE; de Jong, PE

    2002-01-01

    Background-For the general population, the clinical relevance of an increased urinary albumin excretion rate is still debated. Therefore, we examined the relationship between urinary albumin excretion and all-cause mortality and mortality caused by cardiovascular (CV) disease and non-CV disease in t

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

    Directory of Open Access Journals (Sweden)

    Shweta Garg

    2013-06-01

    Full Text Available 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.

  6. 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...

  7. 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 m...

  8. SYNTHESIS AND CHARACTERIZATION OF SURFACE-HYPERBRANCHED MAGNETITE NANOPARTICLE FOR BOVINE SERUM ALBUMIN IMMOBILIZATION

    Institute of Scientific and Technical Information of China (English)

    Bifeng Pan; Feng Gao; Hongchen Gu

    2004-01-01

    A hyperbranched polyamidoamine polymer was synthesized on the surface of magnetite nanoparticles to enhance bovine serum albumin (BSA) immobilization efficiency. The amount of immobilized bovine serum albumin (BSA)on the surface-hyperbranched magnetite nanoparticle was up to 2.5 times as much as that of magnetite nanoparticle modified with only amino silane.

  9. Increased transcapillary escape rate of albumin in type 1 (insulin-dependent) diabetic patients with microalbuminuria

    DEFF Research Database (Denmark)

    Feldt-Rasmussen, B

    1986-01-01

    The transcapillary escape rate, intravascular mass and outflux of albumin were measured in 75 Type 1 (insulin-dependent) diabetic patients. The groups were defined as: group 1: normal urinary albumin excretion, less than 30 mg/24 h (n = 21); group 2: microalbuminuria, 30-300 mg/24 h (n = 36); group...

  10. Interaction of graphene oxide with albumins: Effect of size, pH, and temperature.

    Science.gov (United States)

    Šimšíková, M

    2016-03-01

    Understanding the interaction between graphene oxide (GO) and the biomolecules is fundamentally essential, especially for disease- and drug-related peptides and proteins. In this study, the interaction between GO and albumins (bovine serum albumin, human serum albumin, and bovine alpha-lactalbumin) has been performed by fluorescence and UV-Vis spectroscopic techniques. The fluorescence quenching mechanism between GO and aromatic acids residues with intrinsic fluorescence was determined as mainly static quenching in combination with dynamic quenching. The optimal conditions for the most effective affinity between albumins and GO have been estimated at neutral pH and room temperature. The strong impact of the size of graphene oxide on the interaction between proteins and graphene oxide has been confirmed, as well. The interaction between GO and albumins has been examined as electrostatic and hydrophobic. The electrostatic interaction was confirmed by pH effect, while the hydrophobic interaction was proved by the presence of Poloxamer188. The CD spectra of albumins exhibit decreasing helicity in the secondary structure of albumins upon the addition of GO. However, no significant changes in position and shape of characteristic negative bands have been noted. Mentioned changes indicate the successful interaction between GO and proteins, the predominantly α-helical structure of albumins has been preserved.

  11. Increased metabolic turnover rate and transcapillary escape rate of albumin in long-term juvenile diabetics

    DEFF Research Database (Denmark)

    Parving, H H; Rossing, N; Sander, E

    1975-01-01

    smaller than 0.05). The previously reported decrease in the intravascular albumin mass in long-term diabetics was thus confirmed by an average of 59.0 g/m2 surface area, compared with a normal value of 71.7 g/m2-(minus18%) (P smaller than 0.005). The albumin metabolic rate was increased, the fractional...

  12. Covalent binding of organophosphorothioates to albumin: A new perspective for OP-pesticide biomonitoring?

    NARCIS (Netherlands)

    Noort, D.; Hulst, A.G.; Zuylen, A. van; Rijssel, E. van; Schans, M.J. van der

    2009-01-01

    We here report on the covalent binding of various organophosphorothioate (OPT) pesticides to albumin at in vitro exposure levels that did not give rise to butyrylcholinesterase inhibition. Adduct formation occurred at the Tyr-411 residue of albumin, as was firmly corroborated by LC-tandem MS analysi

  13. Albuminuria and overall capillary permeability of albumin in acute altitude hypoxia

    DEFF Research Database (Denmark)

    Hansen, J M; Olsen, Niels Vidiendal; Feldt-Rasmussen, B

    1994-01-01

    The mechanism of proteinuria at high altitude is unclear. Renal function and urinary excretion rate of albumin (Ualb) at rest and during submaximal exercise and transcapillary escape rate of 125I-labeled albumin (TERalb) were investigated in 12 normal volunteers at sea level and after rapid and p...

  14. Pharmaceutical aspects of the recombinant human serum albumin dimer: structural characteristics, biological properties, and medical applications.

    Science.gov (United States)

    Taguchi, Kazuaki; Chuang, Victor Tuan Giam; Maruyama, Toru; Otagiri, Masaki

    2012-09-01

    Human serum albumin is the most abundant protein in the blood. It is clinically used in the treatment of severe hypoalbuminemia and as a plasma expander. The use of albumins as a carrier for drugs is currently being developed, and some are now in the preclinical and clinical trial stages. The main technologies for utilizing an albumin as a drug carrier are protein fusion, polymerization and surface modification, and so on. Among these technologies, albumin dimerization has wide clinical applications as a plasma expander as well as a drug carrier. Despite the fact that many reports have appeared on drugs using an albumin dimer as a carrier, our knowledge of the characteristics of the albumin dimer itself is incomplete. In this review, we summarize the structural characteristics of recombinant albumin dimers produced by two methods, namely, chemical linkage with 1,6-bis(maleimido)hexane and genetically linked with an amino acid linker, and the physicochemical characteristics and biological properties of these preparations. Finally, the potential for pharmaceutical applications of albumin dimers in clinical situations is discussed.

  15. A Novel Albumin-Based Tissue Scaffold for Autogenic Tissue Engineering Applications

    Science.gov (United States)

    Li, Pei-Shan; -Liang Lee, I.; Yu, Wei-Lin; Sun, Jui-Sheng; Jane, Wann-Neng; Shen, Hsin-Hsin

    2014-07-01

    Tissue scaffolds provide a framework for living tissue regeneration. However, traditional tissue scaffolds are exogenous, composed of metals, ceramics, polymers, and animal tissues, and have a defined biocompatibility and application. This study presents a new method for obtaining a tissue scaffold from blood albumin, the major protein in mammalian blood. Human, bovine, and porcine albumin was polymerised into albumin polymers by microbial transglutaminase and was then cast by freeze-drying-based moulding to form albumin tissue scaffolds. Scanning electron microscopy and material testing analyses revealed that the albumin tissue scaffold possesses an extremely porous structure, moderate mechanical strength, and resilience. Using a culture of human mesenchymal stem cells (MSCs) as a model, we showed that MSCs can be seeded and grown in the albumin tissue scaffold. Furthermore, the albumin tissue scaffold can support the long-term osteogenic differentiation of MSCs. These results show that the albumin tissue scaffold exhibits favourable material properties and good compatibility with cells. We propose that this novel tissue scaffold can satisfy essential needs in tissue engineering as a general-purpose substrate. The use of this scaffold could lead to the development of new methods of artificial fabrication of autogenic tissue substitutes.

  16. Temporal and spatial expression of 2S albumin in castor (Ricinus communis L.).

    Science.gov (United States)

    Ahn, Yeh-Jin; Chen, Grace Q

    2007-11-28

    We studied the temporal and spatial expression of the 2S albumin in castor (Ricinus communis L.) during seed development, germination, post-germination, and plant development. Quantitative polymerase chain reaction analysis showed that the 2S albumin transcript accumulated to a maximum level at the middle of seed development, showing a bell-shaped temporal pattern. Residual levels of the transcript were present in the mature seed and degraded rapidly upon germination. Immunodetection analysis was performed using an anti-2S albumin antibody under reducing conditions. During seed development, the 2S albumin precursor pro-protein began to be synthesized at 26 days after pollination (DAP); the pro-protein was thereafter processed to mature proteins at 40 DAP, suggesting that the post-translation modification of 2S albumin takes place during this time period. Both the 2S albumin precursor pro-protein and the mature proteins accumulated throughout seed maturation and desiccation stages. During seed germination, both forms of the 2S albumin proteins were present in endosperm and cotyledon until the completion of germination and degraded rapidly afterwards. However, the antibody also detected a group of proteins/peptides in endosperm and cotyledon when the seeds progressed to germination and post-germination stages. A 14 kDa protein in the leaves of fully developed seedlings and mature plants also reacted to the anti-2S albumin antibody. The identity of the proteins accumulated in germinating seed and leaf remains unknown.

  17. Albumin activates astrocytes and microglia through mitogen-activated protein kinase pathways.

    Science.gov (United States)

    Ralay Ranaivo, Hantamalala; Wainwright, Mark S

    2010-02-08

    Following acute brain injury, albumin may gain access to the brain parenchyma. Clinical studies indicate a protective role for albumin in stroke but an increase in mortality associated with albumin administration following traumatic brain injury. We investigated the effects of albumin on astrocyte and microglial activation, and the role of mitogen-activated protein kinases (MAPK) in these responses. Albumin activated ERK1/2, p38 MAPK and JNK signaling pathways in astrocytes, and induced the production of interleukin (IL)-1beta, inducible nitric oxide (NO) synthase, the NO metabolite nitrite, and the chemokine CX3CL1 while reducing the level of S100B. The release of inflammatory markers by astrocytes was partially dependent on p38 MAPK and ERK1/2 pathways, but not JNK. In microglia, albumin exposure activated all three MAPK pathways and produced an increase in IL-1beta and nitrite. Inhibition of p38 MAPK in microglia leads to an increased level of IL1beta, while inhibition of all three MAPKs suppressed the release of nitrite. These results suggest that albumin activates astrocytes and microglia, inducing inflammatory responses involved both in the mechanisms of cellular injury and repair via activation of MAPK pathways, and thereby implicate glial activation in the clinical responses to administration of albumin.

  18. Expression of renal cubilin and its potential role in tubulointerstitial inflammation induced by albumin overload

    Institute of Scientific and Technical Information of China (English)

    Jurong YANG; Yani HE; Haiying SHEN; Hanlu DING; Kailong LI; Huiming WANG

    2008-01-01

    Sustained proteinuria is an independent risk factor leading to kidney fibrosis and end-stage renal fail-ure. Over-reabsorption of filtered proteins, notably albu-min, has been proved to trigger interstitial inflammation and fibrosis in proteinuric renal disease. Cubilin, an endo-cytic receptor expressed on the renal tubular brush bor-der, is responsible for albumin reabsorption in physiologic condition. However, little is known about whether it is required for activation of tubular cells induced by albu-min overload. In this work, we investigated the change of cubilin expression and its potential role in albumin-induced up-regulation of chemokines synthesis in vivo and in vitro. Twenty-six patients with nephrotic syndrome were enrolled in this study. Proximal tubule uptake of albumin, expression of apical membrane cubilin and infiltrating cells in kidney interstitium were determined by immunocytochemistry. In vitro, the transcription of cubilin in HK2 cells after exposure to albumin was ana-lyzed by real-time PCR. Endocytosis of albumin in HK2 cells was examined by fluorescent microscope. The influ-ence of inhibition of cubilin on albumin-induced expres-sions of monocyte chemoattractant protein 1 (MCP-1) and regulated upon activation normal T-cell expressed and secreted (RANTES) was investigated by Western blot. The intensity of luminal cubilin and tubular accu-mulation of albumin were significantly increased in nephrotic kidneys. The expression of MCP-1 and RANTES was up-regulated, and there were spatial rela-tionships in localization between these chemokines and cubilin as well as intracellular albumin in kidney tissues. Infiltration of CD-3 and ED-1-positive cells was predom-inant in tubulointerstitial areas displaying signs of increases of cubilin expression and albumin accumula-tion. In vitro, the transcription of cubilin mRNA in HK2 cells was enhanced after 24 h exposure to albumin in a dose-dependent manner. Inhibition of endocytosis of albumin by antisense

  19. A method for estimation of plasma albumin concentration from the buffering properties of whole blood

    DEFF Research Database (Denmark)

    Rees, Stephen Edward; Diemer, Tue; Kristensen, Søren Risom

    2012-01-01

    was diluted at 3 different levels giving 57 data sets. Calculated and measured plasma albumin concentrations were compared using correlation coefficient (r(2)), regression line, and Bland-Altman bias and limits of agreement. RESULTS: Albumin levels covered the clinically interesting range from 8.8 to 53.3 g....../L. Calculated and measured plasma albumin concentrations compared well with r(2) = 0.9, a regression line of albumin-calculated = 1.05 × albumin-measured - 2.25, a small average bias between measured and calculated values of 0.7 g/L, and Bland-Altman limits of agreement of 10 g/L. CONCLUSIONS: This new method...

  20. Renal albumin excretion: twin studies identify influences of heredity, environment, and adrenergic pathway polymorphism

    DEFF Research Database (Denmark)

    Rao, Fangwen; Wessel, Jennifer; Wen, Gen;

    2007-01-01

    Albumin excretion marks early glomerular injury in hypertension. This study investigated heritability of albumin excretion in twin pairs and its genetic determination by adrenergic pathway polymorphism. Genetic associations used single nucleotide polymorphisms at adrenergic pathway loci spanning...... biosynthesis (tyrosine hydroxylase), catabolism (monoamine oxidase A), storage/release (chromogranin A), receptor target (dopamine D1 receptor), and postreceptor signal transduction (sorting nexin 13 and rho kinase). Epistasis (gene-by-gene interaction) occurred between alleles at rho kinase, tyrosine...... hydroxylase, chromogranin A, and sorting nexin 13. Dopamine D1 receptor polymorphism showed pleiotropic effects on both albumin and dopamine excretion. These studies establish new roles for heredity and environment in albumin excretion. Urinary excretions of albumin and catecholamines are highly heritable...

  1. Transcapillary escape rate of albumin in hypertensive patients with type 1 (insulin-dependent) diabetes mellitus

    DEFF Research Database (Denmark)

    Nørgaard, K; Jensen, T; Feldt-Rasmussen, B

    1993-01-01

    . The systemic blood pressure and the transcapillary escape rate of albumin were measured in the following groups after 4 weeks without antihypertensive treatment: Group 1--eleven healthy control subjects. Group 2--ten Type 1 (insulin-dependent) diabetic patients with incipient nephropathy (urinary albumin......Diabetic patients with elevated urinary albumin excretion rate (incipient or clinical nephropathy) also have an increased transcapillary escape rate of albumin. This study was designed to clarify whether this is caused by a general vascular dysfunction or by elevated systemic blood pressure...... excretion rate: 30-300 mg/24 h) and normal blood pressure. Group 3--eleven non-diabetic patients with essential hypertension. Group 4--nine Type 1 diabetic patients with hypertension but normal urinary albumin excretion (diabetic patients with nephropathy (urinary...

  2. Antimicrobial Activity of Ceftriaxone Compared with Cefotaxime in the Presence of Serum Albumin

    Directory of Open Access Journals (Sweden)

    Swapan K Nath

    1995-01-01

    Full Text Available The effect of serum albumin on the antimicrobial activity of ceftriaxone, cefotaxime, and a 1:1 ratio of cefotaxime and its desacetyl metabolite against nonpseudomonal Gram-negative bacilli was determined. Antimicrobial activity of drugs was evaluated by measuring minimum inhibitory (mic and bactericidal (mbc concentrations in broth with and without human serum albumin. The analysis of logarithmically transformed mean mics and mbcs showed that there was a highly significant interaction between drug and serum albumin (P<0.0001. The inhibitory and bactericidal activities were greatest for cefotaxime followed by cefotaxime/desacetylcefotaxime and ceftriaxone (P<0.01. Time-kill kinetics demonstrated that ceftriaxone was less bactericidal than cefotaxime in broth with albumin. On the basis of these results it was concluded that the in vitro antimicrobial activity of ceftriaxone compared with that of cefotaxime was significantly diminished in the presence of serum albumin.

  3. Plasma disappearance of glycated and non-glycated albumin in type 1 (insulin-dependent) diabetes mellitus

    DEFF Research Database (Denmark)

    Bent-Hansen, L; Feldt-Rasmussen, B; Kverneland, Arne;

    1993-01-01

    The fractional plasma escape rates of glycated and non-glycated albumin have earlier been measured in groups of Type 1 (insulin-dependent) diabetic patients and control subjects. The escape of non-glycated albumin was similar in control subjects and normoalbuminuric patients, but elevated...... in patients with micro or macroalbuminuria. In all groups the escape rate of glycated albumin was lower than that of non-glycated albumin. Glycation increases the anionic charge of albumin. To assay for charge-dependent alterations of transport a selectivity index (non-glycated albumin/glycated albumin...... transport ratio) was determined from the disappearance data. The index was high in control subjects (1.021 +/- 0.0057 (SEM)). This reflects a mean difference between the two escape rates of 2.1% per hour (for comparison the mean of the fractional escape rate of non-glycated albumin of the normal control...

  4. Akt recruits Dab2 to albumin endocytosis in the proximal tubule.

    Science.gov (United States)

    Koral, Kelly; Li, Hui; Ganesh, Nandita; Birnbaum, Morris J; Hallows, Kenneth R; Erkan, Elif

    2014-12-15

    Proximal tubule epithelial cells have a highly sophisticated endocytic machinery to retrieve the albumin in the glomerular filtrate. The megalin-cubilin complex and the endocytic adaptor disabled-2 (Dab2) play a pivotal role in albumin endocytosis. We previously demonstrated that protein kinase B (Akt) regulates albumin endocytosis in the proximal tubule through an interaction with Dab2. Here, we examined the nature of Akt-Dab2 interaction. The pleckstrin homology (PH) and catalytic domains (CD) of Akt interacted with the proline-rich domain (PRD) of Dab2 based on yeast-two hybrid (Y2H) experiments. Pull-down experiments utilizing the truncated constructs of Dab2 demonstrated that the initial 11 amino acids of Dab2-PRD were sufficient to mediate the interaction between Akt and Dab2. Endocytosis experiments utilizing Akt1- and Akt2-silencing RNA revealed that both Akt1 and Akt2 mediate albumin endocytosis in proximal tubule epithelial cells; therefore, Akt1 and Akt2 may play a compensatory role in albumin endocytosis. Furthermore, both Akt isoforms phosphorylated Dab2 at Ser residues 448 and 449. Ser-to-Ala mutations of these Dab2 residues inhibited albumin endocytosis and resulted in a shift in location of Dab2 from the peripheral to the perinuclear area, suggesting the physiological relevance of these phosphorylation sites in albumin endocytosis. We conclude that both Akt1 and Akt2 are involved in albumin endocytosis, and phosphorylation of Dab2 by Akt induces albumin endocytosis in proximal tubule epithelial cells. Further delineation of how Akt affects expression/phosphorylation of endocytic adaptors and receptors will enhance our understanding of the molecular network triggered by albumin overload in the proximal tubule.

  5. Megalin mediates transepithelial albumin clearance from the alveolar space of intact rabbit lungs.

    Science.gov (United States)

    Buchäckert, Yasmin; Rummel, Sebastian; Vohwinkel, Christine U; Gabrielli, Nieves M; Grzesik, Benno A; Mayer, Konstantin; Herold, Susanne; Morty, Rory E; Seeger, Werner; Vadász, István

    2012-10-15

    The alveolo-capillary barrier is effectively impermeable to large solutes such as proteins. A hallmark of acute lung injury/acute respiratory distress syndrome is the accumulation of protein-rich oedema fluid in the distal airspaces. Excess protein must be cleared from the alveolar space for recovery; however, the mechanisms of protein clearance remain incompletely understood. In intact rabbit lungs 29.8 ± 2.2% of the radio-labelled alveolar albumin was transported to the vascular compartment at 37°C within 120 min, as assessed by real-time measurement of 125I-albumin clearance from the alveolar space. At 4°C or 22°C significantly lower albumin clearance (3.7 ± 0.4 or 16.2 ± 1.1%, respectively) was observed. Deposition of a 1000-fold molar excess of unlabelled albumin into the alveolar space or inhibition of cytoskeletal rearrangement or clathrin-dependent endocytosis largely inhibited the transport of 125I-albumin to the vasculature, while administration of unlabelled albumin to the vascular space had no effect on albumin clearance. Furthermore, albumin uptake capacity was measured as about 0.37 mg ml−1 in cultured rat lung epithelial monolayers, further highlighting the (patho)physiological relevance of active alveolar epithelial protein transport. Moreover, gene silencing and pharmacological inhibition of the multi-ligand receptor megalin resulted in significantly decreased albumin binding and uptake in monolayers of primary alveolar type II and type I-like and cultured lung epithelial cells. Our data indicate that clearance of albumin from the distal air spaces is facilitated by an active, high-capacity, megalin-mediated transport process across the alveolar epithelium. Further understanding of this mechanism is of clinical importance, since an inability to clear excess protein from the alveolar space is associated with poor outcome in patients with acute lung injury/acute respiratory distress syndrome.

  6. Preparation and characterization of PEG-albumin-curcumin nanoparticles intended to treat breast cancer

    Directory of Open Access Journals (Sweden)

    R Thadakapally

    2016-01-01

    Full Text Available The aim of present research was to prepare novel serum stable long circulating polymeric nanoparticles for curcumin with a modification to the well known and novel nanoparticle albumin bound technology. polyethylene glycol-albumin-curcumin nanoparticles were prepared using serum albumin and poly ethylene glycol using desolvation technique. Nanoparticles were characterized for encapsulation efficiency, particle size and surface morphology. Drug excipient compatibility was determined using fourier transform infrared spectroscopy. Physical state of the drug in the formulations was known by differential scanning colorimetry. In vitrorelease and solubility of the drug from nanoparticles were determined. In vivo Drug release, tissue uptake and kupffer cell uptake was determined with optimized nanoformulation in rats after intravenous administration. Cell viability assay was determined using breast cancer cell line MD-MB-231. Entrapment efficiency for prepared nanoparticle was above 95%. The polyethylene glycol-albumin-curcumin nanoparticles exhibited an interesting release profile with small initial burst followed by slower and controlled release. Solubility of the drug from the formulation was increased. A sustained release of drug from nanoparticles was observed for 35 days in both in vitro and in vivo studies with the optimized formulation. Polyethylene glycol-albumin-curcumin nanoparticles showed lesser liver and kupffer cell uptake as compared to that of curcumin-albumin nanoparticles suggesting the bestowment of stealthness to nanoparticles with pegylation. Also, the antiproliferative activity of polyethylene glycol-albumin-curcumin nanoparticle formulation was more as compared to native curcumin. Polyethylene glycol-albumin-curcumin nanoparticles thus developed can be conveniently used in breast cancer with improved efficacy compared to conventional therapies and as an alternate to nanoparticle albumin bound technology which is used in

  7. 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 fatt

  8. Studies on Reaction Mechanism Between Sparfloxacin and Bovine Serum Albumin

    Institute of Scientific and Technical Information of China (English)

    GUO Ming; ZOU Jian-wei; YI Ping-gui; SHANG Zhi-cai; HU Gui-xiang; YU Qing-sen

    2004-01-01

    The binding of sparfloxacin and bovine serum albumin(BSA) in aqueous solution was studied by means of fluorescence and absorbance spectra, and the interactions influenced by Fe3+ and Cu2+ were explored. Based on the Scatchard′s site binding model and fluorescence quenching, practical formulas for a small molecule ligand attaching to a bio-macromolecule are proposed. The binding parameters were measured according to the suggested models, and the binding distance, the transfer efficiency of energy between sparfloxacin and BSA were obtained in view of the Frster theory of non-radiation energy transfer. The effect of sparfloxacin on the conformation of BSA was analyzed by means of synchronous fluorescence spectroscopy.

  9. Molecular basis of indomethacin-human serum albumin interaction

    DEFF Research Database (Denmark)

    Trivedi, V D; Vorum, H; Honoré, B

    1999-01-01

    in this interaction was studied by modifying exposed and buried lysine residues of HSA with potassium cyanate and studying indomethacin binding with the modified HSA. The data suggest that the interaction takes place via a salt bridge formation between the carboxylate group of indomethacin and a buried lysine residue......, by using a fluorescence quench titration technique. The interaction of indomethacin with human serum albumin has been studied as a function of temperature, ionic strength and pH. The results suggest that electrostatic interaction plays a major role in the binding. The possible role of lysine residues...... of HSA. A technique involving fluorescence enhancement of bilirubin upon its interaction with HSA was used to study its displacement by indomethacin. The displacement, although apparently competitive in nature, was not strong suggesting that the primary sites of interaction of bilirubin and indomethacin...

  10. Interaction of aloe-emodin with human serum albumin

    Institute of Scientific and Technical Information of China (English)

    DU JinFeng; LI Ying; ZHANG Qi; YAO XiaoJun

    2007-01-01

    The presence of several high affinity binding sites on human serum albumin (HAS) makes it a possible target for many drugs. This study is designed to examine the effect of aloe-emodin on HAS by fluorescence, CD spectroscopy and molecular modeling. The results of fluorescence measurements suggested that the hydrophobic interaction was the predominant intermolecular force stabilizing the AE-HAS complex, which was in good agreement with the result of molecular modeling study. And the enthalpy change ΔH0 and the entropy change ΔS0 were calculated to be -7.041 kJ·mol-1 and 76.619 J·mol-1·K-1 according to the Van't Hoff equation. The alterations of protein secondary structure in the presence of AE in aqueous solution were quantitatively calculated from CD spectra, and the content of α-helices obviously increased.

  11. 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.

  12. Albumin microspheres labeled with Ga-67 by chelation: concise communication.

    Science.gov (United States)

    Hnatowich, D J; Schlegel, P

    1981-07-01

    Albumin microspheres have been synthesized eith EDTA and DTPA chelating groups covalently bound to their surface. The microspheres may be labeled with Ga-67 at high yield (97 +/- 2%) by transcomplexation from a 0.1 M Ga-67 acetate solution. With EDTA microspheres the resulting label dissociates only slightly after no detectable dissociation over this period. By contrast, microspheres without chelating groups lose their label virtually completely under these conditions. Following intravenous administration of sized Ga-67 DTPA microspheres in mice, about (84 +/- 16)% of the activity localizes in the lungs at 5 min, with (60 +/- 7)% remaining after 2 hr. Since labeling is by chelation, the microspheres may also be tagged with other metallic radionuclides

  13. Detection of esophageal ulcerations with technetium-99m albumin sucralfate

    Energy Technology Data Exchange (ETDEWEB)

    Goff, J.S.; Adcock, K.A.; Schmelter, R.

    1986-07-01

    Technetium-99m albumin-sucralfate ((/sup 99m/Tc)Su) can be used to demonstrate peptic ulcer disease in man and animals. We evaluated the usefulness of (/sup 99m/Tc)Su for detecting various grades of esophagitis. (/sup 99m/Tc)Su adhered to the distal esophagus for up to 3 hr in five of six patients with esophageal ulcers but adhered to only two of nine with lesser degrees of esophagitis. No adherence was seen in five patients without esophagitis. Thus, (/sup 99m/Tc)Su may not be useful for detecting any but the most severe grade of esophagitis. Based on these results, we speculate that the previously documented beneficial effects of sucralfate on mild to moderate esophagitis may be due to other mechanisms besides adherence to the ulcerated mucosa.

  14. Spectroscopic investigation of interaction between mangiferin and bovine serum albumin

    Science.gov (United States)

    Lin, Hui; Lan, Jingfeng; Guan, Min; Sheng, Fenling; Zhang, Haixia

    2009-09-01

    The mechanism of interaction between mangiferin (MA) and bovine serum albumin (BSA) in aqueous solution was investigated by fluorescence spectra, synchronous fluorescence spectra, absorbance spectra and Fourier transform infrared (FT-IR) spectroscopy. The binding constants and binding sites of MA to BSA at different reaction times were calculated. And the distance between MA and BSA was estimated to be 5.20 nm based on Föster's theory. In addition, synchronous fluorescence and FT-IR measurements revealed that the secondary structures of the protein changed after the interaction of MA with BSA. As a conclusion, the interaction between the anti-diabetes Chinese medicine MA and BSA may provide some significant information for the mechanism of the traditional chinese medicine MA on the protein level to cure diabetes or other diseases.

  15. Albumin-genipin solder for laser tissue welding

    Science.gov (United States)

    Lauto, Antonio; Foster, John; Avolio, Albert; Poole-Warren, Laura

    2004-07-01

    Background. Laser tissue soldering (LTS) is an alternative technique to suturing for tissue repair. One of the major drawbacks of LTS is the weak tensile strength of the solder welds when compared to sutures. In this study, the possibility was investigated for a low cytotoxic crosslinker, acting on amino groups, to enhance the bond strength of albumin solders. Materials and Methods. Solder strips were welded onto rectangular sections of sheep small intestine by a diode laser. The laser delivered in continuous mode mode a power of 170 +/- 10 mW at λ=808 nm, through a multimode optical fiber (core size = 200 μm) to achieve a dose of 10.8 +/- 0.5 J/mg. The solder thickness and surface area were kept constant throughout the experiment (thickness = 0.15 +/- 1 mm, area = 12 +/- 1.2 mm2). The solder incorporated 62% bovine serum albumin, 0.38% genipin, 0.25% indocyanin green dye (IG) and water. Tissue welding was also performed with a similar solder, which did not incorporate genipin, as a control group. The repaired tissue was tested for tensile strength by a calibrated tensiometer. Results. The tensile strength of the "genipin" solder was twice as high as the strength of the BSA solder (0.21 +/- 0.04 N and 0.11 +/- 0.04 N respectively; p~10-15 unpaired t-test, N=30). Discussion. Addition of a chemical crosslinking agent, such as genipin, significantly increased the tensile strength of adhesive-tissue bonds. A proposed mechanism for this enhanced bond strength is the synergistic action of mechanical adhesion with chemical crosslinking by genipin.

  16. Bovine Serum Albumin Metal Complexes for Mimic of SOD

    Indian Academy of Sciences (India)

    GUIFANG YAN; YUFENG HE; GANG LI; YUBING XIONG; PENGFEI SONG; RONG-MIN WANG

    2016-11-01

    Superoxide anion radical (O•−₂ ) is a noxious reactive oxygen species (ROS). Transition metal ion complexes have been generally used as antioxidants to eliminate ROS. In this work, a neoteric watersoluble biopolymer metal complex (BSA-M) was prepared by conjugating the soluble biopolymer bovineserum albumin (BSA) with three transition metal ions (M, M=Cu, Co, Mn). The binding mode and ratio of metal ions bound to albumin were investigated. The BSA-M complexes were characterized by UV-Vis, circular dichroism (CD) spectra and polyacrylamide gel electrophoresis (PAGE). BSA served as polymerscaffold and the metal complex functioned as the catalytic active center. The results demonstrated that the structure of BSA remained unchanged when the binding ratio of transition metal ion complex to BSA was 5:1. Furthermore, the scavenging superoxide anion free radical (O•−₂ ) activity of biopolymer-metal complexes were determined by nitroblue tetrazolium light reduction assay method. The antioxidant capacity of BSA-M has markedly increased. The conjugated BSA-M (M=Cu, Mn) showed preeminent scavenging activity for O•−₂ , and the EC₅₀ value of the BSA-Cu was 0.038±0.0013μmol·L⁻¹, which is comparable to EC₅₀ value (0.041±0.001μmol·L⁻¹) of the natural superoxide dismutase (SOD), the analog quantity reached 107%. As a consequence, it can be considered as a bio-functional mimic of enzyme SOD and has a promising application prospect in antioxidant drug field.

  17. Transcapillary escape rate of albumin and right atrial pressure in chronic congestive heart failure before and after treatment

    DEFF Research Database (Denmark)

    Hesse, B; Parving, H H; Lund-Jacobsen, H;

    1976-01-01

    The transcapillary escape rate of albumin (TERalb), i.e., the fraction of intravascular mass of albumin that passes to the extravascular space per unit of time, was determined from the disappearance of intravenously injected 125I-labeled human serum albumin during the first 60 minutes after injec...

  18. The effect of ascitic fluid hydrostatic pressure on albumin extravasation rate in patients with cirrhosis of the liver

    DEFF Research Database (Denmark)

    Henriksen, J H; Parving, H H; Christiansen, Lasse

    1981-01-01

    Overall transvascular escape rate of albumin [TERalb, i.e. the fraction of intravascular mass of albumin (IVMalb) passing to the extravascular space per unit time] was determined from the disappearance of i.v. injected radioiodinated serum albumin. Patients with tense ascites due to liver cirrhos...

  19. Serum albumin protects from cytokine-induced pancreatic beta cell death by a phosphoinositide 3-kinase-dependent mechanism

    DEFF Research Database (Denmark)

    Kiaer, Caroline; Thams, Peter

    2009-01-01

    ) inhibitors LY294002 (25 micromol/l) and wortmannin (1 micromol/l), suggesting that albumin may rescue beta cells from cytokine-induced cell death by activation of PI3K. In accordance, albumin stimulated phosphorylation of Akt, a down-stream target for PI3K. In conclusion, it is suggested that albumin may...

  20. Increased extravasation and lymphatic return rate of albumin during diuretic treatment of ascites in patients with liver cirrhosis

    DEFF Research Database (Denmark)

    Henriksen, Jens Henrik Sahl; Schlichting, P

    1981-01-01

    During steady state the overall lymphatic return rate of albumin equals the transvascular escape rate of albumin [TERalb, i.e. the fraction of intravascular mass of albumin (IVMalb) passing to the extravascular space per unit time] provided local back-transport is negligible, as previously...

  1. 9 CFR 95.16 - Blood meal, blood albumin, intestines, and other animal byproducts for industrial use...

    Science.gov (United States)

    2010-01-01

    ... 9 Animals and Animal Products 1 2010-01-01 2010-01-01 false Blood meal, blood albumin, intestines... Blood meal, blood albumin, intestines, and other animal byproducts for industrial use; importations permitted subject to restrictions. Blood meal, blood albumin, bone meal, intestines, or other...

  2. Comparison of Calcium Phosphate and Zinc Oxide Nanoparticles as Dermal Penetration Enhancers for Albumin.

    Science.gov (United States)

    Shokri, Narges; Javar, H A

    2015-01-01

    Dermal drug delivery is highly preferred by patients due to its several advantages. Protein therapeutics have attracted huge attention recently. Since dermal delivery of proteins encounter problems, in this investigation, zinc oxide nanoparticles and calcium phosphate nanoparticles were compared as enhancers for dermal permeation of albumin. Albumin was applied simultaneously with zinc oxide nanoparticles or calcium phosphate nanoparticles on pieces of mouse skin. Skin permeation of albumin over time was determined using a diffusion cell. Skin distribution of the nanoparticles and albumin over time was determined by optical and fluorescence microscopy. Zinc oxide nanoparticles and calcium phosphate nanoparticles acted as enhancers for skin permeation of albumin. Cumulative permeated albumin in presence of zinc oxide nanoparticles after 0, 0.5, 1, 1.5 and 2 h, were 0±0, 11.7±3.3, 21.1±3.5, 40.2±3.6 and 40.2±3.6 mg, respectively and in presence of calcium phosphate nanoparticles were 0±0, 20.9±7.4, 33.8±5.5, 33.8±3.7 and 33.8±3.7 mg, respectively. After 0.5 h, little amount of albumin was permeated in presence of every kind of the nanoparticles. After 0.5 or 1 h, the permeated albumin in presence of calcium phosphate nanoparticles was more than that in presence of zinc oxide nanoparticles and after 1.5 h the permeated albumin in presence of zinc oxide nanoparticles was more than that in presence of calcium phosphate nanoparticles. Images of skin distribution of the two nanoparticles over time, were somewhat different and distribution of albumin correlated with the distribution of the nanoparticles alone. The profiles of albumin permeation (in presence of each of the nanoparticles) versus time was delayed and linear for both nanoparticles while the slope for calcium phosphate nanoparticles was higher than zinc oxide nanoparticles. The enhancer effect of zinc oxide nanoparticles was stronger while the enhancer effect of calcium phosphate nanoparticles was

  3. The effects of haemodilution with albumin on coagulation in vitro as assessed by rotational thromboelastometry.

    Science.gov (United States)

    Pathirana, S; Wong, G; Williams, P; Yang, K; Kershaw, G; Dunkley, S; Kam, P C A

    2015-03-01

    We investigated the in vitro viscoelastic changes of progressive haemodilution with 4% albumin compared with normal saline (NS) using rotational thromboelastometry (ROTEM(®), Pentapharm Co., Munich, Germany). Whole blood samples obtained from 20 healthy volunteers were diluted in vitro with 4% albumin or NS by 10%, 20% and 40%. Fibrinogen concentration and ROTEM(®) (EXTEM [screening test for the extrinsic haemostasis system], FIBTEM [EXTEM-based assay for the fibrin part of the clot]) variables including coagulation time, clot formation time (CFT), α-angle, maximum clot firmness and lysis index were measured in the undiluted sample and at each degree of haemodilution. There was no significant difference in fibrinogen concentration at equivalent haemodilutions with normal saline and 4% albumin solutions. Forty percent haemodilution with albumin significantly prolonged coagulation time (EXTEM P=0.007, FIBTEM P=0.0001) and significantly decreased lysis index (FIBTEM P=0.009) compared with NS. A significant decrease in maximum clot firmness from undiluted measurements (P=0.05) was observed at lower haemodilutions with albumin (20% with EXTEM, 10% with FIBTEM) compared with NS (40% with EXTEM and FIBTEM). The adverse effects of large degrees of haemodilution with 4% albumin solution are in excess of what can be explained by haemodilution alone. This study suggests that large degrees of haemodilution with albumin impair fibrinogen activity to a greater extent than equivalent degrees of haemodilution with NS.

  4. Alternative method for measurement of albumin/creatinine ratio using spectrophotometric sequential injection analysis.

    Science.gov (United States)

    Siangproh, Weena; Teshima, Norio; Sakai, Tadao; Katoh, Shuji; Chailapakul, Orawon

    2009-09-15

    A simple, automatic and practical system for successive determination of albumin and creatinine has been developed by combining sequential injection analysis (SIA) and highly sensitive dye-binding assays. Albumin detection was based on the increase in the absorbance due to complex formation between albumin and eosin Y in acidic media. The absorbance of the complex was monitored at 547 nm. For the creatinine assay, the concentration of creatinine was measured by reaction with alkaline picrate to form a colored product which absorbs at 500 nm. The influences of experimental variables such as effects of pH, reagent concentration, standard/sample volume and interferences were investigated. Under optimal conditions, the automated method showed linearity up to 20 mg L(-1) for albumin and 100 mg L(-1) for creatinine. The 3 sigma detection limits were 0.6 and 3.5 mg L(-1) for albumin and creatinine, respectively, and the relative standard deviations (n=10) were 2.49% for 20 mg L(-1) albumin, and 3.14% for 20 mg L(-1) creatinine. Application of the proposed method to the direct analysis of urinary samples yielded results which agreed with those obtained from the Bradford protein assay and a creatinine enzymatic assay according to a paired t-test. The results obtained should be a step towards developing a fully automated and reliable analytical system for clinical research, which requires direct determination of albumin and creatinine and/or its ratios.

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

    Institute of Scientific and Technical Information of China (English)

    Shu-Miao Wu; Dan-Dan Chen

    2016-01-01

    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.

  6. Calmodulin Involvement in Stress-Activated Nuclear Localization of Albumin in JB6 Epithelial Cells.

    Energy Technology Data Exchange (ETDEWEB)

    Weber, Thomas J.; Negash, Sewite; Smallwood, Heather S.; Ramos, Kenneth S.; Thrall, Brian D.; Squier, Thomas C.

    2004-06-15

    We report that in response to oxidative stress, albumin is translocated to the nucleus where it binds in concert with known transcription factors to an antioxidant response element (ARE), which controls the expression of glutathione-S-transferase and other antioxidant enzymes, functioning to mediate adaptive cellular responses. To investigate the mechanisms underlying this adaptive cell response, we have identified linkages between calcium signaling and the nuclear translocation of albumin in JB6 epithelial cells. Under resting conditions, albumin and the calcium regulatory protein, calmodulin (CaM), co-immunoprecipitate using antibodies against either protein, indicating a tight association. Calcium activation of CaM disrupts the association between CaM and albumin, suggesting that transient increases in cytosolic calcium levels function to mobilize intracellular albumin to facilitate its translocation into the nucleus. Likewise, nuclear translocation of albumin is induced by exposure of cells to hydrogen peroxide or a phorbol ester, indicating a functional linkage between reactive oxygen species, calcium, and PKC-signaling pathways. Inclusion of an antioxidant enzyme (i.e., superoxide dismutase) blocks nuclear translocation, suggesting that the oxidation of sensitive proteins functions to coordinate the adaptive cellular response. These results suggest that elevated calcium transients, and associated increases in reactive oxygen species, contribute to adaptive cellular responses through the mobilization and nuclear translocation of cellular albumin to mediate the transcriptional regulation of antioxidant responsive elements.

  7. In vivo biocompatibility, clearance, and biodistribution of albumin vehicles for pulmonary drug delivery.

    Science.gov (United States)

    Woods, A; Patel, A; Spina, D; Riffo-Vasquez, Y; Babin-Morgan, A; de Rosales, R T M; Sunassee, K; Clark, S; Collins, H; Bruce, K; Dailey, L A; Forbes, B

    2015-07-28

    The development of clinically acceptable albumin-based nanoparticle formulations for use in pulmonary drug delivery has been hindered by concerns about the toxicity of nanomaterials in the lungs combined with a lack of information on albumin nanoparticle clearance kinetics and biodistribution. In this study, the in vivo biocompatibility of albumin nanoparticles was investigated following a single administration of 2, 20, and 390μg/mouse, showing no inflammatory response (TNF-α and IL-6, cellular infiltration and protein concentration) compared to vehicle controls at the two lower doses, but elevated mononucleocytes and a mild inflammatory effect at the highest dose tested. The biodistribution and clearance of (111)In labelled albumin solution and nanoparticles over 48h following a single pulmonary administration to mice was investigated by single photon emission computed tomography and X-ray computed tomography imaging and terminal biodistribution studies. (111)In labelled albumin nanoparticles were cleared more slowly from the mouse lung than (111)In albumin solution (64.1±8.5% vs 40.6±3.3% at t=48h, respectively), with significantly higher (P24h indicating that small amounts of activity were cleared from the lungs both by translocation across the lung mucosal barrier, as well as mucociliary clearance. This study provides important information on the fate of albumin vehicles in the lungs, which may be used to direct future formulation design of inhaled nanomedicines.

  8. Species-dependent stereoselective drug binding to albumin: a circular dichroism study.

    Science.gov (United States)

    Pistolozzi, Marco; Bertucci, Carlo

    2008-03-01

    Drug binding to albumins from different mammalian species was investigated to disclose evidence of species-dependent stereoselectivity in drug-binding processes and affinities. This aspect is important for evaluating the reliability of extrapolating distribution data among species. The circular dichroism (CD) signal induced by drug binding to the albumins [human serum albumin (HSA), bovine serum albumin (BSA), rat serum albumin (RSA), and dog serum albumin (DSA)] were measured and analyzed. The binding of selected drugs and metabolites to HSA significantly differed from the binding to the other albumins in terms of affinity and conformation of the bound ligands. In particular, phenylbutazone, a marker of site one on HSA, showed a higher affinity for binding to BSA with respect to RSA, HSA, and DSA, respectively. In the case of diazepam, a marker of site two on HSA, the affinity decreased in order from HSA to DSA, RSA, and BSA. The induced CD spectra were similar in terms of energy and band signs, suggesting almost the same conformation for the bound drug to the different albumins. Stereoselectivity was high for the binding of ketoprofen to HSA and RSA. A different sign was observed for the CD spectra induced by the drug to the two albumins because of the prevalence of a different conformation of the bound drug. Interestingly, the same induced CD spectra were obtained using either the racemic form or the (S)-enantiomer. Finally, significant differences were observed in the affinity of bilirubin, being highest for BSA, then decreasing for RSA, HSA, and DSA. A more complex conformational equilibrium was observed for bound bilirubin.

  9. Impact of serum uric acid, albumin and their interaction on Parkinson's disease.

    Science.gov (United States)

    Wang, Lijun; Hu, Wei; Wang, Jun; Fang, Fangfang; Cheng, Guanliang; Jiang, Yuzhang; Xiao, Hang; Wan, Qi

    2017-02-01

    The study aimed to investigate the correlation between Parkinson's disease (PD) and serum levels of uric acid (UA), albumin and their interaction. A cross-sectional study was conducted to evaluate the relationship of serum UA, albumin with PD. A total of 96 PD patients and 108 healthy controls were recruited at Huai'an First People's Hospital, Nanjing Medical University. Baseline data included age, gender, body mass index (BMI), disease duration, Hoehn and Yahr scale (H&Y) stage, serum UA and albumin levels. The levels of serum UA and albumin were significantly lower in PD patients than those in controls (P = 0.001; P = 0.000). Serum albumin levels were strikingly different in H&Y group (P = 0.004). Multivariable logistic regression showed that the levels of serum UA (P = 0.001, adjusted OR 0.993, 95% CI 0.988-0.997) and albumin (P = 0.000, adjusted OR 0.513, 95% CI 0.425-0.620) were independent risk factors in PD. The receiver operating characteristic (ROC) curve analyses showed that the area under curve (AUC) for serum UA and albumin was 0.669 (95% CI 0.594-0.744) and 0.883 (95% CI 0.835-0.931), respectively. The combination of serum albumin and UA improved the AUC to 0.898 (95% CI 0.854-0.942). Serum UA and albumin levels significantly decreased in PD patients and were independent risk factors for PD. More studies are needed to confirm our findings.

  10. Hot spot(s) of the lung in technetium-99m albumin colloid liver-spleen scintigraphy: case report

    Energy Technology Data Exchange (ETDEWEB)

    Shih, W.J.; Brandenburg, S.; Coupal, J.J.; Sullivan, J.D.; Beeler, J.A.; Magoun, S.; Ryo, U.Y.

    1988-06-01

    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.

  11. Pretreatment serum albumin as a predictor of cancer survival: A systematic review of the epidemiological literature

    Directory of Open Access Journals (Sweden)

    Lis Christopher G

    2010-12-01

    Full Text Available Abstract Background There are several methods of assessing nutritional status in cancer of which serum albumin is one of the most commonly used. In recent years, the role of malnutrition as a predictor of survival in cancer has received considerable attention. As a result, it is reasonable to investigate whether serum albumin has utility as a prognostic indicator of cancer survival in cancer. This review summarizes all available epidemiological literature on the association between pretreatment serum albumin levels and survival in different types of cancer. Methods A systematic search of the literature using the MEDLINE database (January 1995 through June 2010 to identify epidemiologic studies on the relationship between serum albumin and cancer survival. To be included in the review, a study must have: been published in English, reported on data collected in humans with any type of cancer, had serum albumin as one of the or only predicting factor, had survival as one of the outcome measures (primary or secondary and had any of the following study designs (case-control, cohort, cross-sectional, case-series prospective, retrospective, nested case-control, ecologic, clinical trial, meta-analysis. Results Of the 29 studies reviewed on cancers of the gastrointestinal tract, all except three found higher serum albumin levels to be associated with better survival in multivariate analysis. Of the 10 studies reviewed on lung cancer, all excepting one found higher serum albumin levels to be associated with better survival. In 6 studies reviewed on female cancers and multiple cancers each, lower levels of serum albumin were associated with poor survival. Finally, in all 8 studies reviewed on patients with other cancer sites, lower levels of serum albumin were associated with poor survival. Conclusions Pretreatment serum albumin levels provide useful prognostic significance in cancer. Accordingly, serum albumin level could be used in clinical trials to

  12. 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.

  13. Binding interactions of pefloxacin mesylate with bovine lactoferrin and human serum albumin

    Institute of Scientific and Technical Information of China (English)

    FAN Ji-cai; CHEN Xiang; WANG Yun; FAN Cheng-ping; SHANG Zhi-cai

    2006-01-01

    The binding of pefloxacin mesylate (PFLX) to bovine lactoferrin (BLf) and human serum albumin (HSA) in dilute aqueous solution was studied using fluorescence spectra and absorbance spectra. The binding constant K and the binding sites n were obtained by fluorescence quenching method. The binding distance r and energy-transfer efficiency E between pefloxacin mesylate and bovine lactoferrin as well as human serum albumin were also obtained according to the mechanism of Forster-type dipole-dipole nonradiative energy-transfer. The effects of pefloxacin mesylate on the conformations of bovine lactoferrin and human serum albumin were also analyzed using synchronous fluorescence spectroscopy.

  14. Sucrose/bovine serum albumin mediated biomimetic crystallization of calcium carbonate

    Indian Academy of Sciences (India)

    Cheng-Li Yao; Wang-Hua Xu; Ai-Min Ding; Jin-Mao Zhu

    2009-01-01

    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 (SEM), Fourier transform infrared spectrograph (FT-IR) and powder X-ray diffractometry (XRD). The possible formation mechanism of CaCO3 in the sucrose/bovine serum albumin system was discussed.

  15. Protease Inhibition by Oleic Acid Transfer From Chronic Wound Dressings to Albumin

    Energy Technology Data Exchange (ETDEWEB)

    Edwards, J. V.; Howley, Phyllis; Davis, Rachel M.; Mashchak, Andrew D.; Goheen, Steven C.

    2007-08-01

    High elastase and cathepsin G activities have been observed in chronic wounds. These levels can inhibit healing through degradation of growth factors, cytokines, and extracellular matrix proteins. Oleic acid (18:1) is a non-toxic elastase inhibitor with some potential for redressing the imbalance of elastase activity found in chronic wounds. Cotton wound dressing material was characterized as a transfer carrier for affinity uptake of 18:1 by albumin under conditions mimicking chronic wounds. 18:1-treated cotton was examined for its ability to bind and release the fatty acid in the presence of albumin. The mechanism of 18:1 uptake from cotton and binding by albumin was examined with both intact dressings and cotton fiber-designed chromatography. Raman spectra of the albumin-18:1 complexes under liquid-liquid equilibrium conditions revealed fully saturated albumin-18:1 complexes with a 1:1 weight ratio of albumin:18:1. Cotton chromatography under liquid-solid equilibrium conditions revealed oleic acid transfer from cotton to albumin at 27 mole equivalents of 18:1 per mole albumin. Cotton was contrasted with hydrogel, and hydrocolloid wound dressing for its comparative ability to lower elastase activity. Each dressing material evaluated was found to release 18:1 in the presence of albumin with significant inhibition of elastase activity. The 18:1-formulated wound dressings lowered elastase activity in a dose dependent manner in the order cotton gauze > hydrogel > hydrocolloid. In contrast the cationic serine protease Cathepsin G was inihibited by 18:1 within a narrow range of 18:1-cotton formulations. Four per cent Albumin solutions were most effective in binding cotton bound-18:1. However, 2% albumin was sufficient to transfer quantities of 18:1 necessary to achieve a significant elastase-lowering effect. Formulations with 128 mg 18:1/g cotton gauze had equivalent elastase lowering with 1 - 4% albumin. 18:1 bound to cotton wound dressings may have promise in the

  16. Serum Glycated Albumin to Guide the Diagnosis of Diabetes Mellitus.

    Directory of Open Access Journals (Sweden)

    Wan-Chen Wu

    Full Text Available In the diagnosis of diabetes mellitus, hemoglobin A1c (HbA1c is sometimes measured to determine the need of an oral glucose tolerance test (OGTT. However, HbA1c does not accurately reflect glycemic status in certain conditions. This study was performed to test the possibility that measurement of serum glycated albumin (GA better assesses the need for OGTT. From 2006 to 2012, 1559 subjects not known to have diabetes or to use anti-diabetic medications were enrolled. Serum GA was measured, and a 75-g OGTT was then performed to diagnose diabetes. Serum GA correlated significantly to age (r = 0.27, p<0.001, serum albumin (r = -0.1179, age-adjusted p = 0.001, body mass index (r = -0.24, age-adjusted p<0.001, waist circumference (r = -0.16, age-adjusted p<0.001, and plasma GA (r = 0.999, p<0.001, but was unaffected by diet (p = 0.8. Using serum GA at 15% for diagnosis of diabetes, the sensitivity, specificity, and area under the receiver-operating characteristic curve were 74%, 85%, and 0.86, respectively. Applying a fasting plasma glucose (FPG value of < 100 mg/dL to exclude diabetes and of ≥ 126 mg/dL to diagnose diabetes, 14.4% of the study population require an OGTT (OGTT% with a sensitivity of 78.8% and a specificity of 100%. When serum GA value of 14% and 17% were used to exclude and diagnose diabetes, respectively, the sensitivity improved to 83.3%, with a slightly decrease in specificity (98.2%, but a significant increase in OGTT% (35%. Using combined FPG and serum GA cutoff values (FPG < 100 mg/dL plus serum GA < 15% to exclude diabetes and FPG ≥ 126 mg/dL or serum GA ≥ 17% to diagnose diabetes, the OGTT% was reduced to 22.5% and the sensitivity increased to 85.6% with no change in specificity (98.2%. In the diagnosis of diabetes, serum GA measurements can be used to determine the need of an OGTT.

  17. Comparison of normal saline, hypertonic saline albumin and terlipressin plus hypertonic saline albumin in an infant animal model of hypovolemic shock.

    Directory of Open Access Journals (Sweden)

    Javier Urbano

    Full Text Available In series of cases and animal models suffering hemorrhagic shock, the use of vasopressors has shown potential benefits regarding hemodynamics and tissue perfusion. Terlipressin is an analogue of vasopressin with a longer half-life that can be administered by bolus injection. We have previously observed that hypertonic albumin improves resuscitation following controlled hemorrhage in piglets. The aim of the present study was to analyze whether the treatment with the combination of terlipressin and hypertonic albumin can produce better hemodynamic and tissular perfusion parameters than normal saline or hypertonic albumin alone at early stages of hemorrhagic shock in an infant animal model.Experimental, randomized animal study including 39 2-to-3-month-old piglets. Thirty minutes after controlled 30 ml/kg bleed, pigs were randomized to receive either normal saline (NS 30 ml/kg (n = 13, 5% albumin plus 3% hypertonic saline (AHS 15 ml/kg (n = 13 or single bolus of terlipressin 15 μg/kg i.v. plus 5% albumin plus 3% hypertonic saline 15 ml/kg (TAHS (n = 13 over 30 minutes. Global hemodynamic and tissular perfusion parameters were compared.After controlled bleed a significant decrease of blood pressure, cardiac index, central venous saturation, carotid and peripheral blood flow, brain saturation and an increase of heart rate, gastric PCO2 and lactate was observed. After treatment no significant differences in most hemodynamic (cardiac index, mean arterial pressure and perfusion parameters (lactate, gastric PCO2, brain saturation, cutaneous blood flow were observed between the three therapeutic groups. AHS and TAHS produced higher increase in stroke volume index and carotid blood flow than NS.In this pediatric animal model of hypovolemic shock, albumin plus hypertonic saline with or without terlipressin achieved similar hemodynamics and perfusion parameters than twice the volume of NS. Addition of terlipressin did not produce better results than AHS.

  18. 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.

  19. Complexation of insecticide chlorantraniliprole with human serum albumin: Biophysical aspects

    Energy Technology Data Exchange (ETDEWEB)

    Ding Fei [Department of Chemistry, China Agricultural University, No. 2 Yuanmingyuan Xi Road, Haidian District, Beijing 100193 (China); Liu Wei [College of Economics and Management, China Agricultural University, Beijing 100083 (China); Diao Jianxiong [Department of Chemistry, China Agricultural University, No. 2 Yuanmingyuan Xi Road, Haidian District, Beijing 100193 (China); Yin Bin [Key Laboratory of Pesticide Chemistry and Application Technology, Ministry of Agriculture, Department of Applied Chemistry, China Agricultural University, Beijing 100193 (China); Zhang Li, E-mail: zhli.work@gmail.co [Key Laboratory of Pesticide Chemistry and Application Technology, Ministry of Agriculture, Department of Applied Chemistry, China Agricultural University, Beijing 100193 (China); Sun Ying, E-mail: sunying@cau.edu.c [Department of Chemistry, China Agricultural University, No. 2 Yuanmingyuan Xi Road, Haidian District, Beijing 100193 (China)

    2011-07-15

    Chlorantraniliprole is a novel insecticide belonging to the diamide class of selective ryanodine receptor agonists. A biophysical study on the binding interaction of a novel diamide insecticide, chlorantraniliprole, with staple in vivo transporter, human serum albumin (HSA) has been investigated utilizing a combination of steady-state and time-resolved fluorescence, circular dichroism (CD), and molecular modeling methods. The interaction of chlorantraniliprole with HSA gives rise to fluorescence quenching through static mechanism, this corroborates the fluorescence lifetime outcomes that the ground state complex formation and the predominant forces in the HSA-chlorantraniliprole conjugate are van der Waals forces and hydrogen bonds, as derived from thermodynamic analysis. The definite binding site of chlorantraniliprole in HSA has been identified from the denaturation of protein, competitive ligand binding, and molecular modeling, subdomain IIIA (Sudlow's site II) was designated to possess high-affinity binding site for chlorantraniliprole. Moreover, using synchronous fluorescence, CD, and three-dimensional fluorescence we testified some degree of HSA structure unfolding upon chlorantraniliprole binding. - Highlights: {yields} Our study highlights for the first time how binding dynamics can predominate for the new diamide insecticide, chlorantraniliprole. {yields} Chlorantraniliprole is situated within subdomain IIIA, Sudlow's site II, which is the same as that of indole-benzodiazepine site. {yields} Biophysical and molecular modeling approaches are useful to resolve the ligand interaction with biomacromolecule. {yields} It serves as a protective device in binding and in inactivating potential toxic compounds to which the body is exposed.

  20. Size exclusion chromatographic analysis of polyphenol-serum albumin complexes.

    Science.gov (United States)

    Hatano, Tsutomu; Hori, Mami; Hemingway, Richard W; Yoshida, Takashi

    2003-08-01

    Formation of water-soluble polyphenol-protein complexes was investigated by size-exclusion chromatography (SEC). The combination of (-)-epigallocatechin gallate (EGCG) and bovine serum albumin (BSA), which did not form a precipitate after the solutions were mixed, showed an SEC peak due to complex formation 2-24 h after mixing. Peak size of the complex varied with time, suggesting slow change of the conformation of the protein accompanied by complexation. Formation of the complex was substantiated by ultrafiltration of the mixture; the complex did not pass through a membrane with a 100,000 nominal molecular weight limit (NMWL). The SEC profile varied with the combination of compounds. The peaks due to the complexes showed that the apparent value of the number average molecular weight (M(n)) of the EGCG-BSA complex was 2.8x10(5), while that of a pentagalloylglucose (PGG)-BSA complex was 9.5x10(5) under the conditions used. Dimeric hydrolyzable tannins, oenothein B and cornusiin A, also caused changes in the SEC profile of BSA, although the combinations did not show peaks attributable to formation of such large complexes observed for EGCG and PGG. Procyanidin B3 and (+)-catechin did not cause changes in the SEC profile of BSA. With cytochrome c, EGCG did not show any chromatographic changes.

  1. 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).

  2. Characterization of Modified Magnetite Nanoparticles for Albumin Immobilization

    Directory of Open Access Journals (Sweden)

    A. K. Bordbar

    2014-01-01

    Full Text Available Magnetite Fe3O4 nanoparticles (NPs were prepared by chemical coprecipitation method. Silica-coated magnetite NPs were prepared by sol-gel reaction, subsequently coated with 3-aminopropyltriethoxysilane (APTES via silanization reaction, and then were activated with 2,4,6-trichloro-1,3,5-triazine (TCT and covalently immobilized with bovine serum albumin (BSA. The size and structure of the particles were characterized by transmission electron microscopy (TEM, X-ray powder diffraction (XRD, and dynamic light scattering (DLS techniques. The immobilization was confirmed by Fourier transform infrared spectroscopy (FT-IR. XRD analysis showed that the binding process has not done any phase change to Fe3O4. The immobilization time for this process was 4 h and the amount of immobilized BSA for the initial value of 1.05 mg BSA was about 120 mg/gr nanoparticles. Also, the influences of three different buffer solutions and ionic strength on covalent immobilization were evaluated.

  3. [Preparation of Human Serum Albumin Micro/Nanotubes].

    Science.gov (United States)

    Jiao, Pei-pei; Guo, Yan-li; Niu, Ai-hua; Kang, Xiao-feng

    2016-01-01

    In this research, protein micro/nanotubes were fabricated by alternate layer-by-layer (LbL) assembly of human serum albumin (HSA) and polyethyleneimine (PEI) into polycarbonate (PC) membranes. The experimental conditions of pH values, ionic strength, the depositions cycles and the diameter of porous membrane were discussed. The morphology and composition of tubes were characterized by scanning electron microscope (SEM), transmission electron microscope (TEM), fourier transform infrared spectroscopy (FTIR) and energy dispersive spectroscopy (EDS). The results show that pH and ionic strength of the solution are the key factors that influence the effect of assembly. Micro/nanotubes with good opening hollow tubular structure were obtained when pH 7.4 HSA solution and pH 10.3 PEI solution without NaCl were used in synthesis procedure. The outer diameter of tube was dependent on the PC template, thus the micro/nanotubes size was controlled by the wall thickness, which can be adjusted by the number of layers of the HSA and PEI deposited along the pore walls. To avoid the thin wall being damaged in dissolving the template and vacuum drying, the PEI/HSA bilayer number should not be less than 3. The polar solvent N,N-dimethylformamide (DMF) can dissolve PC template to release the micro/nanotubes.

  4. Albumin adsorption on CoCrMo alloy surfaces

    Science.gov (United States)

    Yan, Yu; Yang, Hongjuan; Su, Yanjing; Qiao, Lijie

    2015-12-01

    Proteins can adsorb on the surface of artificial joints immediately after being implanted. Although research studying protein adsorption on medical material surfaces has been carried out, the mechanism of the proteins’ adsorption which affects the corrosion behaviour of such materials still lacks in situ observation at the micro level. The adsorption of bovine serum albumin (BSA) on CoCrMo alloy surfaces was studied in situ by AFM and SKPFM as a function of pH and the charge of CoCrMo alloy surfaces. Results showed that when the specimens were uncharged, hydrophobic interaction could govern the process of the adsorption rather than electrostatic interaction, and BSA molecules tended to adsorb on the surfaces forming a monolayer in the side-on model. Results also showed that adsorbed BSA molecules could promote the corrosion process for CoCrMo alloys. When the surface was positively charged, the electrostatic interaction played a leading role in the adsorption process. The maximum adsorption occurred at the isoelectric point (pH 4.7) of BSA.

  5. Virus-Enabled Biosensor for Human Serum Albumin.

    Science.gov (United States)

    Ogata, Alana F; Edgar, Joshua M; Majumdar, Sudipta; Briggs, Jeffrey S; Patterson, Shae V; Tan, Ming X; Kudlacek, Stephan T; Schneider, Christine A; Weiss, Gregory A; Penner, Reginald M

    2017-01-17

    The label-free detection of human serum albumin (HSA) in aqueous buffer is demonstrated using a simple, monolithic, two-electrode electrochemical biosensor. In this device, both millimeter-scale electrodes are coated with a thin layer of a composite containing M13 virus particles and the electronically conductive polymer poly(3,4-ethylenedioxy thiophene) or PEDOT. These virus particles, engineered to selectively bind HSA, serve as receptors in this biosensor. The resistance component of the electrical impedance, Zre, measured between these two electrodes provides electrical transduction of HSA binding to the virus-PEDOT film. The analysis of sample volumes as small as 50 μL is made possible using a microfluidic cell. Upon exposure to HSA, virus-PEDOT films show a prompt increase in Zre within 5 s and a stable Zre signal within 15 min. HSA concentrations in the range from 100 nM to 5 μM are detectable. Sensor-to-sensor reproducibility of the HSA measurement is characterized by a coefficient-of-variance (COV) ranging from 2% to 8% across this entire concentration range. In addition, virus-PEDOT sensors successfully detected HSA in synthetic urine solutions.

  6. Human Serum Albumin Complexed with Myristate and AZT

    Energy Technology Data Exchange (ETDEWEB)

    Zhu, Lili; Yang, Feng; Chen, Liqing; Meehan, Edward J.; Huang, Mingdong (UGA); (UAH)

    2008-06-16

    3'-Azido-3'-deoxythymidine (AZT) is the first clinically effective drug for the treatment of human immunodeficiency virus infection. The drug interaction with human serum albumin (HSA) has been an important component in understanding its mechanism of action, especially in drug distribution and in drug-drug interaction on HSA in the case of multi-drug therapy. We present here crystal structures of a ternary HSA-Myr-AZT complex and a quaternary HSA-Myr-AZT-SAL complex (Myr, myristate; SAL, salicylic acid). From this study, a new drug binding subsite on HSA Sudlow site 1 was identified. The presence of fatty acid is needed for the creation of this subsite due to fatty acid induced conformational changes of HSA. Thus, the Sudlow site 1 of HSA can be divided into three non-overlapped subsites: a SAL subsite, an indomethacin subsite and an AZT subsite. Binding of a drug to HSA often influences simultaneous binding of other drugs. From the HSA-Myr-AZT-SAL complex structure, we observed the coexistence of two drugs (AZT and SAL) in Sudlow site 1 and the competition between these two drugs in subdomain IB. These results provide new structural information on HSA-drug interaction and drug-drug interaction on HSA.

  7. Cooperative binding of drugs on human serum albumin

    Science.gov (United States)

    Varela, L. M.; Pérez-Rodríguez, M.; García, M.

    In order to explain the adsorption isotherms of the amphiphilic penicillins nafcillin and cloxacillin onto human serum albumin (HSA), a cooperative multilayer adsorption model is introduced, combining the Brunauer-Emmet-Teller (BET) adsorption isotherm with an amphiphilic ionic adsorbate, whose chemical potential is derived from Guggenheim's theory. The non-cooperative model has been previously proved to qualitatively predict the measured adsorption maxima of these drugs [Varela, L. M., García, M., Pérez-Rodríguez, M., Taboada, P., Ruso, J. M., and Mosquera, V., 2001, J. chem. Phys., 114, 7682]. The surface interactions among adsorbed drug molecules are modelled in a mean-field fashion, so the chemical potential of the adsorbate is assumed to include a term proportional to the surface coverage, the constant of proportionality being the lateral interaction energy between bound molecules. The interaction energies obtained from the empirical binding isotherms are of the order of tenths of the thermal energy, therefore suggesting the principal role of van der Waals forces in the binding process.

  8. Bovine Serum Albumin Nanoparticles Containing Quercetin: Characterization and Antioxidant Activity.

    Science.gov (United States)

    Antônio, Emilli; Khalil, Najeh Maissar; Mainardes, Rubiana Mara

    2016-02-01

    Quercetin is a flavonoid reported as anti-allergic, anti-inflammatory, antiplatelet, anti-microbial, antioxidant, antineurodegenerative and antitumoral. However, due to its low water solubility, its efficacy is restricted. Nanotechnology can be an importante tool to improve the quercetin properties and increase its bioavailability. In this study, bovine serum albumin (BSA) nanoparticles containing quercetin were developed by desolvation technique, characterized the mean particle size, polydispersity, zeta potential, encapsulation efficiency, physical state of drug in nanoparticles and drug release profile as well as their antioxidant activity was evaluated. The influence of glutaraldehyde percentage in nanoparticles properties was evaluated and did not influence the nanoparticles parameters. Nanoparticles presented a mean size around 130 nm and encapsulation efficiency around 85%. Results from X-ray diffractometry showed that the crystal of the drug was converted to an amorphous state in polymeric matrix. Quercetin release profile demonstrated a biphasic pattern and after 96 h approximately 18% of drug was released. Kinetic models demonstrated that the quercetin release followed a second-order model and the release was governed by Fickian diffusion. After 96 h, quercetin-loaded nanoparticles were more effective than free quercetin for scanvenger of radical ABTS + and hypochlorous acid. BSA nanoparticles represents potential carriers for improve quercetin properties.

  9. Albumin adsorption on oxide thin films studied by spectroscopic ellipsometry

    Energy Technology Data Exchange (ETDEWEB)

    Silva-Bermudez, P., E-mail: suriel21@yahoo.com [Instituto de Investigaciones en Materiales, Universidad Nacional Autonoma de Mexico, Circuito Exterior s/n, C.U., 04510, Mexico D.F. (Mexico); Unidad de Posgrado, Facultad de Odontologia, Universidad Nacional Autonoma de Mexico, CU, 04510, Mexico D.F. (Mexico); Rodil, S.E.; Muhl, S. [Instituto de Investigaciones en Materiales, Universidad Nacional Autonoma de Mexico, Circuito Exterior s/n, C.U., 04510, Mexico D.F. (Mexico)

    2011-12-15

    Thin films of tantalum, niobium, zirconium and titanium oxides were deposited by reactive magnetron sputtering and their wettability and surface energy, optical properties, roughness, chemical composition and microstructure were characterized using contact angle measurements, spectroscopic ellipsometry, profilometry, X-ray photoelectron spectroscopy and X-ray diffraction, respectively. The purpose of the work was to correlate the surface properties of the films to the Bovine Serum Albumin (BSA) adsorption, as a first step into the development of an initial in vitro test of the films biocompatibility, based on standardized protein adsorption essays. The films were immersed into BSA solutions with different protein concentrations and protein adsorption was monitored in situ by dynamic ellipsometry; the adsorption-rate was dependent on the solution concentration and the immersion time. The overall BSA adsorption was studied in situ using spectroscopic ellipsometry and it was found to be influenced by the wettability of the films; larger BSA adsorption occurred on the more hydrophobic surface, the ZrO{sub 2} film. On the Ta{sub 2}O{sub 5}, Nb{sub 2}O{sub 5} and TiO{sub 2} films, hydrophilic surfaces, the overall BSA adsorption increased with the surface roughness or the polar component of the surface energy.

  10. Paromomycin-loaded albumin microspheres: efficacy and stability studies.

    Science.gov (United States)

    Khan, Wahid; Kumar, Rajendra; Singh, Sukhvinder; Arora, Sunil Kumar; Kumar, Neeraj

    2013-06-01

    In the present work, paromomycin-loaded albumin microspheres (PM-MS) have been formulated for passive targeting of paromomycin (PM) to macrophages, for the treatment of visceral leishmaniasis (VL). PM-MS were prepared by spray-drying method with a mean particle size of ≈ 3 µm. Thermal and chemical cross-linking methods were used for controlling drug release from the prepared microspheres (MS). PM-MS were then tested for efficacy and stability studies. In efficacy study, in vitro promastigote assay was carried out to assess the susceptibility of promastigote to PM in the concentration range of 5.0-150 µg/ml; cytotoxicity assay was performed to determine possible toxicity of PM for the host cells (peritoneal macrophages) and intracellular amastigote assay was carried out to determine the efficacy of free PM (PM solution) and encapsulated PM (PM-MS). Results obtained indicated a significant increase in efficacy of PM-MS in comparison to PM solution at equivalent concentration. Subsequently, stability studies of prepared formulation was carried out at various temperature and humidity conditions, these studies provided stability of formulation at all tested conditions including accelerated conditions. Thus, it can be concluded that present work provides an optimized formulation with stability and enhanced efficacy.

  11. Interaction of albumin with perylene-diimides with aromatic substituents

    Science.gov (United States)

    Farooqi, Mohammed; Penick, Mark; Burch, Jessica; Negrete, George; Brancaleon, Lorenzo

    2015-03-01

    Polyaromatic hydrocarbons (PAH) binding to proteins remains one of the fundamental aspects of research in biophysics. Ligand binding can regulate the function of proteins. Binding to small ligands remains a very important aspect in the study of the function of many proteins. Perylene diimide or PDI derivatives have attracted initial interest as industrial dyes and pigments. Recently, much attention has been focused on their strong π - π stacks resulting from the large PDI aromatic core. These PDI stacks have distinct optical properties, and provide informative models that mimic the light-harvesting system and initial charge separation and charge transfer in the photosynthetic system. The absorption property of PDI derivatives may be largely tuned from visible to near-infrared region by chemical modifications at the bay-positions. We are currently studying a new class of PDI derivatives with substituents made of the side chains of aromatic amino acids (Tyrosine, Tryptophan and Phenylalanine). We have looked at the fluorescence absorption and emission of these PDIs in water and other organic solvents. PDIs show evidence of dimerization and possible aggregation. We also present binding studies of these PDIs with Human Serum Albumin (HSA). The binding was studied using fluorescence emission quenching of the HSA Tryptophan residue. Stern-Volmer equation is used to derive the quenching constants. PDI binding to HSA also has an effect on the fluorescence emission of the PDIs themselves by red shifting the spectra. Funded by RCMI grant.

  12. Platelet-rich fibrin versus albumin in surgical wound repair: a randomized trial with paired design

    DEFF Research Database (Denmark)

    Danielsen, Patricia L; Ågren, Sven Per Magnus; Jørgensen, Lars Nannestad

    2010-01-01

    To study the effects of autologous platelet-rich fibrin (PRF) versus human albumin on incisional wound breaking strength and subcutaneous collagen deposition in patients undergoing laparoscopic cholecystectomy in a randomized trial....

  13. Electric Field-induced Conformational Transition of Bovine Serum Albumin from α -helix to β -sheet

    Institute of Scientific and Technical Information of China (English)

    2000-01-01

    The irreversible conformational transition of bovine serum albumin (BSA) from α -helix to β -sheet, induced by electric field near the electrode surface, was monitored by circular dichroism (CD) with a long optical path thin layer cell (LOPTLC).

  14. Binding of a new bisphenol analogue, bisphenol S to bovine serum albumin and calf thymus DNA.

    Science.gov (United States)

    Wang, Yan-Qing; Zhang, Hong-Mei; Cao, Jian; Tang, Bo-Ping

    2014-09-05

    Interactions of bisphenol S, a new bisphenol analogue with bovine serum albumin and calf thymus DNA were investigated using different spectroscopic methods and molecular modeling calculation. According to the analysis of experimental and theoretical data, we concluded that hydrophobic interactions and hydrogen bonding primarily mediated the binding processes of bisphenol S with bovine serum albumin and DNA. In addition, the electrostatic force should not be excluded. Molecular modeling studies indicated that the binding site of bisphenol S to bovine serum albumin located in the subdomain IB, while bisphenol S was a groove binder of DNA. In addition, BPS did not obviously induce second structural changes of bovine serum albumin, but it induced a conformational change of calf thymus DNA.

  15. Concentration of fish serum albumin (FSA) in the aqueous extract of Indonesian Perciformes fishes' muscle tissue.

    Science.gov (United States)

    Januar, Hedi Indra; Fajarningsih, Nurrahmi Dewi; Zilda, Dewi Seswita; Bramandito, Aditya; Wright, Anthony D

    2015-01-01

    Fish serum albumin (FSA) is an aquatic resource that has potential to be developed as nutraceutical. Therefore, research was undertaken to assess albumin levels in the aqueous extract of muscle tissue of several Perciformes commonly available at a local fish market in Indonesia. Three random replicates for each of 17 Perciformes species were collected and assessed for their FSA content by application of a reversed-phase (C4) HPLC analytical method. Results of these analyses showed that the albumin concentration of the extracts was in the range 3.49-12.61 g/L, and that they varied significantly (P fishes from the family Scrombidae showed the highest concentration (12.61 g/L) of FSA, they would likely have the most value as a source for production of albumin-based nutritional and/or clinical products.

  16. Interaction of cyclodextrins with human and bovine serum albumins: A combined spectroscopic and computational investigation

    Indian Academy of Sciences (India)

    Saptarshi Ghosh; Bijan Kumar Paul; Nitin Chattopadhyay

    2014-07-01

    Interaction of cyclodextrins (CDs) with the two most abundant proteins, namely human serum albumin (HSA) and bovine serum albumin (BSA), has been investigated using steady-state and time-resolved fluorometric techniques, circular dichroism measurements and molecular docking simulation. The study reveals that the three CDs interact differently on the fluorescence and fluorescence lifetimes of the serum albumins. However, fluorescence anisotropy and circular dichroism are not affected. Depending on their size, different CDs bind to the serum albumins in different positions, resulting in changes in the spectral behaviour of the proteins. Docking study suggests the probable binding sites of the three CDs with the proteins. Combined experimental and computational studies imply that sufficiently high concentration of CDs causes loosening of the rigid structures of these transport proteins, although their secondary structures remain intact. Thus, CDs are found to be safe for the serum proteins from the structural point of view.

  17. Oleic acid loading does not add to the nephrotoxic effect of albumin in an amphibian and chronic rat model of kidney injury

    NARCIS (Netherlands)

    van Timmeren, Mirjan M.; Gross, Marie-Luise; Hanke, Wilfried; Klok, Pieter A.; van Goor, Harry; Stegeman, Coen A.; Bakker, Stephan J. L.

    2008-01-01

    Background. Under proteinuric conditions, ultrafiltrated albumin can induce an inflammatory and fibrotic response in proximal tubular cells. It is unclear whether albumin per se or compounds bound to albumin are nephrotoxic. Some studies have supported the toxicity of albumin-bound fatty acids; howe

  18. Fibrinogen and FXIII dose response effects on albumin-induced coagulopathy.

    OpenAIRE

    Hanna, Jennifer; Winstedt, Dag; Schött, Ulf

    2013-01-01

    Objectives. Natural colloid albumin induces a lesser degree of dilutional coagulopathy than synthetic colloids. Fibrinogen concentrate has emerged as a promising strategy to treat coagulopathy, and factor XIII (FXIII) works synergistically with fibrinogen to correct coagulopathy following haemodilution with crystalloids. Our objectives were to examine the ability of fibrinogen and FXIII concentrates to reverse albumin-induced dilutional coagulopathy. Methods. High and low concentrations of bo...

  19. Determinants of formation of aflatoxin-albumin adducts: a seven-township study in Taiwan

    OpenAIRE

    2002-01-01

    Dietary exposure to aflatoxins is one of the major risk factors for hepatocellular carcinoma. Individual susceptibility to aflatoxin-induced hepatocarcinogenesis may be modulated by both genetic and environmental factors affecting metabolism. A cross-sectional study was performed to evaluate determinants of the formation of aflatoxin covalently bound to albumin (AFB1-albumin adducts). A total of 474 subjects who were free of liver cancer and cirrhosis and were initially selected as controls f...

  20. Pretreatment serum albumin as a predictor of cancer survival: A systematic review of the epidemiological literature

    OpenAIRE

    Lis Christopher G; Gupta Digant

    2010-01-01

    Abstract Background There are several methods of assessing nutritional status in cancer of which serum albumin is one of the most commonly used. In recent years, the role of malnutrition as a predictor of survival in cancer has received considerable attention. As a result, it is reasonable to investigate whether serum albumin has utility as a prognostic indicator of cancer survival in cancer. This review summarizes all available epidemiological literature on the association between pretreatme...

  1. Platelet-rich fibrin versus albumin in surgical wound repair: a randomized trial with paired design

    DEFF Research Database (Denmark)

    Danielsen, Patricia L; Ågren, Sven Per Magnus; Jørgensen, Lars Nannestad

    2010-01-01

    To study the effects of autologous platelet-rich fibrin (PRF) versus human albumin on incisional wound breaking strength and subcutaneous collagen deposition in patients undergoing laparoscopic cholecystectomy in a randomized trial.......To study the effects of autologous platelet-rich fibrin (PRF) versus human albumin on incisional wound breaking strength and subcutaneous collagen deposition in patients undergoing laparoscopic cholecystectomy in a randomized trial....

  2. Conformational changes in the bilirubin-human serum albumin complex at extreme alkaline pH

    DEFF Research Database (Denmark)

    Honoré, B; Frandsen, P C

    1986-01-01

    Light-absorption, c.d. and fluorescence of the bilirubin-albumin complex were investigated at extreme alkaline pH. Above pH 11.1 albumin binds the bilirubin molecule, twisted oppositely to the configuration at more neutral pH. On the basis of light-absorption it is shown that two alkaline...... between tryptophan-214 and bilirubin, and partly exposing the liganded bilirubin to the solvent. Udgivelsesdato: 1986-Jun-1...

  3. Hypertrophy of mature Xenopus muscle fibres in culture induced by synergy of albumin and insulin.

    Science.gov (United States)

    Jaspers, R T; van Beek-Harmsen, B J; Blankenstein, M A; Goldspink, G; Huijing, P A; van der Laarse, W J

    2008-10-01

    The aim of this study was to investigate effects of albumin and insulin separately as well as in combination on mature muscle fibres during long-term culture. Single muscle fibres were dissected from m. iliofibularis of Xenopus laevis and attached to a force transducer in a culture chamber. Fibres were cultured in a serum-free medium at slack length (mean sarcomere length 2.3 mum) for 8 to 22 days. The medium was supplemented with (final concentrations): (1) bovine insulin (6 nmol/L or 200-600 nmol/L), (2) 0.2% bovine albumin or (3) 0.2% bovine albumin in combination with insulin (120 nmol/L). In culture medium with insulin, 50% of the muscle fibres became in-excitable within 7-12 days, whereas the other 50% were stable. Caffeine contractures of in-excitable muscle fibres produced 80.4 +/- 2.4% of initial peak tetanic force, indicating impaired excitation-contraction (E-C) coupling in in-excitable fibres. In the presence of albumin, all cultured muscle fibres were stable for at least 10 days. Muscle fibres cultured in medium with insulin or albumin exclusively did not hypertrophy or change the number of sarcomeres in series. In contrast, muscle fibres cultured with both albumin and insulin showed an increase in tetanic force and fibre cross-sectional area of 19.6 +/- 2.8% and 32.5 +/- 4.9%, respectively, (means +/- SEM.; P = 0.007) after 16.3 +/- 1.7 days, whereas the number of sarcomeres in series remained unchanged. We conclude that albumin prevents muscle fibre damage and preserves E-C coupling in culture. Furthermore, albumin is important in regulating muscle fibre adaptation by a synergistic action with growth factors like insulin.

  4. Hydroxyethyl starch 130/0.38-0.45 versus crystalloid or albumin in patients with sepsis

    DEFF Research Database (Denmark)

    Haase, Nicolai; Perner, Anders; Inkeri Hennings, Louise;

    2013-01-01

    To assess the effects of fluid therapy with hydroxyethyl starch 130/0.38-0.45 versus crystalloid or albumin on mortality, kidney injury, bleeding, and serious adverse events in patients with sepsis.......To assess the effects of fluid therapy with hydroxyethyl starch 130/0.38-0.45 versus crystalloid or albumin on mortality, kidney injury, bleeding, and serious adverse events in patients with sepsis....

  5. 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.

  6. Raman spectroscopy provides a powerful diagnostic tool for accurate determination of albumin glycation.

    Directory of Open Access Journals (Sweden)

    Narahara Chari Dingari

    Full Text Available We present the first demonstration of glycated albumin detection and quantification using Raman spectroscopy without the addition of reagents. Glycated albumin is an important marker for monitoring the long-term glycemic history of diabetics, especially as its concentrations, in contrast to glycated hemoglobin levels, are unaffected by changes in erythrocyte life times. Clinically, glycated albumin concentrations show a strong correlation with the development of serious diabetes complications including nephropathy and retinopathy. In this article, we propose and evaluate the efficacy of Raman spectroscopy for determination of this important analyte. By utilizing the pre-concentration obtained through drop-coating deposition, we show that glycation of albumin leads to subtle, but consistent, changes in vibrational features, which with the help of multivariate classification techniques can be used to discriminate glycated albumin from the unglycated variant with 100% accuracy. Moreover, we demonstrate that the calibration model developed on the glycated albumin spectral dataset shows high predictive power, even at substantially lower concentrations than those typically encountered in clinical practice. In fact, the limit of detection for glycated albumin measurements is calculated to be approximately four times lower than its minimum physiological concentration. Importantly, in relation to the existing detection methods for glycated albumin, the proposed method is also completely reagent-free, requires barely any sample preparation and has the potential for simultaneous determination of glycated hemoglobin levels as well. Given these key advantages, we believe that the proposed approach can provide a uniquely powerful tool for quantification of glycation status of proteins in biopharmaceutical development as well as for glycemic marker determination in routine clinical diagnostics in the future.

  7. Raman spectroscopy provides a powerful diagnostic tool for accurate determination of albumin glycation.

    Science.gov (United States)

    Dingari, Narahara Chari; Horowitz, Gary L; Kang, Jeon Woong; Dasari, Ramachandra R; Barman, Ishan

    2012-01-01

    We present the first demonstration of glycated albumin detection and quantification using Raman spectroscopy without the addition of reagents. Glycated albumin is an important marker for monitoring the long-term glycemic history of diabetics, especially as its concentrations, in contrast to glycated hemoglobin levels, are unaffected by changes in erythrocyte life times. Clinically, glycated albumin concentrations show a strong correlation with the development of serious diabetes complications including nephropathy and retinopathy. In this article, we propose and evaluate the efficacy of Raman spectroscopy for determination of this important analyte. By utilizing the pre-concentration obtained through drop-coating deposition, we show that glycation of albumin leads to subtle, but consistent, changes in vibrational features, which with the help of multivariate classification techniques can be used to discriminate glycated albumin from the unglycated variant with 100% accuracy. Moreover, we demonstrate that the calibration model developed on the glycated albumin spectral dataset shows high predictive power, even at substantially lower concentrations than those typically encountered in clinical practice. In fact, the limit of detection for glycated albumin measurements is calculated to be approximately four times lower than its minimum physiological concentration. Importantly, in relation to the existing detection methods for glycated albumin, the proposed method is also completely reagent-free, requires barely any sample preparation and has the potential for simultaneous determination of glycated hemoglobin levels as well. Given these key advantages, we believe that the proposed approach can provide a uniquely powerful tool for quantification of glycation status of proteins in biopharmaceutical development as well as for glycemic marker determination in routine clinical diagnostics in the future.

  8. Quenching of the intrinsic fluorescence of bovine serum albumin by chlorpromazine and hemin

    Directory of Open Access Journals (Sweden)

    Silva D.

    2004-01-01

    Full Text Available The binding of chlorpromazine (CPZ and hemin to bovine serum albumin was studied by the fluorescence quenching technique. CPZ is a widely used anti-psychotic drug that interacts with blood components, influences bioavailability, and affects function of several biomolecules. Hemin is an important ferric residue of hemoglobin that binds within the hydrophobic region of albumin with high specificity. Quenching of the intrinsic fluorescence of bovine serum albumin (BSA was observed by selectively exciting tryptophan residues at 290 nm. Emission spectra were recorded in the range from 300 to 450 nm for each quencher addition. Stern-Volmer graphs were plotted, and the quenching constant estimated for BSA solution titrated with hemin at 25ºC was 1.44 (± 0.05 x 10(5 M-1. Results showed that bovine albumin tryptophans are not equally accessible to CPZ, in agreement with the idea that polar or charged quenchers have more affinity for amino acid residues on the outer wall of the protein. Hemin added to albumin solution at a molar ratio of 1:1 quenched about 25% of their fluorescence. The quenching effect of CPZ on albumin-hemin solution was stronger than on pure BSA. This increase can be the result of combined conformational changes in the structure of albumin caused firstly by hemin and then by CPZ. Our results suggest that the primary binding site for hemin on bovine albumin may be located asymmetrically between the two tryptophans along the sequence formed by subdomains IB and IIA, closer to tryptophan residue 212.

  9. Evaluation of the Relationship between Salivary Albumin Level and Dental Caries

    Directory of Open Access Journals (Sweden)

    H. Abdolsamadi

    2013-07-01

    Full Text Available Introduction & Objective: Recently, it has been suggested that there might be an association between oral diseases such as dental caries, as well as periodontitis and general health . Re-garding the fact that albumin is an indicator of general health, the aim of the present study was to evaluate the relationship of salivary albumin concentration with dental caries. Materials & Methods: In this descriptive-analytical study 108 patients aged 13-19 years old who had teeth caries were placed in 3 groups with mild, moderate and severe dental caries according to their DMFT value (n=36. Five ml of unstimulated saliva were taken from each participant via Navazesh method and their albumin concentrations were assessed by nephelometery method. Data were analyzed by t-test and ANOVA. Results: The mean concentration of salivary albumin in three experimental groups was 84.442±42.915, 97.964±66.717 and 89.850±33.003, respectively. ANOVA showed that the difference among the mean values was not significant (P=0.09 but the relationship between salivary albumins and sex was significant (P=0.009. Conclusion: According to the results of the present study there was no significant relationship between albumin and dental caries in 13-19 year old individuals. (Sci J Hamadan Univ Med Sci 2013; 20 (2:101-106

  10. Binding of benzodiazepine drugs to bovine serum albumin: A second derivative spectrophotometric study

    Science.gov (United States)

    Omran, Ahmed A.; El-Sayed, Abdel-Aziz; Shehata, Ahmed

    2011-12-01

    The binding constants ( K values) of three benzodiazepine drugs to bovine serum albumin were determined by a second derivative spectrophotometric method. Despite the sample and reference samples were prepared in the same way to maintain the same albumin content in each sample and reference pair, the absorption spectra show that the baseline compensation was incomplete because of the strong background signals caused by bovine serum albumin. Accordingly, further quantitative spectral information could not be obtained from these absorption spectra. On the other hand, the calculated second derivative spectra clearly show isosbestic points indicating the complete removal of the residual background signal effects. Using the derivative intensity differences (Δ D values) of the studied benzodiazepine drugs before and after the addition of albumin, the binding constants were calculated and obtained with R.S.D. of less than 8%. The interactions of drugs with bovine serum albumin were investigated using Scatchard's plot. In addition, the consistency between the fractions of bound benzodiazepine calculated from the obtained K values and the experimental values were established. The results indicate that the second derivative method can be advantageously applicable to the determination of binding constants of drugs to serum albumin without prior separation. Moreover, the validity of the proposed method was confirmed.

  11. Octanoate in Human Albumin Preparations Is Detrimental to Mesenchymal Stromal Cell Culture

    Directory of Open Access Journals (Sweden)

    Way-Wua Wong

    2015-01-01

    Full Text Available Cell therapies hold great promise as the next major advance in medical treatment. To enable safe, effective ex vivo culture whilst maintaining cell phenotype, growth media constituents must be carefully controlled. We have used a chemically defined mesenchymal stromal cell culture medium to investigate the influence of different preparations of human serum albumin. We examined two aspects of cell culture, growth rate as measured by population doubling time and colony forming ability which is a representative measure of the stemness of the cell population. Albumin preparations showed comparative differences in both of these criteria. Analysis of the albumin bound fatty acids also showed differences depending on the manufacturing procedure used. We demonstrated that octanoate, an additive used to stabilize albumin during pasteurization, slows growth and lowers colony forming ability during ex vivo culture. Further to this we also found the level of Na+/K+ ATPase, a membrane bound cation pump inhibited by octanoate, is increased in cells exposed to this compound. We conclude that the inclusion of human serum albumin in ex vivo growth media requires careful consideration of not only the source of albumin, but also the associated molecular cargo, for optimal cell growth and behavior.

  12. Albumin infusion in humans does not model exercise induced hypervolaemia after 24 hours

    Science.gov (United States)

    Haskell, A.; Gillen, C. M.; Mack, G. W.; Nadel, E. R.

    1998-01-01

    We rapidly infused 234 +/- 3 mL of 5% human serum albumin in eight men while measuring haematocrit, haemoglobin concentration, plasma volume (PV), albumin concentration, total protein concentration, osmolality, sodium concentration, renin activity, aldosterone concentration, and atrial natriuretic peptide concentration to test the hypotheses that plasma volume expansion and plasma albumin content expansion will not persist for 24 h. Plasma volume and albumin content were expanded for the first 6 h after infusion (44.3 +/- 1.9-47.2 +/- 2.0 mL kg-1 and 1.9 +/- 0.1-2.1 +/- 0.1 g kg-1 at pre-infusion and 1 h, respectively, P plasma volume and albumin content decreased significantly from 1 h post-infusion and were not different from pre-infusion (44.8 +/- 1.9 mL kg-1 and 1.9 +/- 0.1 g kg-1, respectively). Plasma aldosterone concentration showed a significant effect of time over the 24 h after infusion (P plasma volume and 10.5% expansion of plasma albumin content by infusion does not remain in the vascular space for 24 h and suggest a redistribution occurs between the intravascular space and interstitial fluid space.

  13. The evidence for small-volume resuscitation with hyperoncotic albumin in critical illness.

    Science.gov (United States)

    Myburgh, John A

    2008-01-01

    Small-volume resuscitation of critically ill patients with hyperoncotic albumin offers a number of theoretical advantages, such as increasing intravascular volume in excess of the volume of fluid administered and reducing interstitial edema. Whilst iso-oncotic albumin has been shown to be equi-effective to isotonic saline for the resuscitation of critically ill patients without associated traumatic brain injury, the efficacy of hyperoncotic albumin for resuscitation has not been evaluated in large-scale randomized-controlled trials. Overall, the evidence for resuscitation with hyper-oncotic albumin is limited by studies of poor methodological quality with heterogenous study populations and control regimens. There is marginal qualitative evidence of improvements in surrogate outcomes in disparate patient populations, but no evidence of any survival benefit associated with resuscitation with hyperoncotic albumin. Given the lack of evidence and clinical uncertainty about the efficacy of hyperoncotic albumin, a large-scale randomized-controlled trial is required to determine its role in the acute resuscitation of hypovolemic or hypoalbuminemic critically ill patients.

  14. Exploring the binding mechanism of ondansetron hydrochloride to serum albumins: spectroscopic approach.

    Science.gov (United States)

    B, Sandhya; Hegde, Ashwini H; K C, Ramesh; J, Seetharamappa

    2012-02-01

    The mechanism of interaction of ondansetron hydrochloride (OND) to serum albumins [bovine serum albumin (BSA) and human serum albumin (HSA)] was studied for the first time employing fluorimetric, circular dichroism, FTIR and UV-vis absorption techniques under the simulated physiological conditions. Fluorimetric results were utilized to investigate the binding and conformational characteristics of protein upon interaction with varying concentrations of the drug. Higher binding constant values revealed the strong interaction between the drug and protein while the number of binding sites close to unity indicated single class of binding site for OND in protein. Thermodynamic results revealed that both hydrogen bond and hydrophobic interactions played a major role in stabilizing drug-protein complex. Site marker competitive experiments indicated that the OND bound to albumins at subdomin II A (Sudlow's site I). Further, the binding distance between OND and serum albumin was calculated based on the Förster's theory of non-radioactive energy transfer and found to be 2.30 and 3.41 nm, respectively for OND-BSA and OND-HSA. The circular dichroism data revealed that the presence of OND decreased the α-helix content of serum albumins. 3D-fluorescence results also indicated the conformational changes in protein upon interaction with OND. Further, the effects of some cations have been investigated in the interaction of drug to protein.

  15. Interactions Between Sirolimus and Anti-Inflammatory Drugs: Competitive Binding for Human Serum Albumin

    Science.gov (United States)

    Khodaei, Arash; Bolandnazar, Soheila; Valizadeh, Hadi; Hasani, Leila; Zakeri-Milani, Parvin

    2016-01-01

    Purpose: The aim of the present study was investigating the effects of three anti-inflammatory drugs, on Sirolimus protein biding. The binding site of Sirolimus on human serum albumin (HSA) was also determined. Methods: Six different concentrations of Sirolimus were separately exposed to HSA at pH 7.4 and 37°C. Ultrafiltration method was used for separating free drug; then free drug concentrations were measured by HPLC. Finally, Sirolimus protein binding parameters was calculated using Scatchard plots. The same processes were conducted in the presence of NSAIDs at lower concentration of albumin and different pH conditions. To characterize the binding site of Sirolimus on albumin, the free concentration of warfarin sodium and Diazepam, site I and II specific probes, bound to albumin were measured upon the addition of increasing Sirolimus concentrations. Results: Based on the obtained results presence of Diclofenac, Piroxicam and Naproxen, could significantly decrease the percentage of Sirolimus protein binding. The Binding reduction was the most in the presence of Piroxicam. Sirolimus-NSAIDs interactions were increased in higher pH values and also in lower albumin concentrations. Probe displacement study showed that Sirolimus may mainly bind to site I on albumin molecule. Conclusion: More considerations in co-administration of NSAIDs and Sirolimus is recommended. PMID:27478785

  16. 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.

  17. Comparison of Posttranslational Modification and the Functional Impairment of Human Serum Albumin in Commercial Preparations.

    Science.gov (United States)

    Miyamura, Shigeyuki; Imafuku, Tadashi; Anraku, Makoto; Taguchi, Kazuaki; Yamasaki, Keishi; Tominaga, Yuna; Maeda, Hitoshi; Ishima, Yu; Watanabe, Hiroshi; Otagiri, Masaki; Maruyama, Toru

    2016-03-01

    On account of its long circulating half-life, human serum albumin (HSA) is susceptible to posttranslational modifications that can alter its functions. Here, we comprehensively compared the degree of posttranslational modifications with the functional impairment of HSA derived from 5 different commercially available albumin preparations and clarified their relationships. We used electrospray ionization-time of flight mass spectrometry to evaluate the degree of posttranslational modification of the entire HSA molecule that was associated with disease development and found that the fraction of Cys34-cysteinylated HSA (Cys-Cys34-HSA), a major form of oxidative modification, varied substantially among the albumin preparations. Meanwhile, no remarkable difference was found in the degree of glycated or N-terminal truncated HSA among the preparations tested. The nonosmotic pressure maintenance functions of HSA, such as its antioxidative and ligand-binding activities significantly differed among the preparations. Interestingly, the alternations of these functions showed a significantly negative correlation only with the Cys-Cys34-HSA fraction. These findings suggest that the Cys-Cys34-HSA fraction, as estimated by electrospray ionization-time of flight mass spectrometry can be used as a predictive marker for the functional impairment of albumin preparations and that it would be preferable to use albumin preparations with higher contents of functionally effective albumin that correspond to a lower degree of cysteinylation of Cys34 in clinical practice.

  18. Behavior of human serum albumin on strong cation exchange resins: I. experimental analysis.

    Science.gov (United States)

    Voitl, Agnes; Butté, Alessandro; Morbidelli, Massimo

    2010-08-20

    Experiments with human serum albumin on the strong cation exchange resin Fractogel EMD SE Hicap (M) were carried out. Even though human serum albumin was used at high purity, two peaks in gradient elution experiments occurred. The obtained data can be explained by considering that human serum albumin binds to Fractogel EMD SE Hicap (M) in two different binding conformations: the protein adsorbs instantaneously in the first conformation and then changes into the second one with a kinetic limitation. The two-peak behavior of human serum albumin was analyzed in detail, especially at various gradient lengths, concentrations and temperatures. Breakthrough curves were performed at four modifier concentrations and three velocities. The characteristic adsorption behavior, found for gradient experiments, was confirmed by the breakthrough curves. The two-peak elution pattern of human serum albumin was also found for other strong cation exchange resins, but not for weak cation exchange resins. It is concluded that the described behavior is peculiar for the interaction of human serum albumin with the strong cation exchange ligand of the resin.

  19. Albumin resuscitation protects against traumatic/hemorrhagic shock-induced lung apoptosis in rats

    Institute of Scientific and Technical Information of China (English)

    Yun ZHANG; Zhong-yan LIANG; Shao-yang ZHANG; Fang-fang HUANG; Wei WU; Yuan GAO; Zuo-bing CHEN

    2008-01-01

    Objective: To determine the effects of albumin administration on lung injury and apoptosis in traumatic/hemorrhagic shock (T/HS) rats. Methods: Studies were performed on an in vivo model of spontaneously breathing rats with induced T/HS; the rats were subjected to femur fracture, ischemia for 30 min, and reperfusion for 20 rain with Ringer's lactate solution (RS) or 5% (w/v) albumin (ALB), and the left lower lobes of the lungs were resected. Results: Albumin administered during reperfusion markedly attenuated injury of the lung and decreased the concentration of lactic acid and the number of in situ TdT-mediated dUTP nick-end labelling (TUNEL)-positive cells. Moreover, immunohistochemistry performed 24 h after reperfusion revealed increases in the level of nuclear factor κB (NF-κB), and phosphorylated p38 mitogen-activated protein kinase (MAPK) in the albumin-untreated group was down-regulated by albumin treatment when compared with the sham rats. Conclusion: Resuscitation with albumin attenuates tissue injury and inhibits T/HS-induced apoptosis in the lung via the p38 MAPK signal transduction pathway that functions to stimulate the activation of NF-κB.

  20. pH and redox sensitive albumin hydrogel: A self-derived biomaterial.

    Science.gov (United States)

    Raja, S Thirupathi Kumara; Thiruselvi, T; Mandal, Asit Baran; Gnanamani, A

    2015-11-03

    Serum albumin can be transformed to a stimuli (pH and redox) responsive hydrogel using the reduction process followed by oxidative refolding. The preparation of albumin hydrogel involves a range of concentrations (75, 150, 300, 450, 600 and 750 μM) and pH (2.0-10.0) values and the gelation begins at a concentration of 150 μM and 4.5-8.0 pH value. The hydrogel shows maximum swelling at alkali pH (pH > 9.0). The increase in albumin concentration increases hydrogel stability, rheological property, compressive strength, proteolytic resistance and rate of in vivo biodegradation. Based on the observed physical and biological properties of albumin hydrogel, 450 μM was determined to be an optimum concentration for further experiments. In addition, the hemo- and cytocompatibility analyses revealed the biocompatibility nature of albumin hydrogel. The experiments on in vitro drug (Tetracycline) delivery were carried out under non reducing and reducing conditions that resulted in the sustained and fast release of the drug, respectively. The methodology used in the preparation of albumin hydrogel may lead to the development of autogenic tissue constructs. In addition, the methodology can have various applications in tissue engineering and drug delivery.

  1. Optimization of a colorimetric assay for glycosylated human serum albumin

    Energy Technology Data Exchange (ETDEWEB)

    Bohney, J.P.; Feldhoff, R.C.

    1986-05-01

    The thiobarbituric acid (TBA) assay has been used for several years to quantitate the amount of glucose which has been non-enzymatically linked to hemoglobin and other proteins. The ketoamine-protein adduct is converted to 5-hydroxymethylfurfural (HMF) by mild hydrolysis with oxalic acid. Reaction of HMF with TBA yields a colored product which has an absorbance maximum at 443 nm. Several modifications of the original procedure has been published, but none permit the unambiguous quantitation of glycosylated human serum albumin (glc-HSA). Problems relate to reagent preparation and stability, the time and temperature of hydrolysis, the choice of standards, and background color corrections. The authors have found that maximum color yield occurs after hydrolysis in an autoclave for 2 h. This increases the sensitivity 3-fold and cuts the assay time in half relative to hydrolysis for 4.5 h at 100/sup 0/C. A NaBH/sub 4/ reduction of a parallel protein sample must be performed to correct for variable background color associated with different sample sources and amounts. HMF can be used as a standard, however, corrections must be made for HMF degradation. Fructose is a better standard, but HMF formation from fructose is faster than formation from glc-HSA. This may result in an underestimate of percent glycosylation. The best standard appears to be glc-HSA prepared with (/sup 3/H)glucose. It appears that with proper controls and standards the TBA assay can be used to determine actual rather than relative percent glycosylation.

  2. Effect of albumin on brushite transformation to hydroxyapatite.

    Science.gov (United States)

    Xie, J; Riley, C; Chittur, K

    2001-12-05

    Brushite (CaHPO(4) x 2H(2)O) is a precursor to hydroxyapatite [HA, Ca(5)(PO(4))(3)OH]. It has been shown that a modified form of brushite, with potassium substituting for calcium at specific sites, demonstrated accelerated transformation to HA when exposed to nonproteinaceous Hanks' balanced aqueous salt solutions (HBSS). The biocompatibility of a transforming material is related to cellular response to the process, which is initiated by protein adsorption. The effect of adsorbed protein on the kinetics and chemistry of brushite transformation to HA, when exposed to HBSS containing bovine serum albumin (BSA), was examined using Fourier transform IR spectroscopy, X-ray diffraction, and energy dispersive spectrometry techniques. The effect of solution pH was also studied. Results show that, in the presence of a protein-free environment, transformation is faster in buffered medium than in nonbuffered medium. Moreover, curve fitting and second derivatives of the IR spectra show that some bands shift depending on whether the brushite transforms in a buffered or nonbuffered medium. Therefore, variation in pH affects both transformation rate and the associated chemistry. The presence of BSA in either buffered or nonbuffered medium retards the transformation in comparison to the corresponding BSA-free medium. The extent of this retardation increases with the increase in bulk concentration of BSA but does not alter the transformation chemistry. This suggests the retardation on the transformation rate is due to BSA adsorption coverage on the calcium phosphate ceramic. This may be due to the shielding of Ca(2+) and PO(4)(-3) sites, preventing their interaction with the HBSS.

  3. Effect of bovine serum albumin (BSA) on enzymatic cellulose hydrolysis.

    Science.gov (United States)

    Wang, Hui; Mochidzuki, Kazuhiro; Kobayashi, Shinichi; Hiraide, Hatsue; Wang, Xiaofen; Cui, Zongjun

    2013-06-01

    Bovine serum albumin (BSA) was added to filter paper during the hydrolysis of cellulase. Adding BSA before the addition of the cellulase enhances enzyme activity in the solution, thereby increasing the conversion rate of cellulose. After 48 h of BSA treatment, the BSA adsorption quantities are 3.3, 4.6, 7.8, 17.2, and 28.3 mg/g substrate, each with different initial BSA concentration treatments at 50 °C; in addition, more cellulase was adsorbed onto the filter paper at 50 °C compared with 35 °C. After 48 h of hydrolysis, the free-enzyme activity could not be measured without the BSA treatment, whereas the remaining activity of the filter paper activity was approximately 41 % when treated with 1.0 mg/mL BSA. Even after 96 h of hydrolysis, 25 % still remained. Meanwhile, after 48 h of incubation without substrate, the remaining enzyme activities were increased 20.7 % (from 43.7 to 52.7 %) and 94.8 % (from 23.3 to 45.5 %) at 35 and 50 °C, respectively. Moreover, the effect of the BSA was more obvious at 35 °C compared with 50 °C. When using 15 filter paper cellulase units per gram substrate cellulase loading at 50 °C, the cellulose conversion was increased from 75 % (without BSA treatment) to ≥90 % when using BSA dosages between 0.1 and 1.5 mg/mL. Overall, these results suggest that there are promising strategies for BSA treatment in the reduction of enzyme requirements during the hydrolysis of cellulose.

  4. Structural basis of transport of lysophospholipids by human serum albumin

    Energy Technology Data Exchange (ETDEWEB)

    Guo, Shihui; Shi, Xiaoli; Yang, Feng; Chen, Liqing; Meehan, Edward J.; Bian, Chuanbing; Huang, Mingdong; (UAH); (Chinese Aca. Sci.)

    2010-10-08

    Lysophospholipids play important roles in cellular signal transduction and are implicated in many biological processes, including tumorigenesis, angiogenesis, immunity, atherosclerosis, arteriosclerosis, cancer and neuronal survival. The intracellular transport of lysophospholipids is through FA (fatty acid)-binding protein. Lysophospholipids are also found in the extracellular space. However, the transport mechanism of lysophospholipids in the extracellular space is unknown. HSA (human serum albumin) is the most abundant carrier protein in blood plasma and plays an important role in determining the absorption, distribution, metabolism and excretion of drugs. In the present study, LPE (lysophosphatidylethanolamine) was used as the ligand to analyse the interaction of lysophospholipids with HSA by fluorescence quenching and crystallography. Fluorescence measurement showed that LPE binds to HSA with a K{sub d} (dissociation constant) of 5.6 {micro}M. The presence of FA (myristate) decreases this binding affinity (K{sub d} of 12.9 {micro}M). Moreover, we determined the crystal structure of HSA in complex with both myristate and LPE and showed that LPE binds at Sudlow site I located in subdomain IIA. LPE occupies two of the three subsites in Sudlow site I, with the LPE acyl chain occupying the hydrophobic bottom of Sudlow site I and the polar head group located at Sudlow site I entrance region pointing to the solvent. This orientation of LPE in HSA suggests that HSA is capable of accommodating other lysophospholipids and phospholipids. The study provides structural information on HSA-lysophospholipid interaction and may facilitate our understanding of the transport and distribution of lysophospholipids.

  5. Serum Glycated Albumin to Guide the Diagnosis of Diabetes Mellitus.

    Science.gov (United States)

    Wu, Wan-Chen; Ma, Wen-Ya; Wei, Jung-Nan; Yu, Tse-Ya; Lin, Mao-Shin; Shih, Shyang-Rong; Hua, Cyue-Huei; Liao, Ying-Jhu; Chuang, Lee-Ming; Li, Hung-Yuan

    2016-01-01

    In the diagnosis of diabetes mellitus, hemoglobin A1c (HbA1c) is sometimes measured to determine the need of an oral glucose tolerance test (OGTT). However, HbA1c does not accurately reflect glycemic status in certain conditions. This study was performed to test the possibility that measurement of serum glycated albumin (GA) better assesses the need for OGTT. From 2006 to 2012, 1559 subjects not known to have diabetes or to use anti-diabetic medications were enrolled. Serum GA was measured, and a 75-g OGTT was then performed to diagnose diabetes. Serum GA correlated significantly to age (r = 0.27, pdiet (p = 0.8). Using serum GA at 15% for diagnosis of diabetes, the sensitivity, specificity, and area under the receiver-operating characteristic curve were 74%, 85%, and 0.86, respectively. Applying a fasting plasma glucose (FPG) value of diabetes and of ≥ 126 mg/dL to diagnose diabetes, 14.4% of the study population require an OGTT (OGTT%) with a sensitivity of 78.8% and a specificity of 100%. When serum GA value of 14% and 17% were used to exclude and diagnose diabetes, respectively, the sensitivity improved to 83.3%, with a slightly decrease in specificity (98.2%), but a significant increase in OGTT% (35%). Using combined FPG and serum GA cutoff values (FPG diabetes and FPG ≥ 126 mg/dL or serum GA ≥ 17% to diagnose diabetes), the OGTT% was reduced to 22.5% and the sensitivity increased to 85.6% with no change in specificity (98.2%). In the diagnosis of diabetes, serum GA measurements can be used to determine the need of an OGTT.

  6. Human serum albumin complexes with chlorophyll and chlorophyllin.

    Science.gov (United States)

    Ouameur, A Ahmed; Marty, R; Tajmir-Riahi, H A

    2005-02-15

    Porphyrins and their metal derivatives are strong protein binders. Some of these compounds have been used for radiation sensitization therapy of cancer and are targeted to interact with cellular DNA and protein. The presence of several high-affinity binding sites on human serum albumin (HSA) makes it possible target for many organic and inorganic molecules. Chlorophyll a and chlorophyllin (a food-grade derivative of chlorophyll), the ubiquitous green plant pigment widely consumed by humans, are potent inhibitors of experimental carcinogenesis and interact with protein and DNA in many ways. This study was designed to examine the interaction of HSA with chlorophyll (Chl) and chlorophyllin (Chln) in aqueous solution at physiological conditions. Fourier transform infrared, UV-visible, and CD spectroscopic methods were used to determine the pigment binding mode, the binding constant, and the effects of porphyrin complexation on protein secondary structure. Spectroscopic results showed that chlorophyll and chlorophyllin are located along the polypeptide chains with no specific interaction. Stronger protein association was observed for Chl than for Chln, with overall binding constants of K(Chl) = 2.9 x 10(4)M(-1) and K(Chln) = 7.0 x 10(3)M(-1). The protein conformation was altered (infrared data) with reduction of alpha-helix from 55% (free HSA) to 41-40% and increase of beta-structure from 22% (free HSA) to 29-35% in the pigment-protein complexes. Using the CDSSTR program (CD data) also showed major reduction of alpha-helix from 66% (free HSA) to 58 and 55% upon complexation with Chl and Chln, respectively.

  7. Interactions between imazethapyr and bovine serum albumin: Spectrofluorimetric study

    Energy Technology Data Exchange (ETDEWEB)

    Pacheco, Maria E. [Division Quimica Analitica, Departamento de Quimica, Facultad de Ciencias Exactas, Universidad Nacional de La Plata, La Plata, Buenos Aires (Argentina); Bruzzone, Liliana, E-mail: bruzzone@quimica.unlp.edu.ar [Division Quimica Analitica, Departamento de Quimica, Facultad de Ciencias Exactas, Universidad Nacional de La Plata, La Plata, Buenos Aires (Argentina)

    2012-10-15

    The interaction between imazethapyr (IMA) and bovine serum albumin (BSA) was investigated by fluorescence spectroscopy. The Stern-Volmer quenching constant (K{sub SV}) at three temperatures was evaluated in order to determine the quenching mechanism. The dependence of fluorescence quenching on viscosity was also evaluated for this purpose. The results showed that IMA quenches the fluorescence intensity of BSA through a static quenching process. The values of the binding constant for the formed BSA-IMA complex and the number of binding sites were found to be 1.51 Multiplication-Sign 10{sup 5} M{sup -1} and 0.77, respectively, at room temperature. Based on the calculated thermodynamic parameters, the forces that dominate the binding process are hydrogen bonds and van der Waals forces, and the binding process is spontaneous and exothermic. The quenching of protein fluorescence by iodide ion was used to probe the accessibility of tryptophan residues in BSA and the change in accessibility induced by the presence of IMA. According to the obtained results, the BSA-IMA complex is formed in the site where the Trp-134 is located, causing it to become less exposed to the solvent. - Highlights: Black-Right-Pointing-Pointer Fluorescence spectroscopy helps to understand protein binding mechanisms. Black-Right-Pointing-Pointer Quenching measurements reveal the nature of the binding process involved. Black-Right-Pointing-Pointer Iodine ion can be used to study the change in accessibility of tryptophan residues. Black-Right-Pointing-Pointer Thermodynamic parameters for the binding reaction confirm binding modes.

  8. Glycated albumin in diabetic patients with chronic kidney disease.

    Science.gov (United States)

    Zheng, Cai-Mei; Ma, Wen-Ya; Wu, Chia-Chao; Lu, Kuo-Cheng

    2012-10-09

    Chronic hyperglycemia results in a non-enzymatic glycation of proteins, and produces Amadori products, such as glycated albumin (GA), glycosylated hemoglobin (HbA1c), and fructosamine. In current clinical practice, long-term glycemic control is assessed by quarterly measurements of HbA1c. Since the degree of hemoglobin glycosylation depends not only on the level of glycemic control, but also on the lifespan of red blood cells, patients with hemoglobin disorders or anemia of any cause may have erroneous HbA1c levels, and consequently receive insufficient treatment. Patients with chronic kidney disease (CKD) often suffer from various types of anemia, and consequently, they are frequently treated with iron and/or erythropoietin therapy or frequent blood transfusion. Thus, serum GA is a potentially useful glycemic index in diabetic patients with CKD, since it is not influenced by anemia and associated treatments. GA may also reflect the status of blood glucose more rapidly (2-3 weeks) than HbA1c (2-3 months), and is beneficial in those with wide variations in blood glucose or at higher risk for hypoglycemia. If clinical investigations support its utility, it may be applicable as a screening tool for all patients with diabetes during routine health examinations. Serum GA levels are also associated with AGE-related fluorescence and the number of glycation sites, and it may influence the structural and functional changes inalbumin. Since end-stage renal disease is an extreme microvascular complication of diabetic nephropathy, CKD patients with diabetes should be carefully managed to prevent disease progression. In this review, the clinical aspects of GA were discussed, including a comparison of GA with other glycated proteins, the utility and limitations of GA as a glycemic index, its influence on the therapeutic effects of hypoglycemic agents, its correlations with vascular complications, and its potential role in pathogenesis, specifically in diabetic patients with CKD.

  9. Overestimation of canine albumin concentration with the bromcresol green method in heparinized plasma samples.

    Science.gov (United States)

    Stokol, Tracy; Tarrant, Jacqueline M.; Scarlett, Janet M.

    2001-01-01

    Albumin concentrations are routinely measured in dogs with bromcresol green (BCG)-binding assays on automated chemistry analyzers. Several variables affect this assay, including the length of reaction time, sample type, and lack of specificity of BCG for albumin. We observed that albumin concentrations measured with BCG appeared higher in heparinized plasma samples in sick dogs. The objective of this study was to determine the effect of anticoagulant and assay procedure on BCG albumin concentrations in clinically ill dogs. We hypothesized that albumin concentrations would be overestimated in heparinized plasma compared with serum because of the combination of heparin and fibrinogen. Furthermore, we hypothesized that the overestimation would be influenced by assay parameters. Blood was collected from 32 clinically ill dogs into tubes containing heparin, citrate, or no anticoagulant. Citrate was chosen to assess the effect of fibrinogen in the absence of heparin. Albumin concentration was measured in all 3 sample types from each dog using 2 different BCG procedures on an automated chemistry analyzer. The BCG procedures (standard and modified) differed in the wavelengths used for absorbance readings (standard, 600/700; modified, 570/505) and the time point at which absorbance was measured (standard, 100 seconds; modified, 40 seconds). In addition, the modified method incorporated a sample blank. Globulin fractions, fibrinogen concentration, and indices of lipemia, hemolysis, and icterus were evaluated for their contribution to the overestimation of albumin concentration in heparinized plasma compared with serum samples. Albumin concentrations were significantly higher (P

  10. Serum albumin levels and their correlates among individuals with motor disorders at five institutions in Japan

    Science.gov (United States)

    Nakayama, Takeo; Kanaya, Yuki; Tanaka, Yuki

    2017-01-01

    BACKGROUND/OBJECTIVES The level of serum albumin is an index of nourishment care and management. However, the distribution and correlates of serum albumin levels among individuals with motor disorders have not been reported until now. Therefore, we examined the distribution and correlates of serum albumin levels among individuals with motor disorders. SUBJECTS/METHODS A cross-sectional study on 249 individuals with motor disabilities (144 men, mean age: 51.4 years; 105 women, mean age: 51.4 years) was conducted at five institutions in Ibaraki Prefecture, Japan in 2008. The results were compared with data from the National Health and Nutrition Survey. RESULTS The mean serum albumin levels were 4.0 ± 0.4 g/dL for men and 3.8 ± 0.5 g/dL for women. Overall, 17 (11.8%) men and 25 (23.8%) women had hypoalbuminemia (serum albumin level ≤ 3.5 g/dL); these proportions were greater than those among healthy Japanese adults (≤ 1%). Low serum albumin level was related with female sex, older age, low calf circumference, low relative daily energy intake, low hemoglobin (Hb), low blood platelet count, low high-density lipoprotein cholesterol (HDL-C), low HbA1c, and high C-reactive protein (CRP) levels. The strongest correlates, based on standardized betas, were Hb (0.321), CRP (-0.279), and HDL-C (0.279) levels. CONCLUSIONS These results indicate that the prevalence of hypoalbuminemia is higher in individuals with motor disabilities than in healthy individuals and that inflammation is a strong negative correlate of serum albumin levels. Therefore, inflammation should be examined for the assessment of hypoalbuminemia among institutionalized individuals with motor disabilities.

  11. Enhancement of albumin expression in bone tissues with healing rat fractures.

    Science.gov (United States)

    Yamaguchi, Masayoshi; Igarashi, Aki; Misawa, Hiroyuki; Tsurusaki, Yoshinori

    2003-05-15

    The characterization of 66 kDa protein molecule, a major protein component which is produced from femoral-diaphyseal tissues with fracture healing (Igarashi and Yamaguchi [2002] Int. J. Mol. Med. 9:503-508), was investigated. Weaning rats were killed at 7 and 14 days after femoral fracture. When the femoral-diaphyseal tissues with fracture healing were cultured for 48 h in a serum-free medium, many proteins in the bone tissues were released into the medium. Analysis with sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed that a protein molecule of approximately 66 kDa was markedly increased in culture medium from bone tissues with fracture healing. N-terminal sequencing of 66 kDa protein indicated that its N-terminus was identical to that of rat albumin. Western blot analysis of medium 66 kDa protein showed expression of albumin. This expression was significantly enhanced by fracture healing. The expression of albumin was seen in the diaphyseal (cortical bone) and metaphyseal (trabecular bone) tissues of rat femur. When the femoral-diaphyseal tissues obtained at 7 days after femoral fracture were cultured in a serum-free medium containing either vehicle, parathyroid hormone (1-34) (10(-7) M), insulin-like growth factor-I (10(-8) M) or zinc acexamate (10(-4) M), medium albumin was significantly increased in the presence of those bone-stimulating factors. The addition of albumin (0.5 or 1.0 mg/ml of medium) caused a significant increase in calcium and deoxyribonucleic acid contents in the femoral-diaphyseal and -metaphyseal tissues obtained from normal rats in vitro. The present study demonstrates that fracture healing induces a remarkable production of albumin which is a major protein component produced from femoral-diaphyseal tissues of rats, and that albumin has an anabolic effect on bone components.

  12. Urinary albumin excretion in hospitalized patients with acute myocardial infarction. Prevalence of microalbuminuria and correlation to left ventricle wall thickness

    DEFF Research Database (Denmark)

    Taskiran, M; Feldt-Rasmussen, B; Jensen, G B;

    1998-01-01

    Microalbuminuria, a subclinical rise in the urinary albumin excretion, is a risk indicator of atherosclerotic cardiovascular disease. The aim of this study was to measure the urinary albumin excretion in patients with acute myocardial infarction, and to correlate this with known atherosclerotic...... risk factors. One-hundred-and-twenty-six patients and 56 healthy controls matched for age and sex were studied. The albumin/creatinine concentration ratio in morning urine specimens was calculated as an index of the albumin excretion. Microalbuminuria was defined as a urinary albumin....../creatinine concentration ratio above 1 mg/mmol. Urinary albumin excretion (0.88 [95% confidence interval 0.69-1.11] versus 0.51 [0.40-0.63] mg/mmol; p = 0.001) and frequency of microalbuminuria (33 [95% confidence interval 25-41] versus 16 [9-23]%; p = 0.03) were higher in patients than controls. This difference...

  13. Comparison of Enzymatic and Ultrasonic Extraction of Albumin from Defatted Pumpkin (Cucurbita pepo)
Seed Powder.

    Science.gov (United States)

    Tu, Gia Loi; Bui, Thi Hoang Nga; Tran, Thi Thu Tra; Ton, Nu Minh Nguyet; Man Le, Van Viet

    2015-12-01

    In this study, ultrasound- and enzyme-assisted extractions of albumin (water-soluble protein group) from defatted pumpkin (Cucurbita pepo) seed powder were compared. Both advanced extraction techniques strongly increased the albumin yield in comparison with conventional extraction. The extraction rate was two times faster in the ultrasonic extraction than in the enzymatic extraction. However, the maximum albumin yield was 16% higher when using enzymatic extraction. Functional properties of the pumpkin seed albumin concentrates obtained using the enzymatic, ultrasonic and conventional methods were then evaluated. Use of hydrolase for degradation of cell wall of the plant material did not change the functional properties of the albumin concentrate in comparison with the conventional extraction. The ultrasonic extraction enhanced water-holding, oil-holding and emulsifying capacities of the pumpkin seed albumin concentrate, but slightly reduced the foaming capacity, and emulsion and foam stability.

  14. Serum Albumin and C-Reactive Protein/Albumin Ratio Are Useful Biomarkers of Crohn's Disease Activity.

    Science.gov (United States)

    Qin, Guangming; Tu, Jiangfeng; Liu, Lingang; Luo, Laisheng; Wu, Jiaqi; Tao, Lisha; Zhang, Chenjing; Geng, Xiaoge; Chen, Xiaojun; Ai, Xinbo; Shen, Bo; Pan, Wensheng

    2016-11-16

    BACKGROUND Serum albumin (ALB) may be low during acute inflammation, but it is also affected by nutritional status. Therefore, we hypothesized that ALB and the C-reactive protein/ALB ratio (CRP/ALB) may be associated with disease activity in patients with Crohn's disease (CD). MATERIAL AND METHODS Altogether, 100 patients with CD and 100 age- and sex-matched healthy volunteers were retrospectively enrolled in the current study. The patients with CD were subdivided into patients with active disease (Crohn's Disease Activity Index >150) and those in remission. ALB levels, CRP levels, and lipid profiles were measured. RESULTS ALB and CRP levels and the CRP/ALB ratio were the most useful for differentiating between active and nonactive CD. ALB levels (r=-0.50, Pratio (r=0.42, Panalysis indicated that the area under the curve (AUC) representing ALB (0.79) was higher than the AUC representing CRP (0.73) or CRP/ALB ratio (0.75; P>0.05). The AUCs corresponding to ALB level, CRP level, and CRP/ALB ratio were more prominent in males versus females (Pratio (0.69) had sensitivities of 67.7%, 72.6%, and 59.7%, and specificities of 73.7%, 78.9%, and 81.6%, respectively, for CD activity. CONCLUSIONS In the present retrospective study, we found that ALB level and CRP/ALB ratio were useful biomarkers for identifying CD activity, especially in males. These results suggest that, in addition to inflammation, assessment of patient nutritional status could also aid in identifying CD activity.

  15. Human albumin prevents 6-hydroxydopamine-induced loss of tyrosine hydroxylase in in vitro and in vivo.

    Directory of Open Access Journals (Sweden)

    Li-Juan Zhang

    Full Text Available Human albumin has recently been demonstrated to protect brain neurons from injury in rat ischemic brain. However, there is no information available about whether human albumin can prevent loss of tyrosine hydroxylase (TH expression of dopaminergic (DA neurons induced by 6-hydroxydopamine (6-OHDA toxicity that is most commonly used to create a rat model of Parkinson's disease (PD. In the present study, two microliters of 1.25% human albumin were stereotaxically injected into the right striatum of rats one day before or 7 days after the 6-OHDA lesion in the same side. D-Amphetamine-induced rotational asymmetry was measured 7 days, 3 and 10 weeks after 6-OHDA lesion. We observed that intrastriatal administration of human albumin significantly reduced the degree of rotational asymmetry. The number of TH-immunoreactive neurons present in the substantia nigra was greater in 6-OHDA lesioned rats following human albumin-treatment than non-human albumin treatment. TH-immunoreactivity in the 6-OHDA-lesioned striatum was also significantly increased in the human albumin-treated rats. To examine the mechanisms underlying the effects of human albumin, we challenged PC12 cells with 6-OHDA as an in vitro model of PD. Incubation with human albumin prevented 6-OHDA-induced reduction of cell viability in PC12 cell cultures, as measured by MTT assay. Furthermore, human albumin reduced 6-OHDA-induced formation of reactive oxygen species (ROS and apoptosis in cultured PC12 cells, as assessed by flow cytometry. Western blot analysis showed that human albumin inhibited 6-OHDA-induced activation of JNK, c-Jun, ERK, and p38 mitogen-activated protein kinases (MAPK signaling in PC12 cultures challenged with 6-OHDA. Human albumin may protect against 6-OHDA toxicity by influencing MAPK pathway followed by anti-ROS formation and anti-apoptosis.

  16. Proteomic analysis of albumin and globulin fractions of pea (Pisum sativum L. seeds

    Directory of Open Access Journals (Sweden)

    Jerzy Dziuba

    2014-06-01

    Full Text Available Background. Proteomic analysis is emerging as a highly useful tool in food research, including studies of food allergies. Two-dimensional gel electrophoresis involving isoelectric focusing and sodium dodecyl sulfate polyacrylamide gel electrophoresis is the most effective method of separating hundreds or even thousands of proteins. In this study, albumin and globulin tractions of pea seeds cv. Ramrod were subjected to proteomic analysis. Selected potentially alergenic proteins were identified based on their molecular weights and isoelectric points. Material and methods. Pea seeds (Pisum sativum L. cv. Ramrod harvested over a period of two years (Plant Breeding Station in Piaski-Szelejewo were used in the experiment. The isolated albumins, globulins and legumin and vicilin fractions of globulins were separated by two-dimensional gel electrophoresis. Proteomic images were analysed in the ImageMaster 2D Platinum program with the use of algorithms from the Melanie application. The relative content, isoelectric points and molecular weights were computed for all identified proteins. Electrophoregrams were analysed by matching spot positions from three independent replications. Results. The proteomes of albumins, globulins and legumin and vicilin fractions of globulins produced up to several hundred spots (proteins. Spots most characteristic of a given fraction were identified by computer analysis and spot matching. The albumin proteome accumulated spots of relatively high intensity over a broad range of pi values of -4.2-8.1 in 3 molecular weight (MW ranges: I - high molecular-weight albumins with MW of -50-110 kDa, II - average molecular-weight albumins with MW of -20-35 kDa, and III - low molecular-weight albumins with MW of -13-17 kDa. 2D gel electrophoregrams revealed the presence of 81 characteristic spots, including 24 characteristic of legumin and 14 - of vicilin. Conclusions. Two-dimensional gel electrophoresis proved to be a useful tool for

  17. Recombinant fusion protein of albumin-retinol binding protein inactivates stellate cells

    Energy Technology Data Exchange (ETDEWEB)

    Choi, Soyoung; Park, Sangeun; Kim, Suhyun [Laboratory of Cellular Oncology, Korea University Graduate School of Medicine, Ansan, Gyeonggi do 425-707 (Korea, Republic of); Lim, Chaeseung [Department of Laboratory Medicine, Korea University Guro Hospital, Seoul 152-703 (Korea, Republic of); Kim, Jungho [Department of Life Science, Sogang University, Seoul 121-742 (Korea, Republic of); Cha, Dae Ryong [Department of Internal Medicine, Korea University Ansan Hospital, Ansan, Gyeonggi do 425-020 (Korea, Republic of); Oh, Junseo, E-mail: ohjs@korea.ac.kr [Laboratory of Cellular Oncology, Korea University Graduate School of Medicine, Ansan, Gyeonggi do 425-707 (Korea, Republic of)

    2012-02-03

    Highlights: Black-Right-Pointing-Pointer We designed novel recombinant albumin-RBP fusion proteins. Black-Right-Pointing-Pointer Expression of fusion proteins inactivates pancreatic stellate cells (PSCs). Black-Right-Pointing-Pointer Fusion proteins are successfully internalized into and inactivate PSCs. Black-Right-Pointing-Pointer RBP moiety mediates cell specific uptake of fusion protein. -- Abstract: Quiescent pancreatic- (PSCs) and hepatic- (HSCs) stellate cells store vitamin A (retinol) in lipid droplets via retinol binding protein (RBP) receptor and, when activated by profibrogenic stimuli, they transform into myofibroblast-like cells which play a key role in the fibrogenesis. Despite extensive investigations, there is, however, currently no appropriate therapy available for tissue fibrosis. We previously showed that the expression of albumin, composed of three homologous domains (I-III), inhibits stellate cell activation, which requires its high-affinity fatty acid-binding sites asymmetrically distributed in domain I and III. To attain stellate cell-specific uptake, albumin (domain I/III) was coupled to RBP; RBP-albumin{sup domain} {sup III} (R-III) and albumin{sup domain} {sup I}-RBP-albumin{sup III} (I-R-III). To assess the biological activity of fusion proteins, cultured PSCs were used. Like wild type albumin, expression of R-III or I-R-III in PSCs after passage 2 (activated PSCs) induced phenotypic reversal from activated to fat-storing cells. On the other hand, R-III and I-R-III, but not albumin, secreted from transfected 293 cells were successfully internalized into and inactivated PSCs. FPLC-purified R-III was found to be internalized into PSCs via caveolae-mediated endocytosis, and its efficient cellular uptake was also observed in HSCs and podocytes among several cell lines tested. Moreover, tissue distribution of intravenously injected R-III was closely similar to that of RBP. Therefore, our data suggest that albumin-RBP fusion protein comprises

  18. Association between serum albumin and glycated hemoglobin in Asian Indian subjects

    Directory of Open Access Journals (Sweden)

    Shalbha Tiwari

    2015-01-01

    Full Text Available Background: Protein glycation plays a signifi cant role in diabetic complications. Glycated hemoglobin (HbA1c is a known predictor of diabetes and its complications. Albumin, found to be profoundly glycated in diabetes, and its level could regulate plasma protein as well as hemoglobin glycation. Aim: We aimed to evaluate the association between variations in albumin level with HbA1c in the Asian Indian population. Materials and Methods: We screened data of 929 subjects who have had a simultaneous measurement of fasting plasma glucose (FPG, HbA1c and albumin levels via the same blood collection. Data were analyzed by SPSS for 610 subjects who met the study criteria. Results: There was a signifi cant negative correlation between HbA1c and albumin concentration (r = −0.284; P < 0.001. Univariate analysis showed the statistically signifi cant decrease of average HbA1c but not for fasting plasma glucose (FPG across increasing tertiles of albumin. Stepwise multiple regression model showed a signifi cant correlation between HbA1c and serum albumin (P < 0.05, FPG (P < 0.001, hemoglobin (Hb (P < 0.001 and serum globulin (P < 0.05. FPG was the strongest predictor (63.4% of variation of HbA1c. The albumin concentration (r = −0.114 accounted for 0.3% (P < 0.05 of the total variance in HbA1c independent of age, body mass index, FPG, Hb, creatinine, total protein and globulin. It was also observed that HbA1c decreases with increasing albumin concentration in those having FPG between 100 to <126 mg/dl. Conclusion: Serum albumin negatively correlates with HbA1c in Asian Indians independent of other variables. This study suggests that predicting diabetes and its complication based on the HbA1c needs to be further investigated in Indian subjects.

  19. Complexation of serum albumins and triton X-100: Quenching of tryptophan fluorescence and analysis of the rotational diffusion of complexes

    Science.gov (United States)

    Vlasova, I. M.; Vlasov, A. A.; Saletskii, A. M.

    2016-07-01

    The polarized and nonpolarized fluorescence of bovine serum albumin and human serum albumin in Triton X-100 solutions is studied at different pH values. Analysis of the constants of fluorescence quenching for BSA and HSA after adding Triton X-100 and the hydrodynamic radii of BSA/HSA-detergent complexes show that the most effective complexation between both serum albumins and Triton X-100 occurs at pH 5.0, which lies near the isoelectric points of the proteins. Complexation between albumin and Triton X-100 affects the fluorescence of the Trp-214 residing in the hydrophobic pockets of both BSA and HSA.

  20. 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.

  1. Albumin-Folate Conjugates for Drug-targeting in Photodynamic Therapy.

    Science.gov (United States)

    Butzbach, Kathrin; Rasse-Suriani, Federico A O; Gonzalez, M Micaela; Cabrerizo, Franco M; Epe, Bernd

    2016-07-01

    Photodynamic therapy (PDT) is based on the cytotoxicity of photosensitizers in the presence of light. Increased selectivity and effectivity of the treatment is expected if a specific uptake of the photosensitizers into the target cells, often tumor cells, can be achieved. An attractive transporter for that purpose is the folic acid receptor α (FRα), which is overexpressed on the surface of many tumor cells and mediates an endocytotic uptake. Here, we describe the synthesis and photobiological characterization of polar β-carboline derivatives as photosensitizers covalently linked to folate-tagged albumin as the carrier system. The particles were taken up by KB (human carcinoma) cells within albumin-β-carbolinium conjugate proved to be phototoxic, while the corresponding albumin-β-carbolinium conjugates without FA were nontoxic, both with and without irradiation. An excess of free folate as competitor for the FRα-mediated uptake completely inhibited the photocytotoxicity. Interestingly, the albumin conjugates are devoid of photodynamic activity under cell-free conditions, as shown for DNA as a target. Thus, phototoxicity requires cellular uptake and lysosomal degradation of the conjugates. In conclusion, albumin-folate conjugates appear to be promising vehicles for a tumor cell targeted PDT.

  2. Human albumin use at hospitals in the Metropolitan Region of Rio de Janeiro, Brazil.

    Science.gov (United States)

    Matos, Guacira Corrêa de; Rozenfeld, Suely; Martins, Monica

    2010-05-01

    The study analyzes the use of human albumin in hospitals in Rio de Janeiro, Brazil, using inpatient data from the information system of Brazil's health system between 1999 and 2001. Death was the main outcome as patients died in 32% of admissions in which human albumin was used as compared with 4% of all admissions in the same period and region. The Charlson Comorbidity Index was included for risk adjustment. Human albumin was used in 10,111 in-patients more than 1 year old. 87,774 50-ml bottles of 20% human albumin were consumed at a cost of US$ 1,755. The main diagnoses were neoplasms (29.1%), diseases of the digestive system (17.5%) and circulatory system (16%). Death rate increased with age, public ownership of the hospital, clinical services (as opposed to surgical services), length of stay and use of intensive care. Death was associated with use of more than four bottles of human albumin (PR: 1.30; 99%CI: 1.23-1.37), adjusted for severity and speciality. The results are cause for concern as they may be related to poor compliance with guidelines, excess of risk to patients and unnecessary expenses for the public health system.

  3. 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.

  4. Interactions with insulin and dexamethasone in net synthesis of albumin and acute-phase proteins

    Energy Technology Data Exchange (ETDEWEB)

    Miller, L.L.

    1976-01-01

    The isolated rat liver perfused for 12 hours at pH 7.10 with a suspension of bovine erythrocytes in Krebs--Ringer bicarbonate buffer containing 3% bovine serum albumin has been used as a test system to study effects of glucagon and of dexamethasone in the presence and absence of insulin on net biosynthesis of rat serum albumin, fibrinogen, ..cap alpha../sub 1/-acid glycoprotein, ..cap alpha../sub 2/-(acute phase) globulin, and haptoglobin. Quantitative measurement of perfusate glucose, amino acid nitrogen, and urea affords a basis for determining net glucose and nitrogen balance in the perfusion system. Although the dose of dexamethasone (total 1.0 ..mu..g) used was insufficient to induce synthesis of ..cap alpha../sub 2/-acute phase globulin, net syntheses of albumin, fibrinogen, ..cap alpha../sub 1/-acid glycoprotein, and haptoglobin were increased. Glucagon given with dexamethasone depressed albumin and haptoglobin synthesis markedly, but not that of fibrinogen and ..cap alpha../sub 1/-acid glycoprotein. Glucagon with dexamethasone markedly enhanced ureogenesis and glycogenolysis and elicited an exaggerated negative nitrogen balance. The unfavorable effects of glucagon on albumin and haptoglobin synthesis and on nitrogen balance were reversed by giving insulin simultaneously. It is emphasized that insulin is essential for positive nitrogen balance.

  5. Albumin adsorption on unmodified and sulfonated polystyrene surfaces, in relation to cell-substratum adhesion.

    Science.gov (United States)

    Kowalczyńska, Hanna M; Nowak-Wyrzykowska, Małgorzata; Szczepankiewicz, Andrzej A; Dobkowski, Jacek; Dyda, Magdalena; Kamiński, Jarosław; Kołos, Robert

    2011-06-01

    Albumin is commonly applied for blocking the adsorption of other proteins and to prevent the nonspecific adhesion of cells to diverse artificial substrata. Here we address the question of how effective these albumin properties are--by investigating unmodified and sulfonated polystyrene substrata with distinctly different wettabilities. As clearly shown with (125)I-radioisotopic assays, above a concentration of 10-20 μg/mL, the efficiency of bovine serum albumin (BSA) adsorption became markedly higher on the sulfonated surface than on the unmodified one. This study was assisted with the atomic force microscopy. On the unmodified surface, BSA, adsorbed from sufficiently concentrated solutions, formed a monolayer, with occasional intrusions of multilayered patches. Conversely, the arrangement of BSA on the sulfonated surface was chaotic; the height of individual molecules was lower than on the unmodified polystyrene. Importantly, the adhesion study of LNCaP and DU145 cells indicated that both surfaces, subjected to the prior BSA adsorption, did not completely loose their cell-adhesive properties. However, the level of adhesion and the pattern of F-actin organization in adhering cells have shown that cells interacted with unmodified and sulfonated surfaces differently, depending on the arrangement of adsorbed albumin. These results suggest the presence of some bare substratum area accessible for cells after the albumin adsorption to both types of investigated surfaces.

  6. Intracellular delivery of cytochrome c by galactosylated albumin to hepatocarcinoma cells.

    Science.gov (United States)

    Yeh, Tzyy-Harn; Wu, Fe-Lin Lin; Shen, Li-Jiuan

    2014-07-01

    In some cancer cells, translocation of cytochrome c (Cyt c) from mitochondria to the cytoplasma is inhibited. This inhibition prevents cells from undergoing apoptotic cell death and can lead to uncontrolled cell growth. Increasing cytoplasmic concentration of Cyt c can induce apoptosis in cancer cells as a strategy of cancer therapy. Here we proposed a galactosylated albumin based carrier for intracellular delivery of Cyt c to hepatocarcinoma cells. Galactosylated albumin is recognized by highly expressed asialoglycoprotein receptors (ASGPR) on hepatocarcinoma cells and is further internalized into cells via receptor mediated endocytosis. Cyt c was chemically conjugated to galactosylated albumin with a reducible disulfide linker in order to release Cyt c from the carrier inside cells. We tested cellular uptake and cytotoxicity of Cyt c conjugates in ASGPR positive and negative hepatocarcinoma cells. The results showed galatosylated albumin significantly increased cellular uptake in both cell types resulting in cytotoxicity in a dose dependent manner through the induction of apoptosis. The lack of ASGPR specific uptake might be due to other carbohydrate-recognizing receptors expressed on tumor cells. In general, our work has shown that intracellular delivery of Cyt c to tumor cells can be an alternative therapeutic approach and galactosylated albumin can be a protein drug carrier for intracellular delivery.

  7. ATR-FTIR measurements of albumin and fibrinogen adsorption: Inert versus calcium phosphate ceramics.

    Science.gov (United States)

    Boix, Marcel; Eslava, Salvador; Costa Machado, Gil; Gosselin, Emmanuel; Ni, Na; Saiz, Eduardo; De Coninck, Joël

    2015-11-01

    Arthritis, bone fracture, bone tumors and other musculoskeletal diseases affect millions of people across the world. Nowadays, inert and bioactive ceramics are used as bone substitutes or for bone regeneration. Their bioactivity is very much dictated by the way proteins adsorb on their surface. In this work, we compared the adsorption of albumin and fibrinogen on inert and calcium phosphates ceramics (CaPs) using attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR) to follow in situ protein adsorption on these materials. To this effect, we developed a sol-gel technique to control the surface chemistry of an ATR-FTIR detector. Hydroxyapatite adsorbed more albumin and β-tricalcium phosphate adsorbed more fibrinogen. Biphasic calcium phosphate presented the lowest adsorption among CaP for both proteins, illustrating the effect of surface heterogeneities. Inert ceramics adsorbed a lower amount of both proteins compared with bioactive ceramics. A significant change was observed in the conformation of the adsorbed protein versus the surface chemistry. Hydroxyapatite produced a larger loss of α-helix structure on albumin and biphasic calcium phosphate reduced β-sheet percentage on fibrinogen. Inert ceramics produced large α-helix loss on albumin and presented weak interaction with fibrinogen. Zirconia did not adsorb albumin and titanium dioxide promoted huge denaturalization of fibrinogen.

  8. Glomerular endothelial surface layer acts as a barrier against albumin filtration.

    Science.gov (United States)

    Dane, Martijn J C; van den Berg, Bernard M; Avramut, M Cristina; Faas, Frank G A; van der Vlag, Johan; Rops, Angelique L W M M; Ravelli, Raimond B G; Koster, Bram J; van Zonneveld, Anton Jan; Vink, Hans; Rabelink, Ton J

    2013-05-01

    Glomerular endothelium is highly fenestrated, and its contribution to glomerular barrier function is the subject of debate. In recent years, a polysaccharide-rich endothelial surface layer (ESL) has been postulated to act as a filtration barrier for large molecules, such as albumin. To test this hypothesis, we disturbed the ESL in C57Bl/6 mice using long-term hyaluronidase infusion for 4 weeks and monitored albumin passage using immunolabeling and correlative light-electron microscopy that allows for complete and integral assessment of glomerular albumin passage. ESL ultrastructure was visualized by transmission electron microscopy using cupromeronic blue and by localization of ESL binding lectins using confocal microscopy. We demonstrate that glomerular fenestrae are filled with dense negatively charged polysaccharide structures that are largely removed in the presence of circulating hyaluronidase, leaving the polysaccharide surfaces of other glomerular cells intact. Both retention of native ferritin [corrected] in the glomerular basement membrane and systemic blood pressure were unaltered. Enzyme treatment, however, induced albumin passage across the endothelium in 90% of glomeruli, whereas this could not be observed in controls. Yet, there was no net albuminuria due to binding and uptake of filtered albumin by the podocytes and parietal epithelium. ESL structure and function completely recovered within 4 weeks on cessation of hyaluronidase infusion. Thus, the polyanionic ESL component, hyaluronan, is a key component of the glomerular endothelial protein permeability barrier.

  9. Short exposure of albumin to high concentrations of malondialdehyde does not mimic physiological conditions.

    Science.gov (United States)

    Millanta, Susanna; Furfaro, Anna Lisa; Carlier, Paolo; Tasso, Bruno; Nitti, Mariapaola; Domenicotti, Cinzia; Odetti, Patrizio; Pronzato, Maria Adelaide; Traverso, Nicola

    2013-02-01

    Malondialdehyde (MDA), a major lipid peroxidation product, spontaneously binds to, and modifies proteins. In vivo, proteins are physiologically exposed to micromolar MDA concentrations for long periods. In order to mimic this process in vitro, protein modification is often performed by short exposure to millimolar MDA concentrations, also in order to generate antigenic structures for antibody production. However, in our study, spectrophotometric and fluorimetric characteristics, electrophoretic migration, susceptibility to trypsin digestion and reactivity to antibodies indicated substantial differences between albumin incubated with millimolar MDA concentrations for a short period of time and albumin incubated with micromolar MDA concentrations for a long period of time. Therefore, our study showed that short incubation of albumin with millimolar MDA concentrations does not mimic the consequences of albumin exposure to long incubation with micromolar MDA concentrations. This casts doubts on the real possibility that antibodies, elicited with proteins modified with millimolar MDA concentrations for a short period, could detect all MDA-modified proteins in vivo. Moreover, natural antibodies against albumin, modified with micromolar MDA concentrations, have been detected in the serum of healthy blood donors, which appears to justify the existence of these kinds of modified proteins in vivo.

  10. Glycated albumin and diabetes mellitus%糖化白蛋白与糖尿病

    Institute of Scientific and Technical Information of China (English)

    艾艳琴; 邓华聪

    2010-01-01

    糖化白蛋白是葡萄糖与血浆白蛋白发生非酶糖化反应的产物,其值能反映糖尿病患者近2~3周内的平均血糖水平,是反映短期血糖控制的较好指标.同时糖化白蛋白具有促动脉粥样硬化的作用,亦是评估糖尿病合并冠心病时冠状动脉病变严重程度的一项敏感指标.现对糖化白蛋白对糖尿病的诊疗价值进行综述.%Plasma glycated albumin is the product of non-enzymatic glycation by glucose and plasma albumin. The level of glycated albumin can reflect the average blood glucose levels of diabetics in the past 2-3 weeks, and it is a better indicator of short-term glycemic control. Moreover, glycated albumin can accelerate atherosclerosis,and is also a sensitive indicator to assess the presence and severity of coronary artery disease in patients with type 2 diabetes. Here presents the diagnostic value and recent progress of plasma glycated albumin.

  11. Hubungan Kadar Albumin Serum dengan Neutrophil Gelatinase-Associated Lipocalin Urine pada Penderita Sindrom Nefrotik Anak

    Directory of Open Access Journals (Sweden)

    Deasy Nurisya

    2014-09-01

    Full Text Available Neutrophil gelatinase-associated lipocalin (NGAL is a biological marker found in kidney damage that increases in proximal tubular damage. The purpose of this study was to analyze the correlation between serum albumin and urine NGAL (uNGAL levels in children with NS at initial presentation or relapse. Subjects in this study were 1−14 year-old children with NS. An observational analytical study with cross sectional design was conducted in the Pediatric Department of Dr. Hasan Sadikin General Hospital Bandung and Bandung City Public Hospital from September 2011 to March 2012. The serum albumin level and uNGAL level were measured using bromcresol green method and enzyme-linked immunosorbent assay (ELISA, respectively. Data were analyzed using Pearson correlation test on normal distribution data. Subjects consisted of 14 boys and 10 girls. Mean serum albumin and uNGAL levels were 1.37 (SD 0.33 g/dL and 2,719.37 (SD 3,781.82 ng/mL, respectively. There was a significant correlation between decreased albumin level and elevated uNGAL level (r=−0.519, p=0.009. In conclusion, the lower the albumin level, the higher the uNGAL level. An awareness should be developed towards the possibility that hypoalbuminemia in children with NS might decrease renal function.

  12. Effect of catecholamines and insulin on plasma volume and intravascular mass of albumin in man

    DEFF Research Database (Denmark)

    Hilsted, J; Christensen, N J; Larsen, S

    1989-01-01

    1. The effect of intravenous catecholamine infusions and of intravenous insulin on plasma volume and intravascular mass of albumin was investigated in healthy males. 2. Physiological doses of adrenaline (0.5 microgram/min and 3 microgram/min) increased peripheral venous packed cell volume...... significantly; intravenous noradrenaline at 0.5 microgram/min had no effect on packed cell volume, whereas packed cell volume increased significantly at 3 micrograms of noradrenaline/min. No significant change in packed cell volume was found during saline infusion. 3. During adrenaline infusion at 6 micrograms...... in packed cell volume, plasma volume, intravascular mass of albumin and transcapillary escape rate of albumin during hypoglycaemia may be explained by the combined actions of adrenaline and insulin....

  13. New mathematical model for fluid-glucose-albumin transport in peritoneal dialysis

    CERN Document Server

    Cherniha, Roman

    2011-01-01

    A mathematical model for fluid transport in peritoneal dialysis is constructed. The model is based on a three-component nonlinear system of two-dimensional partial differential equations for fluid, glucose and albumin transport with the relevant boundary and initial conditions. Non-constant steady-state solutions of the model are studied. The restrictions on the parameters arising in the model are established with the aim to obtain exact formulae for the non-constant steady-state solutions. As the result, the exact formulae for the fluid fluxes from blood to tissue and across the tissue were constructed together with two linear autonomous ODEs for glucose and albumin concentrations. The analytical results were checked for their applicability for the description of fluid-glucose-albumin transport during peritoneal dialysis.

  14. Experimental and theoretical investigation on the interaction between cyclovirobuxine D and human serum albumin

    Science.gov (United States)

    Yue, Yuanyuan; Liu, Ren; Liu, Jianming; Dong, Qiao; Fan, Jing

    2014-07-01

    Cyclovirobuxine D is an active compound extracted from the plant Buxux microphylla, and widely available as medications; however, its abuse may casts potential detrimental effects on human health. By using multispectroscopic techniques and molecular modeling, the interaction of cyclovirobuxine D with human serum albumin was investigated. The fluorescence results manifested that static type was the operative mechanism for the interaction with human serum albumin. The structural investigation of the complexed HSA through CD, three-dimensional, FT-IR and synchronous fluorescence shown the polypeptide chain of HSA partially destabilizing. Docking studies revealed the molecule to be bound in the subdomain IIA. Finally, we investigated the distance between the bound ligand and Trp-214 of human serum albumin.

  15. THE ROLE OF DIETARY PROPOLIS ON ALBUMINS AND BILIRUBIN CONTENT IN CHICKENS

    Directory of Open Access Journals (Sweden)

    Marcela Capcarová

    2013-12-01

    Full Text Available The present study was designed to determinate the effect of propolis as a feed additive on the serum bilirubin and albumin content of female and male chickens. Broiler chickens hybrid Hubbard JV (n=500 were divided into five groups in each gender (control – C and four experimental groups E1 – E4. Experimental chickens received a propolis extract in feed mixture in various doses (E1 – 150 mg/kg; E2 – 450 mg/kg; E3 – 600 mg/kg; E4 – 800 mg/kg. The group that received feed without propolis addition served as the control. Contents of albumin and bilirubin were determined with spectrophotometer. Supplementation of the diet with propolis in the dose of 600 mg/kg significantly (P<0.05 increased albumin content in male chickens. Propolis addition to diets may be a source for antioxidant capacity in human and animals.

  16. Evaluation of ischemia-modified albumin, oxidative stress, and antioxidant status in acute ischemic stroke patients

    Science.gov (United States)

    Jena, Itishri; Nayak, Sarthak Ranjan; Behera, Sudeshna; Singh, Bratati; Ray, Subhashree; Jena, Diptimayee; Singh, Santosh; Sahoo, Subrat Kumar

    2017-01-01

    Background: Oxidative stress is characterized by increased production of reactive oxygen species resulting in the generation of lipid peroxides such as malondialdehyde (MDA). The studies have shown that ischemia-modified albumin (IMA), which has widely been studied as a marker of ischemia, also increases as result of oxidative stress. Hence, the current study was done to evaluate the serum MDA, IMA along with serum uric acid, and albumin, which are important metabolic antioxidants. Materials and Methods: Fifty patients with acute ischemic stroke were taken as cases and compared with 50 age- and sex-matched controls. Serum MDA, IMA, uric acid, and albumin were estimated both in cases and controls. Serum MDA was estimated by the method of Satoh and IMA by Bar-Or et al. The results were analyzed statistically. Results: Serum MDA and IMA values were significantly increased in cases (P stroke, and the deranged oxidant-antioxidant balance further contributes to its severity. PMID:28250685

  17. Distribution of albumin in the normal monkey eye as revealed by Evans blue fluorescence microscopy.

    Science.gov (United States)

    Radius, R L; Anderson, D R

    1980-03-01

    Since intravenously injected Evans blue binds irreversibly to serum albumin, its distribution reflects albumin exchange between the intravascular and extravascular tissue compartments. In histologic specimens examined by fluorescence, microscopy, extravasated Evans blue--albumin complex was identified within the ciliary body and trabecular meshwork of normal monkey eyes. In eyes fixed by intra-arterial perfusion of fixative, no dye was identified in the choroid, retina, or optic nerve. With immersion fixation, however, some extravasation was seen in the choroid and adjacent optic nerve. In some specimens, the optic nerve was stained not only with material apparently leaking from the choroid but also from a breakdown of the blood-brain barrier in the major disc vasculature during the interval before fixative penetrates into the tissue. Perfusion fixation must be used to avoid this artifact, and freezing techniques would be even better.

  18. ALTERATIONS IN TOTAL PROTEIN CONCENTRATION, SERUM PROTEIN FRACTIONS AND ALBUMIN/GLOBULIN RATIO IN HEALTHY RABBITS

    Directory of Open Access Journals (Sweden)

    Nuzhat Sultana

    2013-08-01

    Full Text Available This study assessed the effect of oral administration of Aloe vera and was to evaluate total serum protein, albumin and globulin concentrations as well as albumin / globulin (A / G ratio. Twenty rabbits weighing 1000 – 1800 g were divided into 2 groups. Each group consisted of ten animals. One served as control and other group served as experimental group. Results show that animals after 07, 15 and 30 days dosing of Aloe vera showed highly significant decrease in total protein and globulin and highly significant decrease in Albumin after 15 and 30 days of dosing of Aloe vera in comparison to control animals group. It is concluded that the long-term use of Aloe vera may cause hypoglobinemia and hypoalbuminemia at 30 days of dosing and it could be due to the liver diseases, evidence of hepatotoxicity induced Aloe vera also reported in previous studies.

  19. Spectroscopic Investigation on the Interaction of a Cyanine Dye with Serum Albumins

    Institute of Scientific and Technical Information of China (English)

    ZHANG Ya-Zhou; YANG Qian-Fan; DU Hong-Yan; TANG Ya-Lin; XU Guang-Zhi; YAN Wen-Peng

    2008-01-01

    The interactions of a cyanine dye with human serum albumin (HSA) and bovine serum albumin (BSA) have been investigated by using absorption and fluorescence spectra.Absorption spectral studies show that binding to the serum albumins leads to a bathochromic shift of the monomer band together with a notable intensity change.Furthermore, the number of binding sites (n) was identified by the absorption spectra.There is a constant enhancement of fluorescence quantum yield when the cyanine dye complexes with HSA or BSA.The apparent binding constant (Ka) and the free energy changes (△G) were obtained by analysis of fluorescence data of the cyanine dye in the absence and presence of HSA and BSA.Compared to BSA, HSA associates with the dye in a stronger way.

  20. Spectral and Fluorescent Studies of the Interaction of an Anionic Oxacarbocyanine Dye with Bovine Serum Albumin

    Science.gov (United States)

    Pronkin, P. G.; Tatikolov, A. S.

    2017-01-01

    The influence of the formation of noncovalent intermolecular complexes with bovine serum albumin (BSA) on the spectral and fluorescent properties of the anionic oxacarbocyanine dye 3,3'-di-(γ-sulfopropyl)-5,5'-diphenyl-9-ethyloxacarbocyanine betaine (OCC) was studied. Binding of OCC to BSA increased significantly the dye fluorescence. Changes in the absorption and fluorescence spectra of OCC upon interaction with BSA argued in favor of a shift of the dye cis-trans equilibrium in the complex. The effects of adding albumin-denaturing compounds (urea, sodium dodecyl sulfate) on the spectral and fluorescent properties of the dye in the OCC-BSA complex were studied. It was concluded that OCC can act as a probe for albumins and can be used to study protein denaturing.

  1. Serum albumin and mortality risk in a hyperendemic area of HCV infection in Japan

    Directory of Open Access Journals (Sweden)

    Sata Michio

    2010-12-01

    Full Text Available Abstract Background Hypoalbuminemia has been shown to be associated with increased mortality. We reported a mass screening in 1990 of X town in Japan, which demonstrated a high prevalence of hepatitis C virus (HCV infection. This follow-up study determined, through a period of 12 years, whether serum albumin levels impact on the life prognosis of the residents of X town. Results Of the 509 subjects, 69 had died and 55 had moved to other regions by 2002. Therefore, we analyzed 454 people for whom we could confirm life and death between 1990 and 2002. Albumin levels were assigned to two groups, low ( Conclusions We show that the serum albumin level is an independent risk factor for mortality from all causes in the residents of X town and an important prognostic indicator. Improvement of hypoalbuminaemia should be considered for improvement of prognosis.

  2. 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 temperature...... constant, it was possible to calculate values for the changes in enthalpy and entropy during the initial binding step. For the medium-chain fatty acids, laurate and myristate, binding of the first molecule to albumin appeared to be enthalpic, with a tendency to an increasing contribution of entropy...... to binding energy with increasing chain length of the fatty acid. Udgivelsesdato: 1990-Jul-5...

  3. Albumin and Furosemide Combination for Management of Edema in Nephrotic Syndrome: A Review of Clinical Studies

    Directory of Open Access Journals (Sweden)

    Margaret Duffy

    2015-10-01

    Full Text Available The treatment of edema in patients with nephrotic syndrome is generally managed by dietary sodium restriction and loop diuretics. However, edema does not improve in some patients despite adequate sodium restriction and maximal dose of diuretics. In such patients, combination of albumin and a loop diuretic may improve edema by diuresis and natriuresis. The response to this combination of albumin and a diuretic has not been observed in all studies. The purpose of this review is to discuss the physiology of diuresis and natriuresis of this combination therapy, and provide a brief summary of various studies that have used albumin and a loop diuretic to improve diuretic-resistant edema. Also, the review suggests various reasons for not observing similar results by various investigators.

  4. Development of albumin-based nanoparticles for the delivery of abacavir.

    Science.gov (United States)

    Wilson, Barnabas; Paladugu, Latishkumar; Priyadarshini, S R Brahmani; Jenita, J Josephine Leno

    2015-11-01

    The study was designed to prepare and evaluate albumin nanoparticles containing antiviral drug abacavir sulphate. Various batches of albumin nanoparticles containing abacavir sulphate were prepared by desolvation method. The abacavir loaded particles were characterized for their yield, percentage of drug loading, surface morphology, particle size, surface charge, pattern of in vitro drug release and release mechanism studies. Drug loading ranged from 1.2 to 5.9%w/w. The mean particle size and the surface charge were 418.2nm and -40.8mV respectively. The in vitro drug release varied between 38.73 and 51.36%w/w for 24h. The n value for Korsmeyer-Peppas was 0.425 indicating Fickian type drug release. The preliminary findings indicated that albumin nanoparticles of abacavir can be prepared by desolvation method with good yield, high drug loading and sustained release.

  5. 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.

  6. Effects of N-acetylcysteine and terbutaline treatment on hemodynamics and regional albumin extravasation in porcine septic shock

    Energy Technology Data Exchange (ETDEWEB)

    Groeneveld, A.B.; den Hollander, W.; Straub, J.; Nauta, J.J.; Thijs, L.G. (Free Univ. Hospital, Amsterdam (Netherlands))

    1990-03-01

    We studied the therapeutic effects of continuously infused N-acetylcysteine, an O2 radical scavenger (N, n = 6), and terbutaline, a beta 2-agonist (T, n = 6), versus dextrose (controls C, N = 6) on hemodynamics and regional albumin extravasation in porcine septic shock. After instrumentation, injection of 99mTc-labeled red blood cells, and baseline measurements, pigs received a 90 min infusion of 11 +/- 9 X 10(8).kg-1 live Escherichia coli bacteria. Thereafter, therapy was started, and 131I human serum albumin was injected. Images were obtained hourly using a gamma camera and a computer until 5 hours after baseline. Regions of interest were drawn in the 99mTc images, yielding regional 131I/99mTc radioactivity ratios, with blood samples as reference. From these ratios, an albumin leak index, a rate constant of transvascular albumin transport, was calculated. Control pigs developed pulmonary hypertension, arterial hypotension, hemoconcentration, and lactic acidemia. In spite of tachycardia and unchanged filling pressures, cardiac output fell. In arterial blood, white cell count, PO2, albumin level, and colloid osmotic pressure fell. The albumin leak index (X10(-3).min-1) measured 1.56 +/- 0.59 over the lungs and 2.87 +/- 1.19 over the abdomen in C, confirming previously found increased albumin flux in both lung and abdomen, the latter exceeding the former. Neither N nor T significantly affected hemodynamic and biochemical changes. The drugs neither decreased the regional albumin leak index nor attenuated the formation of albumin-rich ascites found at autopsy. However, the lung albumin index obtained at autopsy was significantly reduced with N (P less than .01 vs. C), at similar gravimetrically determined extravascular lung water (EVLW). EVLW positively correlated with pulmonary albumin extravasation in C and T but not in N.

  7. In vitro inhibition of human neutrophil elastase by oleic acid albumin formulations from derivatized cotton wound dressings.

    Science.gov (United States)

    Edwards, J Vincent; Howley, Phyllis; Cohen, I Kelman

    2004-10-13

    Human neutrophil elastase (HNE) is elevated in chronic wounds. Oleic acid albumin formulations that inhibit HNE may be applicable to treatment modalities for chronic wounds. Oleic acid/albumin formulations with mole ratios of 100:1, 50:1, and 25:1 (oleic acid to albumin) were prepared and found to have dose response inhibition properties against HNE. The IC50 values for inhibition of HNE with oleic acid/albumin formulations were 0.029-0.049 microM. Oleic acid/albumin (BSA) formulations were bound to positively and negatively charged cotton wound dressings and assessed for elastase inhibition using a fiber bound formulation in an assay designed to mimic HNE inhibition in the wound. Cotton derivatized with both carboxylate and amine functional groups were combined with oleic acid/albumin formulations at a maximum loading of 0.030 mg oleic acid + 0.14 mg BSA/mg fiber. The IC50 values for inhibition of HNE with oleic acid/albumin formulations bound to derivatized cotton were 0.26-0.42 microM. Release of the oleic acid/albumin formulation from the fiber was measured by measuring oleic acid levels with quantitative GC analysis. Approximately, 35-50% of the fiber bound formulation was released into solution within the first 15 min of incubation. Albumin was found to enhance the rate of elastase hydrolysis of the substrate within a concentration range of 0.3-50 g/L. The acceleration of HNE substrate hydrolysis by albumin required increased concentration of inhibitor in the formulation to obtain complete inhibition of HNE. Oleic acid formulations prepared with albumin enable transport, solubility and promote dose response inhibition of HNE from derivatized cotton fibers under aqueous conditions mimicking the chronic wound.

  8. Significant Positive Correlation of Plasma BPDE-Albumin Adducts to Urinary 1-Hydroxypyrene in Coke Oven Workers

    Institute of Scientific and Technical Information of China (English)

    HONG WANG; TANG-CHUN WU; XIAO-BO YANG; AI-LIN LIU; HONG-YAN ZHEN; LIANG GUO; HUA-SHAN LIANG; YONG-YI BI; YUN BAI; YONG-WEN CHEN

    2007-01-01

    Objective To investigate the application of BPDE-albumin adducts as monitoring biomarkers for coke oven workers exposed to polycyclic aromatic hydrocarbons(PAHs)and to explore possible relationship between BPDE-albumin adducts and urinary 1-hydroxypyrene (1-OHP)levels in them.Methods Thirty-seven coke oven workers from a coke plant and 47 controls without the occupational exposure to PAHs were recruited in this study.The levels of plasma BPDE-albumin adducts and urinary 1-OHP were analyzed using high performance liquid chromatography.Results The median levels of BPDE-albumin adducts(42.10 fmol/mg albumin)and urinary 1-OHP(5.46 μmol/mol creatinine)were significantly higher in coke oven workers than in controls(14.16 fmol/mg albumin,2.96 μmol/mol creatinine,respectively;P<0.01).Multiple logistic regression analysis showed that coke oven workers were at higher risk of having BPDE-albumin adduct levels above 25.30 prnol/mg albumin(OR=1.79,P<0.01)and urinary 1-OHP levels above 4.13 μmol/mol creatinine(OR=2.45,P<0.05).There was a positive correlation between the levels of BPDE-albumin adducts and urinary 1-OHP in all subjects(rs=0.349,P<0.01).Conclusion BPDE-albumin adduct is a useful biomarker for monitoring long-term exposure to PAHs,and plasma BPDE-albumin adducts level is significantly correlated to urinary 1-OHP levels in coke oven workers.

  9. 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.

  10. Comparison of methods for urinary albumin determination in patients with type 1 diabetes

    Directory of Open Access Journals (Sweden)

    C. Khawali

    2002-03-01

    Full Text Available We tested the correlation of the albumin-to-creatinine ratio (A/C in an early-morning urine sample, measured with a commercial kit (DCA 2000®, with the conventional immunoturbidimetric determination in the laboratory and with overnight albumin excretion rate (reference method. Fifty-five type 1 diabetic adolescents had their first-morning urine collected on the 1st and 8th day of the period. Urinary albumin and creatinine were determined immediately using the DCA 2000® kit. Samples were also stored for laboratory analysis. To evaluate the correlation between early-morning urinary A/C ratio and overnight albumin excretion rate, 16 subjects had a timed overnight urine collection. A/C ratios determined with the DCA 2000® kit and by the laboratory method were 13.1 ± 20.5 and 20.4 ± 46.3 mg/g, respectively. A/C results by both methods proved to be strongly correlated (r = 0.98, P<0.001. DCA 2000®-determined A/C showed 50% sensitivity and 100% specificity when compared to the reference method. Spot urinary A/C of the subset of 16 subjects significantly correlated with their overnight albumin excretion rate (r = 0.98, P<0.001. Intraindividual variation ranged from 17 to 32% and from 9 to 63% for A/C and overnight albumin excretion rate, respectively. In conclusion, an early-morning specimen should be used instead of timed overnight urine and the A/C ratio is an accurate, reliable and easily determined parameter for the screening of diabetic nephropathy. Immediate measurement of the A/C ratio is feasible using the DCA 2000® kit. Intraindividual variability indicates the need for repeated determinations to confirm microalbuminuria and the diagnosis of incipient diabetic nephropathy.

  11. Chemical Composition Study of Vanadium Pentoxide Xerogels Doped by Bovine Albumin

    Science.gov (United States)

    Sereika, R.; Kaciulis, S.; Mezzi, A.; Brucale, M.

    2016-06-01

    Metal-bioorganic compounds of vanadium pentoxide and bovine serum albumin (BSA) (Fraction V) were obtained by using sol-gel method. Series of the samples (BSA)xV2O5ṡnH2O, where x=0, 0.01 and 0.001, were originally produced by the synthesis of vanadium pentoxide xerogels and subsequent blending with water-dissolved BSA in appropriate molar ratios. It was evident that the gelation process does not occur for x>0.01. For the X-ray photoelectron spectroscopy (XPS) studies, the thin layers of these materials were prepared by drying the gel onto the glass and mica substrates. The surface morphology of the samples was characterized by scanning electron microscopy (SEM) and atomic force microscopy (AFM) techniques. It follows from the analysis of experimental XPS spectra of (BSA)xV2O5ṡnH2O that the nitrogen ions in pure albumin and in (BSA)0.01V2O5ṡnH2O are present in imine, amine and protonated amine groups. The additional protonated amine arises when the concentration of albumin in (BSA)xV2O5ṡnH2O is low (x=0.001). Increasing the amount of albumin results in decrease of the number of oxygen ions bonded to vanadium. At the same time (with increase of albumin), the component of oxygen bounded to carbon and nitrogen is increasing. In the samples with greater amount of albumin, the reduction of vanadium ions occurs. This means that the trivalent and tetravalent vanadium ions are present together with pentavalent ones.

  12. Aging-associated oxidized albumin promotes cellular senescence and endothelial damage

    Directory of Open Access Journals (Sweden)

    Luna C

    2016-02-01

    Full Text Available Carlos Luna,1,* Matilde Alique,2,* Estefanía Navalmoral,2 Maria-Victoria Noci,3 Lourdes Bohorquez-Magro,2 Julia Carracedo,1 Rafael Ramírez2 1Nephrology Unit, Instituto Maimónides de Investigación Biomédica de Córdoba (IMIBIC, Reina Sofía University Hospital, Córdoba, Spain; 2Department of Systems Biology, Physiology Unit, Universidad de Alcalá, Madrid, Spain; 3Anesthesia Unit, Reina sofía University Hospital, Córdoba, Spain*These authors contributed equally to this work Abstract: Increased levels of oxidized proteins with aging have been considered a cardiovascular risk factor. However, it is unclear whether oxidized albumin, which is the most abundant serum protein, induces endothelial damage. The results of this study indicated that with aging processes, the levels of oxidized proteins as well as endothelial microparticles release increased, a novel marker of endothelial damage. Among these, oxidized albumin seems to play a principal role. Through in vitro studies, endothelial cells cultured with oxidized albumin exhibited an increment of endothelial damage markers such as adhesion molecules and apoptosis levels. In addition, albumin oxidation increased the amount of endothelial microparticles that were released. Moreover, endothelial cells with increased oxidative stress undergo senescence. In addition, endothelial cells cultured with oxidized albumin shown a reduction in endothelial cell migration measured by wound healing. As a result, we provide the first evidence that oxidized albumin induces endothelial injury which then contributes to the increase of cardiovascular disease in the elderly subjects.Keywords: elderly, oxidative stress, microparticles, vascular damage

  13. Recombinant albumin adsorption on mica studied by AFM and streaming potential measurements.

    Science.gov (United States)

    Kujda, Marta; Adamczyk, Zbigniew; Morga, Maria; Sofińska, Kamila

    2015-03-01

    Recombinant human serum albumin (rHSA) in monomeric state is widely used in pharmaceutical industry as a drug excipient and for preparing coatings for medical devices. In this work the adsorption process of rHSA on model mica surface at pH 3.5 was studied using the atomic force microscopy (AFM) and in situ streaming potential measurements. The kinetics of albumin adsorption was determined by a direct enumeration of single molecules over various substrate areas. These results were consistent with streaming potential measurements carried out for the parallel-plate channel flow and with theoretical predictions derived from the random sequential adsorption (RSA) model. Desorption kinetics of albumin under flow conditions was also evaluated via the streaming potential measurements. In this way, the amount of irreversibly bound albumin was quantitatively evaluated to be 0.64 and 1.2 mg m(-2) for ionic strength of 0.01 and 0.15 M, respectively. This agrees with previous results obtained for HSA and theoretical calculations derived from the RSA model. Additionally, it was demonstrated that there existed a fraction of reversibly bound albumin that can be fully eluted within a few hours. The binding energy of these fraction of molecules was -18 kT that is consistent with the electrostatic controlled adsorption mechanism of albumin at this pH. It was concluded that the rHSA monolayers of well-defined coverage can find applications for quantitatively analyzing ligand binding and for performing efficient biomaterials and immunological tests.

  14. (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

    -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......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...... liver disease), simultaneous measurements of PV were taken with 99mTc-HSA and 125I-HSA after 1 h in the supine position. Blood samples were obtained before and 10 min after quantitative injection of the two indicators. In a subset of patients (n = 32), the measurements were repeated within 1 h. Results...

  15. Rapidly reversible albumin and beta 2-microglobulin hyperexcretion in recent severe essential hypertension

    DEFF Research Database (Denmark)

    Christensen, Cramer

    1983-01-01

    by conventional methods and serum creatinine was normal. A pronounced but quite variably elevated albumin excretion 440 +/- 448 micrograms/min (mean +/- s.d.) and a moderately increased beta 2-microglobulin excretion 3.06 +/- 3.29 micrograms/min was noted before treatment. The abnormal albumin excretion...... to arterial pressures in all patients. Thus glomerular and to some extent tubular protein handling were both affected in untreated patients, but rapidly reversible during initial antihypertensive treatment. The data indicate that the beta 2-microglobulin hyperexcretion is secondary to enhanced filtration...

  16. Albumin liver dialysis as pregnancy-saving procedure in cholestatic liver disease and intractable pruritus

    Institute of Scientific and Technical Information of China (English)

    Maud Lemoine; Aurélie Revaux; Claire Francoz; Guillaume Ducarme; Sabine Brechignac; Emmanuel Jacquemin; Michèle Uzan; Nathalie Ganne-Carrié

    2008-01-01

    Progressive familial intrahepatic cholestasis type 3 (PFIC3) is a rare cholestatic liver disease. Such liver disease can get worse by female hormone disorder. Albumin dialysis or Molecular Adsorbent Recirculating System (MARS) has been reported to reverse severe cholestasis-linked pruritus. Here, we report the first use of HARS during a spontaneous pregnancy and its successful outcome in a patient with PFIC3 and intractable pruritus. Albumin dialysis could be considered as a pregnancy-saving procedure in pregnant women with severe cholestasis and refractory pruritus.C 2008 The WJG Press. All rights reserved.

  17. Association between Risk Factors and Overnight Albumin/Creatinine Ratio - even in its Normal Range

    DEFF Research Database (Denmark)

    Olivarius, Niels de Fine; Andreasen, A.H.; Mogensen, C.E.

    1994-01-01

    I denne lille artikel påvises det, at selv en ganske let forøget udskillelse af albumin i urinen forekommer hyppigere hos aldersdiabetikere med (andre) risikofaktorer såsom hypertension, hyperlipidæmi, hyperglykæmi etc. Udgivelsesdato: 1994......I denne lille artikel påvises det, at selv en ganske let forøget udskillelse af albumin i urinen forekommer hyppigere hos aldersdiabetikere med (andre) risikofaktorer såsom hypertension, hyperlipidæmi, hyperglykæmi etc. Udgivelsesdato: 1994...

  18. Cobinding of bilirubin and laurate to human serum albumin: spectroscopic characterization of stoichiometric complexes

    DEFF Research Database (Denmark)

    Honoré, B; Sato, H; Brodersen, R

    1988-01-01

    Light absorption and CD spectra of bound bilirubin and albumin fluorescence spectra have been recorded from mixtures containing albumin, A, bilirubin, B, and laurate, L, in Tris-NaCl buffer at pH 8.2, 25 degrees C. Concentrations of the corresponding stoichiometric complexes, ABiLj, for i = 0....... Brodersen et al. (1987) Eur. J. Biochem. 169, 487-495). The results were utilized at the microscopic level to investigate ligand-induced conformational changes. When laurate was bound to AB, a decrease of the distance between Trp-214 and the bound bilirubin occurred, as measured according to Förster...

  19. 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

  20. Interaction of Palmitic Acid with Metoprolol Succinate at the Binding Sites of Bovine Serum Albumin

    OpenAIRE

    Mashiur Rahman; Farzana Prianka; Mohammad Shohel; Md. Abdul Mazid

    2014-01-01

    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 a...

  1. Microalbuminuria reflects a generalized transvascular albumin leakiness in clinically healthy subjects

    DEFF Research Database (Denmark)

    Jensen, J S; Borch-Johnsen, K; Jensen, G;

    1995-01-01

    1. In epidemiological studies microalbuminuria, i.e. slightly elevated urinary albumin excretion rate, predicts increased atherosclerotic vascular morbidity and mortality. This study aimed to test the hypothesis that microalbuminuria in clinically healthy subjects is associated with a systemic...... excretion rate was 6.6 micrograms/min. Twenty-seven patients with persistent microalbuminuria (urinary albumin excretion rate 6.6-150 micrograms/min), and 56 age- and sex-matched control subjects with persistent normoalbuminuria (UAER ...% confidence interval 0.1-0.7; n = 83), r = 0.29, P microalbuminuria is an independent marker...

  2. Nanomolar detection of glucose using SERS substrates fabricated with albumin coated gold nanoparticles

    Science.gov (United States)

    Perez-Mayen, Leonardo; Oliva, Jorge; Salas, P.; de La Rosa, Elder

    2016-06-01

    This work presents the design of substrates for Surface Enhanced Raman Scattering (SERS) using star-like gold nanoparticles synthesized by a wet chemical method. The SERS substrates were used for glucose detection for concentrations as low as 10-7 M, which represents an enhancement factor (EF) of 109, as a result of the hot spot formed by the spike termination and appropriate distribution of the gold nanoparticles. An improvement of two orders of magnitude was obtained by coating the gold nanoparticles with albumin with the configuration: glass/Au nanoparticles/albumin. In this case the lowest detection was at a concentration of 10-9 M for an EF of 1011. The albumin molecule allowed us to enhance the Raman signal because of the formation of peptide bonds (COOH-NH2) generated due to the interaction of glucose with albumin, and the appropriate separation distance between the glucose molecules and gold nanoparticles. The presence of such peptide conjugates was confirmed by FTIR spectra. Thus, our results suggest that our SERS substrates can be useful for the detection of very low concentrations of glucose, which is important for the diagnosis of diabetes in the field of medicine.This work presents the design of substrates for Surface Enhanced Raman Scattering (SERS) using star-like gold nanoparticles synthesized by a wet chemical method. The SERS substrates were used for glucose detection for concentrations as low as 10-7 M, which represents an enhancement factor (EF) of 109, as a result of the hot spot formed by the spike termination and appropriate distribution of the gold nanoparticles. An improvement of two orders of magnitude was obtained by coating the gold nanoparticles with albumin with the configuration: glass/Au nanoparticles/albumin. In this case the lowest detection was at a concentration of 10-9 M for an EF of 1011. The albumin molecule allowed us to enhance the Raman signal because of the formation of peptide bonds (COOH-NH2) generated due to the

  3. Albumin activation of urinary amylase as determined with the Du Pont aca.

    Science.gov (United States)

    Garber, C C; Carey, R N

    1978-04-01

    Protein activation of urinary alpha-amylase (EC 3.2.1.1) activity was observed during an evaluation of the Du Pont aca procedure for the determination of urinary alpha-amylase. This activation effect became constant for urinary albumin concentrations exceeding 1.50 g/liter. It is recommended that urinary alpha-amylase be analyzed with sufficient albumin added to maximize this effect. The aca alpha-amylase procedure is compared to an amyloclastic method for both serum and urine analysis. Expected ranges are presented for the aca method for serum and urinary amylase, amylase clearance, and the amylase clearance/creatinine clearance ratio.

  4. Determination of albumin transport rate between plasma and peritoneal space in decompensated cirrhosis

    DEFF Research Database (Denmark)

    Ring-Larsen, H; Henriksen, Jens Henrik Sahl

    1984-01-01

    the abdominal puncture may lead to overestimation of TERperit.space, whereas systematic understimation seems less likely. This may besides differences in patient selection and unsteady state, account for the discrepancy between the present relatively low value and earlier reports on much higher values.......10-0.59). The transport rate of albumin from ascitic fluid back to plasma was measured in eight patients by plasma sampling after intraperitoneal injection of 131I-labelled serum albumin. After correction for tracer re-extravasation this back transport (median 0.31, range 0.07-0.44% IVM/h-1) was not significantly...

  5. Fluorescence spectroscopic studies on binding of a flavonoid antioxidant quercetin to serum albumins

    Indian Academy of Sciences (India)

    Beena Mishra; Atanu Barik; K Indira Priyadarsini; Hari Mohan

    2005-11-01

    Binding of quercetin to human serum albumin (HSA) was studied and the binding constant measured by following the red-shifted absorption spectrum of quercetin in the presence of HSA and the quenching of the intrinsic protein fluorescence in the presence of different concentrations of quercetin. Fluorescence lifetime measurements of HSA showed decrease in the average lifetimes indicating binding at a location, near the tryptophan moiety, and the possibility of fluorescence energy transfer between excited tryptophan and quercetin. Critical transfer distance () was determined, from which the mean distance between tryptophan-214 in HSA and quercetin was calculated. The above studies were also carried out with bovine serum albumin (BSA).

  6. Competitive Protein Adsorption of Albumin and Immunoglobulin G from Human Serum onto Polymer Surfaces

    DEFF Research Database (Denmark)

    Holmberg, Maria; Hou, Xiaolin

    2010-01-01

    Competitive protein adsorption from human serum onto unmodified polyethylene terephthalate (PET) surfaces and plasma-polymerized PET surfaces, using the monomer diethylene glycol vinyl ether (DEGVE), has been investigated using radioactive labeling. Albumin and immunoglobulin G (IgG) labeled...... with two different iodine isotopes have been added to human serum solutions of different concentrations, and adsorption has been performed using adsorption times from approximately 5 s to 24 h. DEGVE surfaces showed indications of being nonfouling regarding albumin and IgG adsorption during competitive...

  7. Comparison of Normal Saline, Hypertonic Saline Albumin and Terlipressin plus Hypertonic Saline Albumin in an Infant Animal Model of Hypovolemic Shock

    OpenAIRE

    Javier Urbano; Rafael González; Jorge López; Solana, María J.; Bellón, José M.; Marta Botrán; Ana García; Fernández, Sarah N.; Jesús López-Herce

    2015-01-01

    Introduction In series of cases and animal models suffering hemorrhagic shock, the use of vasopressors has shown potential benefits regarding hemodynamics and tissue perfusion. Terlipressin is an analogue of vasopressin with a longer half-life that can be administered by bolus injection. We have previously observed that hypertonic albumin improves resuscitation following controlled hemorrhage in piglets. The aim of the present study was to analyze whether the treatment with the combination of...

  8. Cohort study of predictive value of urinary albumin excretion for atherosclerotic vascular disease in patients with insulin dependent diabetes

    DEFF Research Database (Denmark)

    Deckert, T; Yokoyama, H; Mathiesen, E

    1996-01-01

    atherosclerotic vascular disease during follow up of 2457 person year. Elevated urinary albumin excretion was significantly predictive of atherosclerotic vascular disease (hazard ratio 1.06 (95% confidence interval 1.02 to 1.18) per 5 mg increase in 24 hour urinary albumin excretion, P = 0.002). Predictive effect...

  9. 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...

  10. Modification of the free sulphydryl groups of bovine serum albumin to probe conformational transitions in the neutral region

    NARCIS (Netherlands)

    Janssen, L.H.M.; Roomer, Anton C.J.

    1985-01-01

    The free SH group in bovine serum albumin has been modified by covalent coupling with 2-chloromercuri-4-nitrophenol and 2-chloromercuri-2,4-dinitrophenol. The ionization of the phenolic OH group of the former label when bound to albumin can be followed spectrophotometrically. The pK of this group wa

  11. 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

    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...

  12. 9 CFR 95.15 - Blood meal, blood albumin, intestines, and other animal byproducts for industrial use...

    Science.gov (United States)

    2010-01-01

    ... 9 Animals and Animal Products 1 2010-01-01 2010-01-01 false Blood meal, blood albumin, intestines... BYPRODUCTS (EXCEPT CASINGS), AND HAY AND STRAW, OFFERED FOR ENTRY INTO THE UNITED STATES § 95.15 Blood meal, blood albumin, intestines, and other animal byproducts for industrial use; requirements for...

  13. High Mobility Group Box Protein 1 Boosts Endothelial Albumin Transcytosis through the RAGE/Src/Caveolin-1 Pathway

    Science.gov (United States)

    Shang, Dan; Peng, Tao; Gou, Shanmiao; Li, Yiqing; Wu, Heshui; Wang, Chunyou; Yang, Zhiyong

    2016-01-01

    High-mobility group box protein 1 (HMGB1), an inflammatory mediator, has been reported to destroy cell-cell junctions, resulting in vascular endothelial hyperpermeability. Here, we report that HMGB1 increases the endothelial transcytosis of albumin. In mouse lung vascular endothelial cells (MLVECs), HMGB1 at a concentration of 500 ng/ml or less did not harm cell-cell junctions but rapidly induced endothelial hyperpermeability to 125I-albumin. HMGB1 induced an increase in 125I-albumin and AlexaFluor 488-labeled albumin internalization in endocytosis assays. Depletion of receptor for advanced glycation end products (RAGE), but not TLR2 or TLR4, suppressed HMGB1-induced albumin transcytosis and endocytosis. Genetic and pharmacological destruction of lipid rafts significantly inhibited HMGB1-induced albumin endocytosis and transcytosis. HMGB1 induced the rapid phosphorylation of caveolin (Cav)-1 and Src. Either RAGE gene silencing or soluble RAGE suppressed Cav-1 Tyr14 phosphorylation and Src Tyr418 phosphorylation. The Src inhibitor 4-amino-5-(4-chlorophenyl)-7-(t-butyl) pyrazolo[3,4-d] pyrimidine (PP2) blocked HMGB1-induced Cav-1 Tyr14 phosphorylation. PP2 and overexpression of Cav-1 with a T14F mutation significantly inhibited HMGB1-induced transcytosis and albumin endocytosis. Our findings suggest that HMGB1 induces the transcytosis of albumin via RAGE-dependent Src phosphorylation and Cav-1 phosphorylation. These studies revealed a new mechanism of HMGB1-induced endothelial hyperpermeability. PMID:27572515

  14. Long-term albumin infusion improves survival in patients with cirrhosis and ascites: An unblinded randomized trial

    Institute of Scientific and Technical Information of China (English)

    Roberto Giulio Romanelli; Paolo Gentilini; Giacomo Laffi; Giorgio La Villa; Giuseppe Barletta; Francesco Vizzutti; Fabio Lanini; Umberto Arena; Vieri Boddi; Roberto Tarquini; Pietro Pantaleo

    2006-01-01

    AIM: To investigate the effects of long-term albumin administration on survival, recurrence of ascites and onset of other complications.METHODS: One hundred consecutive patients admitted for first-onset ascites were randomized to receive diuretics plus human albumin 25 g/wk in the first year and 25g every two wk thereafter (group 1) or diuretics alone (group 2). The primary endpoint was survival without liver transplantation. Secondary endpoints were recurrence of ascites and occurrence of other complications.RESULTS: Median follow-up was 84 (2-120) mo. Albumin-treated patients had significantly greater cumulative survival rate (Breslow test= 7.05, P= 0.0078) and lower probability of ascites recurrence (51% versus 94%,P<0.0001). Chronic albumin infusion resulted in a mean increase in survival of 16 mo.CONCLUSION: Long-term albumin administration after first-onset ascites significantly improves patients' survival and decreases the risk of ascites recurrence.

  15. Effect of insulin on albumin production and incorporation of 14C-leucine into proteins in isolated parenchymal liver cells from normal rats

    DEFF Research Database (Denmark)

    Dich, J; Gluud, C N

    1975-01-01

    the immunologically determined increment in the incubation medium was 1.7 +/- 0.2 mug albumin/min per g liver wet wt. This is about 30% of the rate of production in the perfused liver. Addition of insulin (10(-6)-10(-10) M) enhanced albumin production (50-17%), and incorporation of 14C-leucine both into albumin (50......Parenchymal rat liver cells were isolated by a modification of the collagenase method of Quistorff, Bondesen and Grunnet. The cells secreted albumin into the medium and incorporated 14C-leucine both into cell proteins and proteins secreted into the medium. Albumin production measured from......-8%), secreted proteins (40-9%) and cell proteins (20-8%). Insulin does not increase the production of albumin by depleting the cells. The effect of insulin on albumin production is compatible with an effect on the rate of synthesis as the specific activity of albumin is unaffected by addition of insulin....

  16. Albumin modulates S1P delivery from red blood cells in perfused microvessels: mechanism of the protein effect.

    Science.gov (United States)

    Adamson, R H; Clark, J F; Radeva, M; Kheirolomoom, A; Ferrara, K W; Curry, F E

    2014-04-01

    Removal of plasma proteins from perfusates increases vascular permeability. The common interpretation of the action of albumin is that it forms part of the permeability barrier by electrostatic binding to the endothelial glycocalyx. We tested the alternate hypothesis that removal of perfusate albumin in rat venular microvessels decreased the availability of sphingosine-1-phosphate (S1P), which is normally carried in plasma bound to albumin and lipoproteins and is required to maintain stable baseline endothelial barriers (Am J Physiol Heart Circ Physiol 303: H825-H834, 2012). Red blood cells (RBCs) are a primary source of S1P in the normal circulation. We compared apparent albumin permeability coefficients [solute permeability (Ps)] measured using perfusates containing albumin (10 mg/ml, control) and conditioned by 20-min exposure to rat RBCs with Ps when test perfusates were in RBC-conditioned protein-free Ringer solution. The control perfusate S1P concentration (439 ± 46 nM) was near the normal plasma value at 37 °C and established a stable baseline Ps (0.9 ± 0.4 × 10(-6) cm/s). Ringer solution perfusate contained 52 ± 8 nM S1P and increased Ps more than 10-fold (16.1 ± 3.9 × 10(-6) cm/s). Consistent with albumin-dependent transport of S1P from RBCs, S1P concentrations in RBC-conditioned solutions decreased as albumin concentration, hematocrit, and temperature decreased. Protein-free Ringer solution perfusates that used liposomes instead of RBCs as flow markers failed to maintain normal permeability, reproducing the "albumin effect" in these mammalian microvessels. We conclude that the albumin effect depends on the action of albumin to facilitate the release and transport of S1P from RBCs that normally provide a significant amount of S1P to the endothelium.

  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. Targeted non-covalent self-assembled nanoparticles based on human serum albumin

    NARCIS (Netherlands)

    Bunschoten, Anton; Buckle, Tessa; Kuil, Joeri; Luker, Gary D.; Luker, Kathryn E.; Nieweg, Omgo; van Leeuwen, Fijs W. B.

    2012-01-01

    Human serum albumin (HSA) is a biological nanocarrier that forms non-covalent complexes with a number of synthetic and biomolecules. Previously we demonstrated radiolabeled HSA-based nanoparticles can form non-covalent complexes with fluorescent cyanine dyes yielding imaging agents for surgical guid

  19. Ischemia-Modified albumin level in type 2 diabetes mellitus—Preliminary report

    Directory of Open Access Journals (Sweden)

    Agnieszka Piwowar

    2008-01-01

    Full Text Available Aim: The main goal of the present study was the evaluation of ischemia-modified albumin (IMA in patients with type 2 diabetes mellitus and estimation of its connection with vascular complications, glycemic control, hypertension, dyslipidemia and obesity.

  20. Urine albumin to creatinine ratio: A marker of early endothelial dysfunction in youth

    Science.gov (United States)

    The urine albumin-to-creatinine ratio (UACR) is a useful predictor of cardiovascular (CV) events in adults. Its relationship to vascular function in children is not clear. We investigated whether UACR was related to insulin resistance and endothelial function, a marker of subclinical atherosclerosis...

  1. What predicts progression and regression of urinary albumin excretion in the nondiabetic population?

    NARCIS (Netherlands)

    Brantsma, Auke H.; Atthobari, Jarir; Bakker, Stephan J. L.; de Zeeuw, Dick; de Jong, Paul E.; Gansevoort, Ronald T.

    2007-01-01

    An increase or decrease in urinary albumin excretion (UAE) is associated with, respectively, a higher or lower risk for renal and cardiovascular disease, independent of widely known cardiovascular risk factors. This study aimed to identify factors that are associated with changes in UAE in the nondi

  2. Glomerular endothelial surface layer acts as a barrier against albumin filtration

    NARCIS (Netherlands)

    Dane, M.J.; Berg, B.M. van den; Avramut, M.C.; Faas, F.G.; Vlag, J. van der; Rops, A.L.; Ravelli, R.B.; Koster, B.J.; Zonneveld, A.J. van; Vink, H.; Rabelink, T.J.

    2013-01-01

    Glomerular endothelium is highly fenestrated, and its contribution to glomerular barrier function is the subject of debate. In recent years, a polysaccharide-rich endothelial surface layer (ESL) has been postulated to act as a filtration barrier for large molecules, such as albumin. To test this hyp

  3. Preoperative albumin-to-globulin ratio and prognostic nutrition index predict prognosis for glioblastoma

    Science.gov (United States)

    Xu, Wen-Zhe; Li, Feng; Xu, Zhen-Kuan; Chen, Xuan; Sun, Bin; Cao, Jing-Wei; Liu, Yu-Guang

    2017-01-01

    Objective Impaired immunonutritional status has disadvantageous effects on outcomes for cancer patients. Preoperative albumin-to-globulin ratio (AGR) and the prognostic nutrition index (PNI) have been used as prognostic factors in various cancers. We aimed to evaluate the clinical significance of the AGR and PNI in glioblastoma. Materials and methods This retrospective analysis involved 166 patients. Demographic, clinical, and laboratory data were collected. AGR and the PNI were calculated as AGR = albumin/(total serum protein − albumin) and PNI = albumin (g/L) + 5 × total lymphocyte count (109/L). Overall survival (OS) was estimated by Kaplan–Meier analysis. Receiver-operating characteristic analysis was used to assess the predictive ability of AGR and the PNI. Cox proportional-hazard models estimating hazard ratios (HRs) and 95% confidence intervals (CIs) were used for univariable and multivariable survival analyses. Results The cutoff values of AGR and PNI were 1.75 and 48. OS was enhanced, with high AGR (>1.75) and the PNI (>48) (Pglioblastoma. AGR and the PNI could also help in developing good adjuvant-therapy schedules. PMID:28223828

  4. Urinary albumin excretion and the renin-angiotensin system in cardiovascular risk management

    NARCIS (Netherlands)

    Van de Wal, R. M. A.; Voors, A. A.; Gansevoort, R. T.

    2006-01-01

    Microalbuminuria has been shown to be a strong predictor of cardiovascular morbidity and mortality in diabetic and hypertensive patients, but also in the general population. Moreover, several reports suggest that reduction of urinary albumin excretion (UAE) is associated with improvement of cardiova

  5. Usefulness of serum-ascites albumin difference in separating transudative from exudative ascites. Another look.

    Science.gov (United States)

    Mauer, K; Manzione, N C

    1988-10-01

    The serum-ascites albumin difference is reported to be superior to ascitic total protein, ascitic-to-serum total protein ratio, lactic dehydrogenase, and ascitic-to-serum lactic dehydrogenase ratio in differentiating between ascites from liver disease and malignant ascites, S-A greater than 1.1 reflecting portal hypertension. We analyzed ascitic fluid from 46 consecutive patients with chronic liver disease, 28 patients with ascites associated with malignancy, 10 patients with right-sided heart failure, 4 patients with hypothyroidism, and 6 patients with miscellaneous causes of ascites to determine if this albumin difference is indeed a more valuable parameter. Analysis of our data confirms with a larger number of patients that the serum-ascites albumin difference is a more reliable indicator of transudative ascites, better termed portal hypertensive ascites. Malignant ascites without liver metastases had features of nonportal hypertensive ascites, and the serum-ascites albumin difference confirms this. The characteristics of malignant ascites associated with liver metastases, however, resemble those of the portal hypertensive ascites complicating liver disease. This new parameter is also helpful in distinguishing congestive heart failure with high protein ascites and portal hypertensive ascitic features from malignant ascites without liver metastases. Of particular note, myxedematous ascitic fluid, classically categorized as exudative, had an S-A greater than 1.1, indicating the possible role of portal hypertension in the development of ascites in these patients.

  6. Relationship between Plasma Albumin Concentration and Plasma Volume in 5 Inbred Rat Strains.

    Science.gov (United States)

    Rose, Rajiv; Klemcke, Harold G

    2015-09-01

    Using the Evans Blue procedure, we previously found strain-related differences in plasma volumes in 5 inbred rat strains. Because albumin binds strongly with Evans blue, this protein is important in the Evans blue method of plasma volume determination. Therefore, we speculated that interstrain differences in plasma albumin concentration (PAC) could distort calculated plasma volumes. To address this concern, we used ELISA techniques to measure PAC in these inbred rat strains. In study A, the blood volume was measured by using Evans blue dye, and albumin was measured at the start of hemorrhage. In study B, blood volume was not measured, and albumin was measured twice, near the start and end of hemorrhage (approximately 14 min apart). Neither study revealed any interstrain differences in PAC, which decreased after hemorrhage in all 5 strains. No correlation was found between PAC and plasma volume, survival time, blood lactate, or blood base excess. Percentage changes in PAC during hemorrhage were greater in salt-sensitive compared with Lewis rats. Moreover, these percentage changes were associated with survival time in Fawn hooded hypertensive rats. Our data show that the plasma volumes we measured previously were not misrepresented due to variations in PAC.

  7. Serum albumin acts as a shuttle to enhance cholesterol efflux from cells.

    Science.gov (United States)

    Sankaranarayanan, Sandhya; de la Llera-Moya, Margarita; Drazul-Schrader, Denise; Phillips, Michael C; Kellner-Weibel, Ginny; Rothblat, George H

    2013-03-01

    An important mechanism contributing to cell cholesterol efflux is aqueous transfer in which cholesterol diffuses from cells into the aqueous phase and becomes incorporated into an acceptor particle. Some compounds can enhance diffusion by acting as shuttles transferring cholesterol to cholesterol acceptors, which act as cholesterol sinks. We have examined whether particles in serum can enhance cholesterol efflux by acting as shuttles. This task was accomplished by incubating radiolabeled J774 cells with increasing concentrations of lipoprotein-depleted sera (LPDS) or components present in serum as shuttles and a constant amount of LDL, small unilamellar vesicles, or red blood cells (RBC) as sinks. Synergistic efflux was measured as the difference in fractional efflux in excess of that predicted by the addition of the individual efflux values of sink and shuttle alone. Synergistic efflux was obtained when LPDS was incubated with cells and LDL. When different components of LPDS were used as shuttles, albumin produced synergistic efflux, while apoA-I did not. A synergistic effect was also obtained when RBC was used as the sink and albumin as shuttle. The previously observed negative association of albumin with coronary artery disease might be linked to reduced cholesterol shuttling that would occur when serum albumin levels are low.

  8. Tissue to plasma capillary permeability of 131I-albumin in the perfused rabbit ear

    DEFF Research Database (Denmark)

    Bent-Hansen, L; Svendsen, Jesper Hastrup

    1991-01-01

    The tissue to plasma transfer of 131I-albumin was recorded in perfused rabbit ears (n = 6) following equilibration for 24 hr. 125I-fibrinogen served as the plasma marker, and was introduced intravenously 15 min before clamping. The ears were rollerpump perfused with isotonic diluted plasma...

  9. Arene control over thiolate to sulfinate oxidation in albumin by organometallic ruthenium anticancer complexes.

    Science.gov (United States)

    Hu, Wenbing; Luo, Qun; Ma, Xiaoyan; Wu, Kui; Liu, Jianan; Chen, Yi; Xiong, Shaoxiang; Wang, Jianping; Sadler, Peter J; Wang, Fuyi

    2009-07-06

    Interactions of organometallic ruthenium anticancer complexes [Ru(eta6-arene)Cl(en)][PF6] (arene=p-cymene (1) or biphenyl (2), en=ethylenediamine) with human serum albumin were investigated by means of mass spectrometry combined with trypsin digestion, specific sidechain modifications and computational modelling. Both complexes were shown to bind to surface histidine (His128, His247, His510) and methionine (Met298) residues in human albumin, but only the p-cymene complex can gain entry to the crevice containing the free cysteine thiolate (Cys34) and induce oxidation to sulfinate. The two complexes exhibit a similar coordination preference for histidine and methionine residues on the protein surface. His128 binding is favoured both kinetically and thermodynamically. At 310 K, six days of incubation of recombinant human albumin (rHA) with complex 1 (rHA:Ru 50:250 microM) led to about 18 % ruthenation of His128 in the protein. However, the extent of ruthenation of albumin by complex 2 was less than that by 1, due to the steric hindrance from the biphenyl ligand. These results imply that the arene ligand in the organometallic ruthenium anticancer complexes plays a crucial role in interactions with proteins.

  10. Usefulness of the bilirubin/albumin ratio for predicting bilirubin-induced neurotoxicity in premature infants

    NARCIS (Netherlands)

    Hulzebos, C. V.; van Imhoff, D. E.; Bos, A. F.; Ahlfors, C. E.; Verkade, H. J.; Dijk, P. H.

    2008-01-01

    Unconjugated hyperbilirubinaemia occurs in almost all premature infants and is potentially neurotoxic. Treatment is based on total serum bilirubin (TSB), but treatment thresholds are not evidence based. Free bilirubin (Bf) - that is, not bound to albumin, seems a better parameter for bilirubin neuro

  11. Chronic kidney disease : Defining clinical cut-offs for albumin:creatinine ratio

    NARCIS (Netherlands)

    Bakker, Stephan J L

    2013-01-01

    Albuminuria is rapidly gaining recognition as a marker of the presence and of the progression of chronic kidney disease (CKD). In a new study, Naresh et al. attempt to define cut-off values for percentage change in urinary albumin:creatinine ratio that reflect changes in CKD status rather than rando

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

    Directory of Open Access Journals (Sweden)

    Saurabh Bobdey

    2016-06-01

    Conclusion: Pretreatment serum albumin levels are of useful prognostic significance in oral cancer patients. Thus, this easily accessible variable may not only serve as a potent marker to predict the outcomes, but more importantly as an indicator for initiating aggressive nutrition intervention in oral cancer patients. [Int J Res Med Sci 2016; 4(6.000: 2135-2141

  13. Interaction of triprolidine hydrochloride with serum albumins: thermodynamic and binding characteristics, and influence of site probes.

    Science.gov (United States)

    Sandhya, B; Hegde, Ashwini H; Kalanur, Shankara S; Katrahalli, Umesha; Seetharamappa, J

    2011-04-01

    The interaction between triprolidine hydrochloride (TRP) to serum albumins viz. bovine serum albumin (BSA) and human serum albumin (HSA) has been studied by spectroscopic methods. The experimental results revealed the static quenching mechanism in the interaction of TRP with protein. The number of binding sites close to unity for both TRP-BSA and TRP-HSA indicated the presence of single class of binding site for the drug in protein. The binding constant values of TRP-BSA and TRP-HSA were observed to be 4.75 ± 0.018 × 10(3) and 2.42 ± 0.024 × 10(4)M(-1) at 294 K, respectively. Thermodynamic parameters indicated that the hydrogen bond and van der Waals forces played the major role in the binding of TRP to proteins. The distance of separation between the serum albumin and TRP was obtained from the Förster's theory of non-radioactive energy transfer. The metal ions viz., K(+), Ca(2+), Co(2+), Cu(2+), Ni(2+), Mn(2+) and Zn(2+) were found to influence the binding of the drug to protein. Displacement experiments indicated the binding of TRP to Sudlow's site I on both BSA and HSA. The CD, 3D fluorescence spectra and FT-IR spectral results revealed the changes in the secondary structure of protein upon interaction with TRP.

  14. Preparation of albumin nanospheres loaded with gemcitabine and their cytotoxicity against BXPC-3 cells in vitro

    Institute of Scientific and Technical Information of China (English)

    Jin-ming LI; Wei CHEN; Hao WANG; Chen JIN; Xian-jun YU; Wei-yue LU; Long CUI; De-liang FU; Quan-xing NI; Hui-min HOU

    2009-01-01

    Aim: To optimize formulation methods for loading gemcitabine(GEM), the main drug against pancreatic cancer, into albumin nanopar-ticles for extended blood circulation and improved efficacy. Methods: GEM was loaded into two sizes of disolvation-crosslinked bovine serum albumin nanoparticles, with a mean diameter of 109.7 nm and 405.6 nm, respectively, by co-precipitation (the direct method) and follow-up adsorption (the indirect method). The anti-tumor activities of the two nanoparticulate formulations, were evaluated according to their anti-proliferative effects on the human pan-creatic cell line BXPC-3, which were assessed using the MTT assay. Results: The two nanoparticulate formulations, created by direct co-precipitation and indirect adsorption, possessed smooth surfaces and high drug loading efficiencies, 83% and 93% at 11% and 13% drug loading, respectively. The two formulations released GEM for 8 and 12 h, respectively, and significantly improved anti-BXPC-3 proliferation effects, as compared with the GEM solution and the drug-free albumin particles. Conclusion: Co-precipitating and adsorbing GEM into albumin particles resulted in sustained-release nanoparticulate formulations with improved antitumor cytotoxicity. The result suggests that this is a useful formulation strategy for improving the antitumor efficacy of GEM.

  15. Normal urinary albumin excretion in recently diagnosed type 1 diabetic patients

    DEFF Research Database (Denmark)

    Lind, B; Jensen, T; Feldt-Rasmussen, B;

    1989-01-01

    The urinary excretion of albumin and retinol binding protein were measured in 51 recently diagnosed Type 1 diabetic patients and 48 control subjects, matched for age and sex. The diabetic patients, admitted consecutively to the Steno Memorial Hospital, were all studied 3 to 6 months after the ons...

  16. Photosensitizer-Conjugated Human Serum Albumin Nanoparticles for Effective Photodynamic Therapy

    Directory of Open Access Journals (Sweden)

    Hayoung Jeong, MyungSook Huh, So Jin Lee, Heebeom Koo, Ick Chan Kwon, Seo Young Jeong, Kwangmeyung Kim

    2011-01-01

    Full Text Available Photodynamic therapy (PDT is an emerging theranostic modality for various cancers and diseases. The focus of this study was the development of tumor-targeting albumin nanoparticles containing photosensitizers for efficient PDT. To produce tumor-targeting albumin nanoparticles, the hydrophobic photosensitizer, chlorin e6 (Ce6, was chemically conjugated to human serum albumin (HSA. The conjugates formed self-assembled nanoparticle structures with an average diameter of 88 nm under aqueous conditions. As expected, the Ce6-conjugated HSA nanoparticles (Ce6-HSA-NPs were nontoxic in their native state, but upon illumination with the appropriate wavelength of light, they produced singlet oxygen and damaged target tumor cells in a cell culture system. Importantly, when the nanoparticles were injected through the tail vein into tumor-bearing HT-29 mice, Ce6-HSA-NPs compared with free Ce6 revealed enhanced tumor-specific biodistribution and successful therapeutic results following laser irradiation. These results suggest that highly tumor-specific albumin nanoparticles have the potential to serve not only as efficient therapeutic agents, but also as photodynamic imaging (PDI reagents in cancer treatment.

  17. 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.

  18. The Effect of Turmeric , Cardamom and Ginger on in vitro Albumin Glycation

    Directory of Open Access Journals (Sweden)

    N. Sheikh

    2004-01-01

    Full Text Available Diabetes mellitus is one of the most common disease in the world that imposes a tremendous health and societal burden whether that burden is measured in terms of sickness , use of health systems resources or costs. Hyperglycemia is the most important clinical sign of diabetes leading to glycation of the various proteins in the body that leads to change in their nature , structure and biochemical activity. One of the probable methods in the treatment of diabetes mellitus is decrease or inhibition of this reaction. It seems that Turmeric , Cardamom and Ginger are useful for this purpose. The main goal of this research is to determine the effect of above agents on in vitro albumin glycation. In the presence of various concentration of these agents , albumin was glycated and evaluated using TBA method. Results showed that these food additives have inhibitory effects on albumin glycation reaction with the concentraction of 1 g/dl , 0.2 g/dl and 0.1 g/dl. Among these agents , Ginger had the most inhibitory effect (78% with the concentration of 1 g/dl. The sequence of effect is : Ginger > Cardamom > Turmeric These findings showed that these agents decrease albumin glycation reaction.

  19. [Kinetics of serum albumin adsorption on the macroporous glass MPS-250 GKH].

    Science.gov (United States)

    Naumova, L V; El'Kin, G E; Dmitrenko, L V

    1996-01-01

    Intrinsic diffusion (defined as diffusion within micropores or microgranules) was shown to be a major factor that determines the kinetics of bovine serum albumin adsorption to macroporous silica MPS-250 GKh. The effective coefficient of intrinsic diffusion (within the silica phase) was calculated (Def = 7 x 10(-7) cm2/s).

  20. Reversibility of structural rearrangements in bovine serum albumin during homomolecular exchange from AgI particles

    NARCIS (Netherlands)

    Vermonden, T; Giacomelli, CE; Norde, W

    2001-01-01

    The reversibility of the homomolecular exchange of bovine serum albumin (BSA) from AgI particles was studied by differential scanning calorimetry, the binding of 8-anilino-1-naphthaIene-sulfonic acid, and circular dichroism spectroscopy. The structure of BSA in solution before adsorption, in the ads

  1. Urinary albumin and beta 2-microglobulin excretion rates in patients with systemic lupus erythematosus

    DEFF Research Database (Denmark)

    Parving, H H; Sørensen, S F; Mogensen, C E

    1980-01-01

    The daily urinary albumin and beta 2-microglobulin excretion rates were measured with sensitive radioimmunoassays in 14 patients with systemic lupus erythematosus (SLE). The duration of SLE ranged from 0.5 to 18 years, mean 10 years. The mean age was 37 years. All patients except 5 received...

  2. 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.

  3. Peroxidase mediated conjugation of corn fibeer gum and bovine serum albumin to improve emulsifying properties

    Science.gov (United States)

    The emulsifying properties of corn fiber gum (CFG), a naturally-occurring polysaccharide protein complex, were improved by kinetically controlled formation of hetero-covalent linkages with bovine serum albumin (BSA), using horseradish peroxidase. The formation of hetero-crosslinked CFG-BSA conjugate...

  4. A Comparative Analysis of Synonymous Codon Usage Bias Pattern in Human Albumin Superfamily

    Directory of Open Access Journals (Sweden)

    Hoda Mirsafian

    2014-01-01

    Full Text Available Synonymous codon usage bias is an inevitable phenomenon in organismic taxa across the three domains of life. Though the frequency of codon usage is not equal across species and within genome in the same species, the phenomenon is non random and is tissue-specific. Several factors such as GC content, nucleotide distribution, protein hydropathy, protein secondary structure, and translational selection are reported to contribute to codon usage preference. The synonymous codon usage patterns can be helpful in revealing the expression pattern of genes as well as the evolutionary relationship between the sequences. In this study, synonymous codon usage bias patterns were determined for the evolutionarily close proteins of albumin superfamily, namely, albumin, α-fetoprotein, afamin, and vitamin D-binding protein. Our study demonstrated that the genes of the four albumin superfamily members have low GC content and high values of effective number of codons (ENC suggesting high expressivity of these genes and less bias in codon usage preferences. This study also provided evidence that the albumin superfamily members are not subjected to mutational selection pressure.

  5. Characterization of the Interaction between Bovine Serum Albumin and Lomefloxacin by Capillary Zone Electrophoresis

    Institute of Scientific and Technical Information of China (English)

    Ming GUO; Qing Sen YU; Jian Wei YAN; Fei TAN; Guo Zheng MA

    2004-01-01

    Three capillary zone electrophoresis (CZE) methods of the frontal analysis (FA), vacancy peak (VP) and simplified Hummel-Dreyer (SHD) were applied to investigate interaction between bovine serum albumin (BSA) and lomefloxacin, the experimental condition was established after a large number of tests. Based on the site-binding model, the binding parameters were measured according to the site model by Scatchard.

  6. Single-pass albumin dialysis in a child aged six months with phenobarbital poisoning.

    Science.gov (United States)

    Kıhtır, Hasan Serdar; Yıldırım, Hamdi Murat; Yeşilbaş, Osman; Duramaz, Burcu Bursal; Şevketoğlu, Esra

    2016-12-01

    A girl aged six months was hospitalized because of resistant seizures and was discharged with phenobarbital and carbamazepine therapy. She was admitted to a state hospital with symptoms of inability to waken and difficulty in breathing. It was learned that phenobarbital had been used incorrectly and the patient was sent to our pediatric intensive care unit because of severe phenobarbital overdose. The decision was taken for hemodialysis. Single-pass albumin dialysis was planned because phenobarbital can bind to high levels of plasma protein. The process was undertaken with 1% albumin-containing dialysate, which was prepared manually. After 6 hours of dialysis, the phenobarbital blood level measured 62 mcg/mL (>140 mcg/mL on admission) and the patient's clinical findings were markedly regressed. There are no case reports about phenobarbital overdose treated with single-pass albumin dialysis in the literature. We conclude that single-pass albumin dialysis may be a useful treatment, especially with intoxications of drugs that bind protein at high levels.

  7. Development of enzyme-linked immunosorbent assay for estimation of urinary albumin.

    Science.gov (United States)

    Shrivastav, Tulsidas G; Kariya, Kiran P; Prasad, Pramod K V; Chaube, Shail K; Kumar, Dinesh

    2014-01-01

    Yearly estimation of urinary albumin is a prerequisite for predicting renal status in Diabetes Type II patients with negative dipstick results for overt proteinuria. A simple, sensitive, and cost-effective enzyme linked immunosorbent assay (ELISA) for urinary albumin has been developed using human serum albumin antiserum (HSA-antiserum), HSA-biotin, and streptavidin-horseradish peroxidase (SA-HRP) conjugates. To the antibody-coated wells, 100 μL of HSA standards followed by 1:100 diluted urine samples in duplicate were added and then 50 μL of HSA-biotin conjugates was added in all the wells. 100 μL of SA-HRP was added after washing. Bound enzyme activity was measured by adding 100 μL TMB/H2O2. The analytical sensitivity and ED50 of the developed method was found to be 0.01 μg/mL and 0.35 μg/mL, respectively. The percent recovery of the HSA from exogenously spiked urine pools were in the range of 98.13-100.29%. The intra- and inter-assay coefficient of variation (CVs) ranged from 3.38-10.32 % and 4.22-11.01%, respectively. The antibody showed 4.4% and 3.2% cross reactivity with monkey and horse serum albumin, respectively. There was no cross reaction with human β2-microglobulin, γ-globulin, and haemoglobulin.

  8. A spectroscopic and molecular docking approach on the binding of tinzaparin sodium with human serum albumin

    Science.gov (United States)

    Abdullah, Saleh M. S.; Fatma, Sana; Rabbani, Gulam; Ashraf, Jalaluddin M.

    2017-01-01

    Protein bound toxins are poorly removed by conventional extracorporeal therapies. Venous thromboembolism (VTE) is a major cause of morbidity and mortality in patients with cancer. The interaction between tinzaparin, an inhibitor of angiotensin converting enzyme and human serum albumin, a principal plasma protein in the liver has been investigated in vitro under a simulated physiological condition by UV-vis spectrophotometry and fluorescence spectrometry. The intrinsic fluorescence intensity of human serum albumin was strongly quenched by tinzaparin (TP). The binding constants and binding stoichiometry can be calculated from the data obtained from fluorescence quenching experiments. The negative value of ΔG° reveals that the binding process is a spontaneous process. Thermodynamic analysis shows that the HSA-TP complex formation occurs via hydrogen bonds, hydrophobic interactions and undergoes slight structural changes as evident by far-UV CD. It indicated that the hydrophobic interactions play a main role in the binding of TP to human serum albumin. In addition, the distance between TP (acceptor) and tryptophan residues of human serum albumin (donor) was estimated to be 2.21 nm according to the Förster's resonance energy transfer theory. For the deeper understanding of the interaction, thermodynamic, and molecular docking studies were performed as well. Our docking results suggest that TP forms stable complex with HSA (Kb ∼ 104) and its primary binding site is located in subdomain IIA (Sudlow Site I). The results obtained herein will be of biological significance in pharmacology and clinical medicine.

  9. Effect of vitamin E in the treatment of bovine-albumin-induced uveitis in rabbits.

    Science.gov (United States)

    Yücel, I; Paksoy, N; Yücel, G; Aksu, G; Aksu, T A

    1992-01-01

    In order to assess the role of vitamin E, an antioxidant, in the treatment of uveitis, a controlled experimental study was carried out on 20 New Zealand albino rabbits with bovine-albumin-induced uveitis. In all vitamin-E-treated animals, clinical and histopathological study of the retina and uvea revealed no significant changes in comparison with those in untreated rabbits.

  10. Adsorption of albumin and sodium hyaluronate on UHMWPE: a QCM-D and AFM study.

    Science.gov (United States)

    Serro, A P; Degiampietro, K; Colaço, R; Saramago, B

    2010-06-15

    The biotribological properties of artificial joints, in particular the efficiency of the lubrication, strongly determine their lifetime. The most commonly used artificial joints combine a metallic or ceramic part articulating against a ultra high molecular weight polyethylene (UHMWPE) counterface, and are lubricated by the periprosthetic fluid. This fluid contains several macromolecules, namely albumin and sodium hyaluronate (NaHA), that are known to be involved in the lubrication process. There are several studies in the literature concerning the interaction of the referred macromolecules with ceramic or metallic prosthetic materials. However, to our knowledge, information about their binding to the polymeric surface is practically inexistent. The objective of this work is to contribute to clarify the role played by albumin and NaHA on the biolubrication process, through the investigation of their interaction with the UHMWPE surface. The study involves adsorption measurements using a quartz crystal microbalance with dissipation (QCM-D), the characterization of the adsorbed films by atomic force microscopy (AFM) and wettability determinations. Albumin was found to adsorb strongly and extensively to the polymer, while NaHA led to a very low adsorption. In both cases rigid films were obtained, but with different morphology and porosity. The high binding affinity of the protein to the polymer was demonstrated both by the results of the fittings to Langmuir and Freundlich models and by the values of the adhesion forces determined by AFM. In the simultaneous adsorption of albumin and NaHA, protein adsorption is predominant and determines the surface properties.

  11. Synthesis of Metal Porphyrins Tailed with Salicylic Acid and their Interaction with Bovine Serum Albumin

    Institute of Scientific and Technical Information of China (English)

    Tao JIA; Kai WANG; Yi Mei ZHAO; Zao Ying LI

    2004-01-01

    A synthetic method of porphyrins tailed with salicylic substituents is described. Reaction of bromoalkoxyphenyl porphyrin 1 with salicylic acid gave porphyrins 2~5. These new compounds were confirmed by 1H NMR, IR, UV-vis, MS and elemental analysis, and observed their interaction with bovine serum albumin (BSA) in fluorescence spectrum.

  12. POTENT INVITRO ANTI-HUMAN IMMUNODEFICIENCY VIRUS-1 ACTIVITY OF MODIFIED HUMAN SERUM ALBUMINS

    NARCIS (Netherlands)

    JANSEN, RW; MOLEMA, G; PAUWELS, R; SCHOLS, D; DECLERCQ, E; MEIJER, DKF

    1991-01-01

    A series of neoglycoproteins was synthesized by coupling of thiophosgene-activated p-aminophenyl derivatives [Biol. Cell. 47:95-110 (1983); J. Histochem. Cytochem. 32:1091-1094 (1984)] of various sugars to human serum albumin. The compounds were evaluated for their in vitro activity against human im

  13. Albumin Enhances Caspofungin Activity against Aspergillus Species by Facilitating Drug Delivery to Germinating Hyphae.

    Science.gov (United States)

    Ioannou, Petros; Andrianaki, Aggeliki; Akoumianaki, Tonia; Kyrmizi, Irene; Albert, Nathaniel; Perlin, David; Samonis, George; Kontoyiannis, Dimitrios P; Chamilos, Georgios

    2015-12-07

    The modest in vitro activity of echinocandins against Aspergillus implies that host-related factors augment the action of these antifungal agents in vivo. We found that, in contrast to the other antifungal agents (voriconazole, amphotericin B) tested, caspofungin exhibited a profound increase in activity against various Aspergillus species under conditions of cell culture growth, as evidenced by a ≥4-fold decrease in minimum effective concentrations (MECs) (P = 0. 0005). Importantly, the enhanced activity of caspofungin against Aspergillus spp. under cell culture conditions was strictly dependent on serum albumin and was not observed with the other two echinocandins, micafungin and anidulafungin. Of interest, fluorescently labeled albumin bound preferentially on the surface of germinating Aspergillus hyphae, and this interaction was further enhanced upon treatment with caspofungin. In addition, supplementation of cell culture medium with albumin resulted in a significant, 5-fold increase in association of fluorescently labeled caspofungin with Aspergillus hyphae (P caspofungin, with albumin acting as a potential carrier molecule to facilitate antifungal drug delivery to Aspergillus hyphae.

  14. FORMATION OF HEMOGLOBIN AND ALBUMIN ADDUCTS OF BENZENE OXIDE IN MOUSE, RAT, AND HUMAN BLOOD

    Science.gov (United States)

    Little is known about the formation and disposition of benzene oxide (BO), the initial metabolite arising from oxidation of benzene by cytochrome P450. In this study, reactions of BO with hemoglobin (Hb) and albumin (Alb) were investigated in blood from B6C3F1 mice, F344 rats, ...

  15. Genome-wide association study of urinary albumin excretion rate in patients with type 1 diabetes

    DEFF Research Database (Denmark)

    Sandholm, Niina; Forsblom, Carol; Mäkinen, Ville-Petteri;

    2014-01-01

    AIMS/HYPOTHESIS: An abnormal urinary albumin excretion rate (AER) is often the first clinically detectable manifestation of diabetic nephropathy. Our aim was to estimate the heritability and to detect genetic variation associated with elevated AER in patients with type 1 diabetes. METHODS: The di...

  16. Preoperative albumin level is a marker of alveolar echinococcosis recurrence after hepatectomy

    Science.gov (United States)

    Joliat, Gaëtan-Romain; Labgaa, Ismail; Demartines, Nicolas; Halkic, Nermin

    2017-01-01

    AIM To identify a preoperative blood marker predictive of alveolar echinococcosis (AE) recurrence after hepatectomy. METHODS All consecutive patients who underwent operation for liver AE at the Lausanne University Hospital (CHUV) between January 1992 and December 2015 were included in this retrospective study. Preoperative laboratory values of leukocytes, mean corpuscular volume (MCV), red blood cell distribution width (RDW), thrombocytes, C-reactive protein (CRP) and albumin were collected and analyzed. Univariate and multivariate Cox regression analyses were performed to determine the risk factors for AE recurrence after liver resection. A receiver operating characteristic (ROC) curve was used to define the best discrimination threshold of the blood marker. Moreover, recurrence-free survival curves were calculated using the Kaplan-Meier method. RESULTS The cohort included 68 adult patients (37 females) with median age of 61 years [interquartile range (IQR): 46-71]. Eight of the patients (12%) presented a recurrence over a median follow-up time of 76 mo (IQR: 34-128). Median time to recurrence was 10 mo (IQR: 6-11). Median preoperative leukocyte, MCV, RDW, thrombocyte and CRP levels were similar between recurrent and non-recurrent cases. Median preoperative albumin level was 43 g/L (IQR: 41-45) for non-recurrent cases and 36 g/L (IQR: 33-42) for recurrent cases (P = 0.005). The area under the ROC curve for preoperative albumin level to predict recurrence was 0.840 (95%CI: 0.642-1, P = 0.002). The cut-off albumin level value was 37.5 g/L for sensitivity of 94.5% and specificity of 75%. In multivariate analysis, preoperative albumin and surgical resection margins were independent predictors of AE recurrence (HR = 0.099, P = 0.007 and HR = 0.182, P = 0.045 respectively). CONCLUSION Low preoperative albumin level was associated with AE recurrence in the present cohort. Thus, preoperative albumin may be a useful biomarker to guide follow-up. PMID:28223729

  17. Mesenchymal stem cells modulate albumin-induced renal tubular inflammation and fibrosis.

    Directory of Open Access Journals (Sweden)

    Hao Jia Wu

    Full Text Available Bone marrow-derived mesenchymal stem cells (BM-MSCs have recently shown promise as a therapeutic tool in various types of chronic kidney disease (CKD models. However, the mechanism of action is incompletely understood. As renal prognosis in CKD is largely determined by the degree of renal tubular injury that correlates with residual proteinuria, we hypothesized that BM-MSCs may exert modulatory effects on renal tubular inflammation and epithelial-to-mesenchymal transition (EMT under a protein-overloaded milieu. Using a co-culture model of human proximal tubular epithelial cells (PTECs and BM-MSCs, we showed that concomitant stimulation of BM-MSCs by albumin excess was a prerequisite for them to attenuate albumin-induced IL-6, IL-8, TNF-α, CCL-2, CCL-5 overexpression in PTECs, which was partly mediated via deactivation of tubular NF-κB signaling. In addition, albumin induced tubular EMT, as shown by E-cadherin loss and α-SMA, FN and collagen IV overexpression, was also prevented by BM-MSC co-culture. Albumin-overloaded BM-MSCs per se retained their tri-lineage differentiation capacity and overexpressed hepatocyte growth factor (HGF and TNFα-stimulating gene (TSG-6 via P38 and NF-κB signaling. Albumin-induced tubular CCL-2, CCL-5 and TNF-α overexpression were suppressed by recombinant HGF treatment, while the upregulation of α-SMA, FN and collagen IV was attenuated by recombinant TSG-6. Neutralizing HGF and TSG-6 abolished the anti-inflammatory and anti-EMT effects of BM-MSC co-culture in albumin-induced PTECs, respectively. In vivo, albumin-overloaded mice treated with mouse BM-MSCs had markedly reduced BUN, tubular CCL-2 and CCL-5 expression, α-SMA and collagen IV accumulation independent of changes in proteinuria. These data suggest anti-inflammatory and anti-fibrotic roles of BM-MSCs on renal tubular cells under a protein overloaded condition, probably mediated via the paracrine action of HGF and TSG-6.

  18. Mesenchymal stem cells modulate albumin-induced renal tubular inflammation and fibrosis.

    Science.gov (United States)

    Wu, Hao Jia; Yiu, Wai Han; Li, Rui Xi; Wong, Dickson W L; Leung, Joseph C K; Chan, Loretta Y Y; Zhang, Yuelin; Lian, Qizhou; Lin, Miao; Tse, Hung Fat; Lai, Kar Neng; Tang, Sydney C W

    2014-01-01

    Bone marrow-derived mesenchymal stem cells (BM-MSCs) have recently shown promise as a therapeutic tool in various types of chronic kidney disease (CKD) models. However, the mechanism of action is incompletely understood. As renal prognosis in CKD is largely determined by the degree of renal tubular injury that correlates with residual proteinuria, we hypothesized that BM-MSCs may exert modulatory effects on renal tubular inflammation and epithelial-to-mesenchymal transition (EMT) under a protein-overloaded milieu. Using a co-culture model of human proximal tubular epithelial cells (PTECs) and BM-MSCs, we showed that concomitant stimulation of BM-MSCs by albumin excess was a prerequisite for them to attenuate albumin-induced IL-6, IL-8, TNF-α, CCL-2, CCL-5 overexpression in PTECs, which was partly mediated via deactivation of tubular NF-κB signaling. In addition, albumin induced tubular EMT, as shown by E-cadherin loss and α-SMA, FN and collagen IV overexpression, was also prevented by BM-MSC co-culture. Albumin-overloaded BM-MSCs per se retained their tri-lineage differentiation capacity and overexpressed hepatocyte growth factor (HGF) and TNFα-stimulating gene (TSG)-6 via P38 and NF-κB signaling. Albumin-induced tubular CCL-2, CCL-5 and TNF-α overexpression were suppressed by recombinant HGF treatment, while the upregulation of α-SMA, FN and collagen IV was attenuated by recombinant TSG-6. Neutralizing HGF and TSG-6 abolished the anti-inflammatory and anti-EMT effects of BM-MSC co-culture in albumin-induced PTECs, respectively. In vivo, albumin-overloaded mice treated with mouse BM-MSCs had markedly reduced BUN, tubular CCL-2 and CCL-5 expression, α-SMA and collagen IV accumulation independent of changes in proteinuria. These data suggest anti-inflammatory and anti-fibrotic roles of BM-MSCs on renal tubular cells under a protein overloaded condition, probably mediated via the paracrine action of HGF and TSG-6.

  19. Relationship between serum albumin and pulse wave velocity in patients on continuous ambulatory peritoneal dialysis

    Directory of Open Access Journals (Sweden)

    Li-Tao Cheng

    2008-08-01

    Full Text Available Li-Tao Cheng1, Li-Jun Tang1,2, Hui-Min Chen1,3, Wen Tang1, Tao Wang11Division of Nephrology, Peking University Third Hospital, Beijing, China; 2Division of Nephrology, Qilu Hospital of Shandong University, Ji’nan, China; 3Division of Cardiology, Guangdong Provincial Hospital of Traditional Chinese Medicine, Guangzhou, ChinaBackground: Hypoalbuminemia is a risk factor for cardiovascular events and mortality in dialysis patients, but the underlying mechanism remains unclear. Meanwhile, increased pulse wave velocity (PWV, the marker of arterial stiffness, has been proved to be an independent predictor of cardiovascular disease. The relationship between serum albumin and PWV in continuous ambulatory peritoneal dialysis patients (CAPD was studied.Methods: Sixty-two CAPD patients were studied. The average age was 63 ± 12 years and dialysis duration was 23 ± 22 months. Serum albumin, C-reactive protein (CRP, and carotid-femoral PWV were measured.Results: Among these patients, 43.5% were men. The mean serum albumin concentration was 37 ± 4 g/L and PWV was 11.9 ± 2.3 m/s. PWV positively correlated with age (r = 0.35, P < 0.01, diabetes (yes = 1, no = 0; r = 0.292, P < 0.05, systolic blood pressure (SBP; r = 0.493, P < 0.001 and CRP (r = 0.295, P < 0.05, but negatively correlated with serum albumin (r = −0.357, P < 0.01. In multiple regression analysis, SBP (β = 0.615, P < 0.001, age (β = 0.414, P < 0.01, albumin (β = −0.315, P < 0.05 and total cholesterol (β = 0.275, P < 0.05 were independent determinants of PWV. In a non-inflamed subgroup (CRP < 3 mg/L, n = 30, albumin still negatively correlated with PWV (r = −0.66, P < 0.001.Conclusion: Serum albumin inversely correlated with increased PWV in CAPD patients, suggesting that increased arterial stiffness might be the link between hypoalbuminemia and increased cardiovascular mortality in dialysis patients.Keywords: hypoalbuminemia, cardiovascular events, pulse wave velocity, arterial

  20. Effect of glucagon on cyclic AMP, albumin metabolism and incorporation of 14C-leucine into proteins in isolated parenchymal rat liver cells

    DEFF Research Database (Denmark)

    Dich, J; Gluud, C N

    1976-01-01

    wet wt. This is about the rate found in the perfused liver, Glucagon (10(-8-10(-6) M) inhibited albumin secretion and the incorporation of 14C-leucine into albumin, into total proteins in the medium and into total proteins in the cell suspension. The effect of glucagon on albumin secretion...

  1. Albumin synthesis in humans increases immediately following the administration of endotoxin.

    Science.gov (United States)

    Barle, Hans; Januszkiewicz, Anna; Hållström, Lars; Essén, Pia; McNurlan, Margaret A; Garlick, Peter J; Wernerman, Jan

    2002-11-01

    In order to investigate the immediate (i.e. within 3 h) response of albumin synthesis to the administration of endotoxin, as a model of a moderate and well controlled catabolic insult, two measurements employing L-[(2)H(5)]phenylalanine were performed in 16 volunteers. One group ( n =8) received an intravenous injection of endotoxin (4 ng/kg; lot EC-6) immediately after the first measurement of albumin synthesis, whereas the other group received saline. A second measurement was initiated 1 h later. In the endotoxin group, the fractional synthesis rate of albumin was 6.9+/-0.6%/day (mean+/-S.D.) in the first measurement. In the second measurement, a significant increase was observed (9.6+/-1.2%/day; P <0.001). The corresponding values in the control group were were 6.6+/-0.6%/day and 7.0+/-0.6%/day respectively (not significant compared with first measurement and P <0.001 compared with the second measurement in the endotoxin group). The absolute synthesis rates of albumin were 148+/-35 and 201+/-49 mg x kg(-1) x day(-1) before and after endotoxin ( P <0.01). In the control group, the corresponding values were 131+/-21 and 132+/-20 mg x kg(-1) x day(-1) (not significant compared with the first measurement and P <0.01 compared with the second measurement in the endotoxin group). In conclusion, these results indicate that albumin synthesis increases in the very early phase after a catabolic insult, as represented by the administration of endotoxin.

  2. Protein-thiol substitution or protein dethiolation by thiol/disulfide exchange reactions: the albumin model.

    Science.gov (United States)

    Summa, Domenico; Spiga, Ottavia; Bernini, Andrea; Venditti, Vincenzo; Priora, Raffaella; Frosali, Simona; Margaritis, Antonios; Di Giuseppe, Danila; Niccolai, Neri; Di Simplicio, Paolo

    2007-11-01

    Dethiolation experiments of thiolated albumin with thionitrobenzoic acid and thiols (glutathione, cysteine, homocysteine) were carried out to understand the role of albumin in plasma distribution of thiols and disulfide species by thiol/disulfide (SH/SS) exchange reactions. During these experiments we observed that thiolated albumin underwent thiol substitution (Alb-SS-X+RSHAlb-SS-R+XSH) or dethiolation (Alb-SS-X+XSHAlb-SH+XSSX), depending on the different pK(a) values of thiols involved in protein-thiol mixed disulfides (Alb-SS-X). It appeared in these reactions that the compound with lower pK(a) in mixed disulfide was a good leaving group and that the pK(a) differences dictated the kind of reaction (substitution or dethiolation). Thionitrobenzoic acid, bound to albumin by mixed disulfide (Alb-TNB), underwent rapid substitution after thiol addition, forming the corresponding Alb-SS-X (peaks at 0.25-1 min). In turn, Alb-SS-X were dethiolated by the excess nonprotein SH groups because of the lower pK(a) value in mixed disulfide with respect to that of other thiols. Dethiolation of Alb-SS-X was accompanied by formation of XSSX and Alb-SH up to equilibrium levels at 35 min, which were different for each thiol. Structures by molecular simulation of thiolated albumin, carried out for understanding the role of sulfur exposure in mixed disulfides in dethiolation process, evidenced that the sulfur exposure is important for the rate but not for determining the kind of reaction (substitution or dethiolation). Our data underline the contribution of SH/SS exchanges to determine levels of various thiols as reduced and oxidized species in human plasma.

  3. Cubilin is essential for albumin reabsorption in the renal proximal tubule.

    Science.gov (United States)

    Amsellem, Sabine; Gburek, Jakub; Hamard, Ghislaine; Nielsen, Rikke; Willnow, Thomas E; Devuyst, Olivier; Nexo, Ebba; Verroust, Pierre J; Christensen, Erik I; Kozyraki, Renata

    2010-11-01

    Receptor-mediated endocytosis is responsible for protein reabsorption in the proximal tubule. This process involves two interacting receptors, megalin and cubilin, which form a complex with amnionless. Whether these proteins function in parallel or as part of an integrated system is not well understood. Here, we report the renal effects of genetic ablation of cubilin, with or without concomitant ablation of megalin, using a conditional Cre-loxP system. We observed that proximal tubule cells did not localize amnionless to the plasma membrane in the absence of cubilin, indicating a mutual dependency of cubilin and amnionless to form a functional membrane receptor complex. The cubilin-amnionless complex mediated internalization of intrinsic factor-vitamin B12 complexes, but megalin considerably increased the uptake. Furthermore, cubilin-deficient mice exhibited markedly decreased uptake of albumin by proximal tubule cells and resultant albuminuria. Inactivation of both megalin and cubilin did not increase albuminuria, indicating that the main role of megalin in albumin reabsorption is to drive the internalization of cubilin-albumin complexes. In contrast, cubulin deficiency did not affect urinary tubular uptake or excretion of vitamin D-binding protein (DBP), which binds cubilin and megalin. In addition, we observed cubilin-independent reabsorption of the "specific" cubilin ligands transferrin, CC16, and apoA-I, suggesting a role for megalin and perhaps other receptors in their reabsorption. In summary, with regard to albumin, cubilin is essential for its reabsorption by proximal tubule cells, and megalin drives internalization of cubilin-albumin complexes. These genetic models will allow further analysis of protein trafficking in the progression of proteinuric renal diseases.

  4. Akt Links Insulin Signaling to Albumin Endocytosis in Proximal Tubule Epithelial Cells.

    Directory of Open Access Journals (Sweden)

    Sam Coffey

    Full Text Available Diabetes mellitus (DM has become an epidemic, causing a significant decline in quality of life of individuals due to its multisystem involvement. Kidney is an important target organ in DM accounting for the majority of patients requiring renal replacement therapy at dialysis units. Microalbuminuria (MA has been a valuable tool to predict end-organ damage in DM but its low sensitivity has driven research efforts to seek other alternatives. Albumin is taken up by albumin receptors, megalin and cubilin in the proximal tubule epithelial cells. We demonstrated that insulin at physiological concentrations induce albumin endocytosis through activation of protein kinase B (Akt in proximal tubule epithelial cells. Inhibition of Akt by a phosphorylation deficient construct abrogated insulin induced albumin endocytosis suggesting a role for Akt in insulin-induced albumin endocytosis. Furthermore we demonstrated a novel interaction between Akt substrate 160kDa (AS160 and cytoplasmic tail of megalin. Mice with type 1 DM (T1D displayed decreased Akt, megalin, cubilin and AS160 expression in their kidneys in association with urinary cubilin shedding preceding significant MA. Patients with T1D who have developed MA in the EDC (The Pittsburgh Epidemiology of Diabetes Complications study demonstrated urinary cubilin shedding prior to development of MA. We hypothesize that perturbed insulin-Akt cascade in DM leads to alterations in trafficking of megalin and cubilin, which results in urinary cubilin shedding as a prelude to MA in early diabetic nephropathy. We propose that utilization of urinary cubilin shedding, as a urinary biomarker, will allow us to detect and intervene in diabetic nephropathy (DN at an earlier stage.

  5. Akt Links Insulin Signaling to Albumin Endocytosis in Proximal Tubule Epithelial Cells.

    Science.gov (United States)

    Coffey, Sam; Costacou, Tina; Orchard, Trevor; Erkan, Elif

    2015-01-01

    Diabetes mellitus (DM) has become an epidemic, causing a significant decline in quality of life of individuals due to its multisystem involvement. Kidney is an important target organ in DM accounting for the majority of patients requiring renal replacement therapy at dialysis units. Microalbuminuria (MA) has been a valuable tool to predict end-organ damage in DM but its low sensitivity has driven research efforts to seek other alternatives. Albumin is taken up by albumin receptors, megalin and cubilin in the proximal tubule epithelial cells. We demonstrated that insulin at physiological concentrations induce albumin endocytosis through activation of protein kinase B (Akt) in proximal tubule epithelial cells. Inhibition of Akt by a phosphorylation deficient construct abrogated insulin induced albumin endocytosis suggesting a role for Akt in insulin-induced albumin endocytosis. Furthermore we demonstrated a novel interaction between Akt substrate 160kDa (AS160) and cytoplasmic tail of megalin. Mice with type 1 DM (T1D) displayed decreased Akt, megalin, cubilin and AS160 expression in their kidneys in association with urinary cubilin shedding preceding significant MA. Patients with T1D who have developed MA in the EDC (The Pittsburgh Epidemiology of Diabetes Complications) study demonstrated urinary cubilin shedding prior to development of MA. We hypothesize that perturbed insulin-Akt cascade in DM leads to alterations in trafficking of megalin and cubilin, which results in urinary cubilin shedding as a prelude to MA in early diabetic nephropathy. We propose that utilization of urinary cubilin shedding, as a urinary biomarker, will allow us to detect and intervene in diabetic nephropathy (DN) at an earlier stage.

  6. Current position of vasoconstrictor and albumin infusion for type 1 hepatorenal syndrome

    Institute of Scientific and Technical Information of China (English)

    Abhasnee; Sobhonslidsuk

    2015-01-01

    Spontaneous bacterial peritonitis(SBP),refractory ascites,hepatorenal syndrome(HRS),hyponatremia and hepatic encephalopathy are complicationswhich frequently happen during a clinical course of decompensated cirrhosis.Splanchnic and peripheral vasodilatation,increased intrarenal vasoconstriction and impaired cardiac responsive function are pathological changes causing systemic and hemodynamic derangement.Extreme renal vasoconstriction leads to severe reduction of renal blood flow and glomerular filtration rate,which finally evolves into the clinical feature of HRS.Clinical manifestations of type 1 and type 2 HRS come to medical attention differently.Patients with type1 HRS present as acute kidney injury whereas those with type 2 HRS will have refractory ascites as the leading problem.Prompt diagnosis of type 1 HRS can halt the progression of HRS to acute tubular necrosis if the combined treatment of albumin infusion and vasoconstrictors is started timely.HRS reversal was seen in 34%-60%of patients,followed with decreasing mortality.Baseline serum levels of creatinine less than5 mg/dL,bilirubin less than 10 mg/dL,and increased mean arterial pressure of over 5 mmHg by day 3 of the combined treatment of vasoconstrictor and albumin are the predictors of good response.Type 1 HRS can be prevented in some conditions such as albumin infusion in SBP,prophylactic antibiotics for upper gastrointestinal hemorrhage,albumin replacement after large volume paracentesis in cirrhotic patients with massive ascites.The benefit of albumin infusion in infection with primary source other than SBP requires more studies.

  7. Albumin induces upregulation of matrix metalloproteinase-9 in astrocytes via MAPK and reactive oxygen species-dependent pathways

    Directory of Open Access Journals (Sweden)

    Ranaivo Hantamalala

    2012-04-01

    Full Text Available Abstract Background Astrocytes are an integral component of the blood–brain barrier (BBB which may be compromised by ischemic or traumatic brain injury. In response to trauma, astrocytes increase expression of the endopeptidase matrix metalloproteinase (MMP-9. Compromise of the BBB leads to the infiltration of fluid and blood-derived proteins including albumin into the brain parenchyma. Albumin has been previously shown to activate astrocytes and induce the production of inflammatory mediators. The effect of albumin on MMP-9 activation in astrocytes is not known. We investigated the molecular mechanisms underlying the production of MMP-9 by albumin in astrocytes. Methods Primary enriched astrocyte cultures were used to investigate the effects of exposure to albumin on the release of MMP-9. MMP-9 expression was analyzed by zymography. The involvement of mitogen-activated protein kinase (MAPK, reactive oxygen species (ROS and the TGF-β receptor-dependent pathways were investigated using pharmacological inhibitors. The production of ROS was observed by dichlorodihydrofluorescein diacetate fluorescence. The level of the MMP-9 inhibitor tissue inhibitor of metalloproteinase (TIMP-1 produced by astrocytes was measured by ELISA. Results We found that albumin induces a time-dependent release of MMP-9 via the activation of p38 MAPK and extracellular signal regulated kinase, but not Jun kinase. Albumin-induced MMP-9 production also involves ROS production upstream of the MAPK pathways. However, albumin-induced increase in MMP-9 is independent of the TGF-β receptor, previously described as a receptor for albumin. Albumin also induces an increase in TIMP-1 via an undetermined mechanism. Conclusions These results link albumin (acting through ROS and the p38 MAPK to the activation of MMP-9 in astrocytes. Numerous studies identify a role for MMP-9 in the mechanisms of compromise of the BBB, epileptogenesis, or synaptic remodeling after ischemia or

  8. Distribution of albumin variants Naskapi amd Mexico among Aleuts, Frobisher Bay Eskimos, and Micmac, Naskapi, Mohawk, Omaha, and Apache Indians.

    Science.gov (United States)

    Schell, L M; Agarwal, S S; Blumberg, B S; Levy, H; Bennett, P H; Laughlin, W S; Martin, J P

    1978-07-01

    In order to help define the boundaries of the distribution of the albumin variants Naskapi and Mexico which are polymorphic among several American Indian groups, we examined sera from Micmac, Mohawk, Northwest River Naskapi, Omaha and Apache Indians, and from Aleuts and Eskimos. Sera from a total of 1,524 individuals were examined. Using a cellulose acetate membrane electrophoretic system with Tris-Citric acid at pH 5.4 we were able to distinguish normal albumin and both variants in the same run. Naskapi and Mexico variants were absent from Aleut, Eskimo, Micmac, Mohawk and Omaha samples. The albumin Naskapi variant was present in an allele frequency of 0.03 in the Naskapi Indian sample. Albumin variants Naskapi and Mexico were found in the Apache sample at frequencies of 0.016 and 0.037, respectively. This report supersedes that previously published by Schell and Agarwal ('76). Generally, within an area there is a correspondence between changes in the frequency of albumin variants and changes in the ethnic background and history of the area's populations. At the same time, when viewing widely separated areas, relationships between distant groups based on linguistic and cultural similarities are paralleled on a biologic level by the distribution of normal albumin and variant albumins.

  9. Albumin modulates lateral assembly of fibrin polymers: evidence of enhanced fine fibril formation and of unique synergism with fibrinogen

    Energy Technology Data Exchange (ETDEWEB)

    Galanakis, D.K.; Lane, B.P.; Simon, S.R.

    1987-04-21

    The authors identified a new property of human albumin. It enhances formation of fine fibril (or leptofibril) structure during fibrin gelation, and by nephelometric and electron microscopic measurements, this property is independent of and synergistic with that of fibrinogen. They examined fibrin aggregation using physiologic temperatures and pH and albumin:fibrin concentration ratios below those at which the known accelerating effect on fibrin aggregation occurs. An albumin concentration dependent decrease in gel turbidity maxima was consistently demonstrable in buffers containing or lacking (2-5 mM) CaCl/sub 2/. Electron microscopic measurements of cross-sectional fibril widths, performed on sections of glutaraldehyde-fixed gels, disclosed differences between albumin-containing and control gels which were significant. Spin-labeled albumin displayed no change in electron (para) magnetic spin resonance spectral measurements during its inhibition of fibrin, indicating no perturbation on albumin conformation in the vicinities of Cys-34 and of fatty acid binding sites. Certain fibrinogen:albumin ratios designed to induce maximal inhibition yet permit gelation in the presence of either alone prevented gelation of buffer-diluted fibrin monomers. Aliquots from these which were dried and negatively stained on formvar-coated grids disclosed strands of 5-17 nm width, most displaying a 60-250-nm approximate length. The amounts of /sup 131/I-labeled coagulable fibrin which remained soluble in fibrinogen solutions were increased by albumin. They conclude that albumin enhances formation of leptofibril-rich gel domains when other plasma factors favor formation of such structures. Available evidence indicating decreased permeability implies that such gel domains limit efflux rates from the intrathrombus environment and from intra- to extravascular space.

  10. Study on Interaction of Ginsenosides with Bovine or Human Serum Albumin Using Wavelength Modulation Surface Plasmon Resonance Biosensor

    Institute of Scientific and Technical Information of China (English)

    LIU Xia; SUN Ying; SONG Da-Qian; LI Xu-Wen; ZHANG Qing-Lin; TIAN Yuan; LIU Zhong-Ying; ZHANG Han-Qi

    2006-01-01

    To use a newly developed wavelength modulation surface plasmon resonance (SPR) biosensor, an experimental protocol was developed to investigate the interaction of ginsenosides with serum albumin. With a known concentration of the ginsenosides, bound percentages of the ginsenosides with human serum albumin (HSA) or bovine serum albumin (BSA) were obtained. SPR technique could require no labeling and this method provided the detailed information on association and disassociation of molecules in real time. The results indicate that the sensitivity of wavelength modulation SPR biosensor is sufficient for detection and characterization of binding events involving low-molecular weight compounds and their immobilized protein targets.

  11. Relationship between in vitro Fe and Zn dialysability and peptide composition of albumin and globulins extracted from cooked bean (Phaseolus vulgaris L.).

    Science.gov (United States)

    Lombardi-Boccia, G; Carbonaro, M; Cappelloni, M; Carnovale, E

    1996-11-01

    In vitro dialysability of iron, zinc and protein was determined from whole bean (Phaseolus vulgaris), albumin and globulin (G1, G2) after cooking. Albumin showed the highest iron, zinc, protein and phytic acid content. Cooking increased iron and protein dialysability only in whole bean and albumin. Compared to globulins, albumin also presented a higher in vitro protein digestibility and cystine chemical reactivity. HPLC analysis of peptides in dialysates of bean and protein fractions suggested that some aggregation occurred during dialysis. The percentage of amino acids in dialysed peptides was found to be different between albumin and globulins. The difference in iron and zinc dialysability between albumin and globulins seems to depend on the phytic acid content of the albumin fraction and the protein properties of globulins.

  12. Ciprofloxacin Loaded Bovine Serum Albumin Microspheres: Prepa-ration and Drug Release Characterization In Vitro

    Institute of Scientific and Technical Information of China (English)

    LiFengqian; HuJinhong; LuBin; ZhuQuangang; SunHuajun

    2001-01-01

    Ciprofloxacin loaded microspheres were prepared by spray drying technique, with bovine serum albumin as the natural biodegradable wall materials. The obtained microspheres, using aqueous system, were organic solvent-free. The diameters of the spherical microspheres were in the range of 1-5 1:4. The drug entrapment of microspheres, formulated with different ciprofloxacin/albumin ratios as 1:1, 1:2 and 1:4, were 46.93%, 32.96% and 20.56% (n=3). And the encapsulation efflciencies for ciprofloxacin during spray drying were higher than 90%. Thermal denaturation programs at different temperatures (100-120℃) for different time intervals (3-6-12 h) were further processed to stabilize the spray-dried microspheres. The higher the extent for thermal denaturation, the slower the rate of ciprofloxacin released from microspheres in vitro. So the release rate of ciprofloxacin from microspheres can be controlled by modifing the conditions of thermal denaturation.

  13. Ligand binding strategies of human serum albumin: how can the cargo be utilized?

    Science.gov (United States)

    Varshney, Ankita; Sen, Priyankar; Ahmad, Ejaz; Rehan, Mohd; Subbarao, Naidu; Khan, Rizwan Hasan

    2010-01-01

    Human serum albumin (HSA), being the most abundant carrier protein in blood and a modern day clinical tool for drug delivery, attracts high attention among biologists. Hence, its unfolding/refolding strategies and exogenous/endogenous ligand binding preference are of immense use in therapeutics and clinical biochemistry. Among its fellow proteins albumin is known to carry almost every small molecule. Thus, it is a potential contender for being a molecular cargo/or nanovehicle for clinical, biophysical and industrial purposes. Nonetheless, its structure and function are largely regulated by various chemical and physical factors to accommodate HSA to its functional purpose. This multifunctional protein also possesses enzymatic properties which may be used to convert prodrugs to active therapeutics. This review aims to highlight current overview on the binding strategies of protein to various ligands that may be expected to lead to significant clinical applications.

  14. Zinc phthalocyanine-conjugated with bovine serum albumin mediated photodynamic therapy of human larynx carcinoma

    Science.gov (United States)

    Silva, E. P. O.; Santos, E. D.; Gonçalves, C. S.; Cardoso, M. A. G.; Soares, C. P.; Beltrame, M., Jr.

    2016-10-01

    Phthalocyanines, which are classified as second-generation photosensitizers, have advantageous photophysical properties, and extensive studies have demonstrated their potential applications in photodynamic therapy. The present work describes the preparation of a new zinc phthalocyanine conjugated to bovine serum albumin (compound 4a) and its photodynamic efficiency in human larynx-carcinoma cells (HEp-2 cells). The unconjugated precursor (compound 4) was also studied. Compounds 4 and 4a penetrated efficiently into the cell, exhibiting cytoplasmic localization, and showed no cytotoxicity in the dark. However, high photodynamic activities were observed in HEp-2 cells after treatments with 5 µM photosensitizers and 4.5 J cm-2 light. These conditions were sufficient to decrease the cell viability to 57.93% and 32.75% for compounds 4 and 4a, respectively. The present results demonstrated high photodynamic efficiency of zinc phthalocyanine conjugated with bovine serum albumin in destroying the larynx-carcinoma cells.

  15. Covalent modification of human serum albumin by the natural sesquiterpene lactone parthenolide.

    Science.gov (United States)

    Plöger, Michael; Sendker, Jandirk; Langer, Klaus; Schmidt, Thomas J

    2015-04-09

    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.

  16. Binding equilibrium of I~- to serum albumin with resonance Rayleigh scattering

    Institute of Scientific and Technical Information of China (English)

    梁宏; 沈星灿; 蒋治良; 何锡文; 申泮文

    2000-01-01

    The binding equilibrium between l- and human serum albumin (HSA) or bovine serum albumin (BSA) has been studied by means of the resonance Rayleigh scattering (RRS) and equilibrium dialysis. It has been found for the first time that RRS and multiple frequency scattering (MFS) are enhanced as the l- binding to the HSA and BSA, but fluorescence quenches. The equilibrium dialysis results suggest that the binding of l- to HSA and BSA fits a phase-distribution model other than Scsitchard model, and that the order of magnitude of its phase-distribution constant was found to be 104. It is most probable that Cl~ or other anion ions influence the binding of P by changing the ionic strength in the solution. The dialysis at different pH indicates that the binding mechanism is due to the electrostatic forces between the T-and protonated basic amino-acid residues.

  17. [Results of a drug use investigation of nanoparticle albumin-bound Paclitaxel for breast cancer].

    Science.gov (United States)

    Nakamura, Seigo; Iwata, Hiroji; Funato, Yuya; Ito, Kunio; Ito, Yoshinori

    2015-04-01

    A drug use investigation of nanoparticle albumin-bound paclitaxel was conducted based on conditions for approval. A total of 963 patients were enrolled in this study from September 24, 2010 to February 14, 2011. Twenty-nine patients were excluded, and a total of 934 patients were evaluated for determining the safety of nanoparticle albumin-bound paclitaxel. Adverse drug reactions were observed in 92.8%of the patients, and major adverse drug reactions included myelosuppression and peripheral sensory neuropathy, both of which are characteristic adverse reactions of paclitaxel treatment. Both adverse drug reactions were observed at a high frequency after the second course of treatment, resulting in these reactions being primary causes for discontinuation. Increase in the rates of continuous drug administration may be accomplished by carrying out laboratory tests and noting the medical history in order to prevent myelosuppression from becoming serious and to perform earlier countermeasures for peripheral sensory neuropathy, leading to improved therapeutic effects.

  18. 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

    In the treatment of infertility employing in vitro fertilisation and embryo transfer (IVF-EF), oocytes, spermatozoa and pre-embryos are cultured for 48 hours outside the woman's body before they are introduced into the uterus. In addition to the necessary salts, the media in which this culture...... 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......) but the difference is not significant. On the other hand, the quality of the pre-embryos as assessed by morphological criteria became significantly better and the implantation rate per transplanted pre-embryo was found to be significantly increased in the albumin group. On the basis of this investigation, h...

  19. Centrifugal partition chromatography as a tool for preparative purification of pea albumin with enhanced yields.

    Science.gov (United States)

    Bérot, Serge; Le Goff, Elisabeth; Foucault, Alain; Quillien, Laurence

    2007-01-15

    A new procedure including the use of centrifugal partition chromatography (CPC) is proposed to purify PA1b and its isoforms. These pea (Pisum sativum L.) seed proteins are toxic against weevils and can be used as an environment-friendly insecticide. CPC was applied to a whole albumin fraction prepared from pea flour. The butanol:aqueous TFA system used in CPC allowed the separation of PA1b from other albumins and a degree of purification above 95%. Compared to analytical procedures based on methanol extraction, anion exchange and then reversed-phase chromatography (RPC), CPC recovered PA1b in much better yield, which is indispensable for large-scale purification of a biodegradable insecticide.

  20. The effect of structural alterations of three mammalian serum albumins on their binding properties

    Science.gov (United States)

    Równicka-Zubik, J.; Sułkowski, L.; Maciążek-Jurczyk, M.; Sułkowska, A.

    2013-07-01

    The binding of piroxicam (PIR) to human (HSA), bovine (BSA) and sheep (SSA) serum albumin in native and destabilized/denaturated state was studied by the fluorescence quenching technique. Quenching of the intrinsic fluorescence of three analyzed serum albumins was observed due to selective exciting of tryptophanyl and tyrosil residues at 295 nm and 280 nm. Based on fluorescence emission spectra the quenching (KQ) and binding constants (Ka) were determined. The results showed that PIR is bound mainly in IIA subdomain of HSA and is additionally able to interact with tyrosil groups located in subdomains IB, IIB or IIIA. PIR interacts only with tryptophanyl residues of BSA and SSA [Trp-214, Trp-237 (IIA) and Trp-135, Trp-158 (IB)]. The presence of denaturating factors modified the mechanism of fluorescence quenching of SSA by PIR. Linear Scatchard plots suggest that HSA, BSA and SSA bind PIR in one class of binding sites.

  1. Semiconductor quantum dot/albumin complex is a long-life and highly photostable endosome marker.

    Science.gov (United States)

    Hanaki, Ken-ichi; Momo, Asami; Oku, Taisuke; Komoto, Atsushi; Maenosono, Shinya; Yamaguchi, Yukio; Yamamoto, Kenji

    2003-03-14

    For the purpose of selecting the efficient dispersion condition of hydrophilic semiconductor quantum dots (QDs) in biological buffers, the dispersion of the QDs mixed with a serum albumin from 9 different species or an ovalbumin was compared by a fluorescence intensity analysis. The QDs mixed with sheep serum albumin (SSA) showed the highest fluorescence of all when the mixtures were dissolved in Dulbecco's MEM. QD/SSA complexes were accumulated in the endosome/lysosome of Vero cells and the fluorescence could be detected over a 5-day post-incubation period. The photostability of QD/SSA complexes associated with the endosomes was detectable, at least, 30 times as long as that of fluorescein-labeled dextran involved in endosomes. QD/SSA complex, therefore, can be used as a long-life and highly photostable endosome marker.

  2. 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......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...... that cooperativity is absent while the stoichiometric equation is valid even when cooperativity is present. It was found with palmitate as well as with stearate that the two equations fitted the data equally well, and it was concluded that the observations were compatible with absence of cooperativity. The relative...

  3. 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.

  4. Research of biological liquid albumin based on terahertz time domain spectroscopy

    Science.gov (United States)

    Yang, Shuai; Liu, Shang-jian; Zuo, Jian; Zhang, Cun-lin

    2016-11-01

    There is no corresponding fingerprint characteristic spectrum detecting complex ensemble biological samples in liquid, in the paper, such urine of kidney disease patients as samples of the research, using terahertz time-domain spectroscopy emphatically explores response characteristics of the urine albumin in the terahertz spectrum characteristics, and combined with stoichiometric method, we find a certain kind of relationship between terahertz spectrum data and the content of urine albumin, which offsets the defects of other spectroscopy in measuring liquid protein, and in accordance with hospital clinical data. This study established a semi-qualitative method of using terahertz spectroscopy in detecting non-purification of biological liquid sample, which provides a simple, nondestructive, cheap and fast reference method in identifying the early nephropathy for medical test.

  5. Impact of Albumin on Coagulation Competence and Hemorrhage During Major Surgery

    DEFF Research Database (Denmark)

    Rasmussen, Kirsten C; Højskov, Michael; Johansson, Pär I;

    2016-01-01

    For patients exposed to a massive blood loss during surgery, maintained coagulation competence is important. It is less obvious whether coagulation competence influences bleeding during elective surgery where patients are exposed to infusion of a crystalloid or a colloid.This randomized controlled...... trial evaluates whether administration of 5% human albumin (HA) or lactated Ringer solution (LR) affects coagulation competence and in turn blood loss during cystectomy due to bladder cancer.Forty patients undergoing radical cystectomy were included to receive either 5% HA (n = 20) or LR (n = 20......) evaluated coagulation competence, albumin affected clot growth (TEG-angle 69 ± 5 vs 74° ± 3°, P blood loss (P = 0...

  6. 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.

  7. Studies on binding interactions between clenbuterol hydrochloride and two serum albumins by multispectroscopic approaches in vitro.

    Science.gov (United States)

    Wang, Qin; Zhang, Shengrui

    2014-08-01

    In this study, binding properties of clenbuterol hydrochloride (CL) with human serum albumin (HSA) and bovine serum albumin (BSA) were examined using constant protein concentrations and various CL contents under physiological conditions. The binding parameters were confirmed using fluorescence quenching spectroscopy at various temperatures. The experimental results confirmed that the quenching mechanisms of CL and HSA/BSA were both static quenching processes. The thermodynamic parameters, namely, enthalpy change (ΔH) and entropy change (ΔS), were calculated according to the van't Hoff equation, which suggested that the electrostatic interactions were the predominant intermolecular forces in stabilizing the CL-HSA complex, and hydrogen bonds and van der Waals force were the predominant intermolecular forces in stabilizing the CL-BSA complex. Furthermore, the conformational changes of HSA/BSA in the presence of CL were determined using the data obtained from three-dimensional fluorescence spectroscopy, ultraviolet-visible absorption spectroscopy and circular dichroism spectroscopy.

  8. Linolenic acid prevents early and advanced glycation end-products (AGEs) modification of albumin.

    Science.gov (United States)

    Prasanna, Govindarajan; Saraswathi, N T

    2017-02-01

    In this study, we report the protective effects of linolenic acid towards the formation of early (HbA1c) and advanced glycation end-products (AGEs) based on fluorescence, circular dichroism, confocal microscopy and molecular interaction studies. Linolenic acid was found to be a potent inhibitor of AGEs formed by both glucose and fructose. The HbA1c (early glycation product) level was found to be reduced to 7.4% when compared to glycated control (8.4%). Similarly, linolenic acid also inhibited the methylglyoxal mediated AGEs formation. Circular dichroism spectroscopy studies suggested that the protective effect of linolenic acid for the helical structure of albumin. The molecular interaction studies showed that linolenic acid interacts with arginine residues of albumin with high affinity. Results suggested linolenic acid to be a potent antiglycation compound and also it could be a better lead compound for AGE inhibition.

  9. Radiopharmaceutical development based on human blood albumin microspheres and 90Y

    Science.gov (United States)

    Petriev, V. M.; Vlasova, O. P.; Postnov, A. A.; Epstein, N. B.

    2017-01-01

    New radiopharmaceutial (RP) based on human serum albumin microspheres (MSA) and 90Y was developed for treatment of liver cancer. The optimized synthesis using chelation resulted in approximately 80% yield with high specific activity. The RP developed was tested in mice with inoculated sarcoma-37. In two weeks the tumor size reduced by 43% after the treatment with the dose of 500 μCi injected into the tumor site.

  10. Monitoring and managing urinary albumin excretion: practical advice for primary care clinicians.

    Science.gov (United States)

    Bakris, George L; Kuritzky, Louis

    2009-07-01

    Albuminuria has a strong, continuous, direct, linear relationship with adverse cardiovascular (CV) outcomes and chronic kidney disease progression. Even at levels below the accepted upper limit of what is considered "normal" daily albumin excretion (albumin excretion level and adverse CV events is evident. Primary care clinicians (eg, physicians, nurse practitioners, physicians' assistants) are usually the first point of contact for patients at risk for CV and kidney disease. Hence, identifying and treating problematic albuminuria levels are important in primary care. Both the American Diabetes Association (ADA) and the National Kidney Foundation (NKF) endorse routine annual screening for microalbuminuria (small amounts of albumin in the urine). Once excess albumin excretion is detected, clinicians must employ aggressive CV risk reduction. To optimize outcomes, treatment of microalbuminuria often requires the combined skills of experts in primary care, cardiology, metabolic disease, and nephrology. Although blood pressure reduction usually improves microalbuminuria, agents that block the renin-angiotensin-aldosterone system (RAAS) are most efficacious. Renin-angiotensin-aldosterone system blockers (ie, angiotensin-converting enzyme inhibitors, angiotensin II receptor blockers, direct renin inhibitors) may confer CV and kidney advantages in high-risk patients. Their effects on microalbuminuria reduction are greater than those associated with attaining guideline-recommended blood pressure goals. Effective RAAS blockade sometimes induces transient changes in creatinine and potassium, which merit consistent monitoring for the first 2 to 3 months of their use, but rarely necessitate discontinuation. This article also presents an approach to managing increases in creatinine and potassium that should fit comfortably in the hands of primary care clinicians.

  11. Isolation of bovine plasma albumin by liquid chromatography and its polymerization for use in immunohematology

    Directory of Open Access Journals (Sweden)

    K. Tanaka

    2001-08-01

    Full Text Available The aim of the method described here is to remove hemoglobin, the major contaminant in the bovine plasma obtained from slaughterhouses, by adding a mixture of 19% cold ethanol and 0.6% chloroform, followed by fibrinogen and globulin precipitation by the Cohn method and nonspecific hemagglutinin by thermocoagulation. The experimental volume of bovine plasma was 2,000 ml per batch. Final purification was performed by liquid chromatography using the ion-exchange gel DEAE-Sepharose FF. The bovine albumin thus obtained presented > or = 99% purity, a yield of 25.0 ± 1.2 g/l plasma and >71.5% recovery. N-acetyl-DL-tryptophan (0.04 mmol/g protein and sodium caprylate (0.04 mmol/g protein were used as stabilizers and the final concentration of albumin was adjusted to 22.0% (w/v, pH 7.2 to 7.3. Viral inactivation was performed by pasteurization for 10 h at 60°C. The bovine albumin for the hemagglutination tests used in immunohematology was submitted to chemical treatment with 0.06% (w/v glutaraldehyde and 0.1% (w/v formaldehyde at 37°C for 12 h to obtain polymerization. A change in molecular distribution was observed after this treatment, with average contents of 56.0% monomers, 23.6% dimers, 12.2% trimers and 8.2% polymers. The tests performed demonstrated that this polymerized albumin enhances the agglutination of Rho(D-positive red cells by anti-Rho(D serum, permitting and improving visualization of the results.

  12. Purification of human albumin by the combination of the method of Cohn with liquid chromatography

    Directory of Open Access Journals (Sweden)

    Tanaka K.

    1998-01-01

    Full Text Available Large volumes of plasma can be fractionated by the method of Cohn at low cost. However, liquid chromatography is superior in terms of the quality of the product obtained. In order to combine the advantages of each method, we developed an integrated method for the production of human albumin and immunoglobulin G (IgG. The cryoprecipitate was first removed from plasma for the production of factor VIII and the supernatant of the cryoprecipitate was fractionated by the method of Cohn. The first precipitate, containing fractions (F-I + II + III, was used for the production of IgG by the chromatographic method (see Tanaka K et al. (1998 Brazilian Journal of Medical and Biological Research, 31: 1375-1381. The supernatant of F-I + II + III was submitted to a second precipitation and F-IV was obtained and discarded. Albumin was obtained from the supernatant of the precipitate F-IV by liquid chromatography, ion-exchange on DEAE-Sepharose FF, filtration through Sephacryl S-200 HR and introduction of heat treatment for fatty acid precipitation. Viral inactivation was performed by pasteurization at 60ºC for 10 h. The albumin product obtained by the proposed procedure was more than 99% pure for the 15 lots of albumin produced, with a mean yield of 25.0 ± 0.5 g/l plasma, containing 99.0 to 99.3% monomer, 0.7 to 1.0% dimers, and no polymers. Prekallikrein activator levels were <=5 IU/ml. This product satisfies the requirements of the 1997 Pharmacopée Européenne.

  13. Albumin dialysis has a favorable effect on amino acid profile in hepatic encephalopathy.

    Science.gov (United States)

    Koivusalo, Anna-Maria; Teikari, Taru; Höckerstedt, Krister; Isoniemi, Helena

    2008-12-01

    According to one popular theory, hepatic encephalopathy (HE) is partly caused by an imbalance in plasma amino acid levels. The Fischer's ratio between branched chain amino acids (BCAAs) and aromatic amino acids (AAAs) correlates with the degree of HE; the lower Fischer's ratio, the higher the grade of HE. Extra-corporeal liver support systems, like MARS(R)-albumin dialysis (Molecular Adsorbents Recirculating System), can improve HE. The MARS(R) system uses a hyperosmolar albumin circuit to remove both water-soluble and albumin-bound substances. Plasma levels of neuroactive amino acids were analyzed in 82 consecutive patients with life-threatening liver failure admitted to our ICU. All patients fulfilled our indications for MARS treatment and most also fulfilled the criteria for liver transplantation (LTx). In patients with acute liver failure (ALF), as compared to those with acute decompensation of chronic liver failure (AcOChr), levels of leucine and isoleucine were significantly higher before MARS(R) treatment. In all patients, before MARS(R) treatment the higher the grade of HE grade the lower was the Fischer's ratio and higher were the levels of inhibitory neuroactive amino acids. During MARS(R) treatments the Fischer's ratio increased, and the grade of HE decreased. The increase in Fischer's ratio was mainly due to the decrease in AAAs. The plasma levels of neuroactive amino acids, methionine, glutamine, glutamate, histidine and taurine decreased during MARS(R)-treatment. In this study MARS(R)-albumin dialysis had a favorable effect on the plasma amino acid profile of patients with HE.

  14. Interaction of chlorogenic acids and quinides from coffee with human serum albumin.

    Science.gov (United States)

    Sinisi, Valentina; Forzato, Cristina; Cefarin, Nicola; Navarini, Luciano; Berti, Federico

    2015-02-01

    Chlorogenic acids and their derivatives are abundant in coffee and their composition changes between coffee species. Human serum albumin (HSA) interacts with this family of compounds with high affinity. We have studied by fluorescence spectroscopy the specific binding of HSA with eight compounds that belong to the coffee polyphenols family, four acids (caffeic acid, ferulic acid, 5-O-caffeoyl quinic acid, and 3,4-dimethoxycinnamic acid) and four lactones (3,4-O-dicaffeoyl-1,5-γ-quinide, 3-O-[3,4-(dimethoxy)cinnamoyl]-1,5-γ-quinide, 3,4-O-bis[3,4-(dimethoxy)cinnamoyl]-1,5-γ-quinide, and 1,3,4-O-tris[3,4-(dimethoxy)cinnamoyl]-1,5-γ-quinide), finding dissociation constants of the albumin-chlorogenic acids and albumin-quinides complexes in the micromolar range, between 2 and 30μM. Such values are comparable with those of the most powerful binders of albumin, and more favourable than the values obtained for the majority of drugs. Interestingly in the case of 3,4-O-dicaffeoyl-1,5-γ-quinide, we have observed the entrance of two ligand molecules in the same binding site, leading up to a first dissociation constant even in the hundred nanomolar range, which is to our knowledge the highest affinity ever observed for HSA and its ligands. The displacement of warfarin, a reference drug binding to HSA, by the quinide has also been demonstrated.

  15. Thermodynamic study on the interaction between anti-tumor drug tegafur and human serum albumin

    Institute of Scientific and Technical Information of China (English)

    2007-01-01

    The changes of thermodynamic properties of the system on interaction between tegafur and human serum albumin (HSA) and the changes of secondary structure units of HSA in the system at 298.15 K have been investigated by the Nano-Watt-Scale isothermal titration calorimetry (ITC), the Langmuirs binding model and the circular dichroism (CD) spectrometry.(C) 2007 Lin Wei Li. Published by Elsevier B.V. on behalf of Chinese Chemical Society. All rights reserved.

  16. Removal of Endotoxin from Human Serum Albumin Solutions by Hydrophobic and Cationic Charged Membrane

    Institute of Scientific and Technical Information of China (English)

    2000-01-01

    A novel matrix of macropore cellulose membrane was prepared by chemical graft, and immobilized the cationic charged groups as affinity ligands. The prepared membrane can be used for the removal of endotoxin from human serum albumin (HSA) solutions. With a cartridge of 20 sheets affinity membrane of 47 mm diameter, the endotoxin level in HSA solution can be reduced to 0.027 eu/mL. Recovery of HSA was over 95%.

  17. Voltammetric Studies of the Interaction of Tris (1, 10-phenanthroline) Cobalt (Ⅲ) with Bovine Serum Albumin

    Institute of Scientific and Technical Information of China (English)

    2001-01-01

    The voltammetric methods were used to prove the interaction of metal complex Co(phen)33+ with bovine serum albumin (BSA). The interaction of BSA with Co(phen)33+ molecules using BSA-modified electrode is described. Information of the binding ratio and interaction mode can be obtained from their electrochemical behavior and electrochemical data. Furthermore, attenuated total reflection infrared experiment was performed to prove the interaction between complexes and BSA.

  18. Expression and purification of recombinant human serum albumin from selectively terminable transgenic rice*

    OpenAIRE

    Zhang, Qing; Yu, Hui; Zhang, Feng-zhen; Shen, Zhi-Cheng

    2013-01-01

    Human serum albumin (HSA) is widely utilized for medical purposes and biochemical research. Transgenic rice has proved to be an attractive bioreactor for mass production of recombinant HSA (rHSA). However, transgene spread is a major environmental and food safety concern for transgenic rice expressing proteins of medical value. This study aimed to develop a selectively terminable transgenic rice line expressing HSA in rice seeds, and a simple process for recovery and purification of rHSA for ...

  19. Improvement of the Shami goat semen quality by adding bovine serum albumin

    Directory of Open Access Journals (Sweden)

    O.I. Azawi

    2014-06-01

    Full Text Available The present study was aimed to improve the quality of Shami goat semen diluted with Tris diluent by adding bovine serum albumin. In the current study, six male goats were used. Semen was collected using artificial vagina of one ejaculate per week of every male included in this study. This study was performed during the breeding season from 1 \\ 10 \\ 2012 to 1 \\ 12 \\ 2012. In this study, two semen diluents were use first; Tris- fructose- egg yolk 2.5% and second Tris - fructose - 2.5% egg yolk with 1% of bovine serum albumin. Diluted semen samples were cooled gradually and stored at 5 ° C. Cooled diluted semen samples were examined every 24 h of storage to 144 h. These tests includes the proportion of live sperm and the percentage of secondary abnormalities of the sperm, the percentage of sperm acrosomal defects and percentage of progressive motility using a computer-aided sperm analysis. These results showed that the addition of bovine serum albumin with egg yolk to semen of male goats led to improved qualities of semen significantly (P<0.05 including the proportion of live sperm and the percentage of secondary abnormalities of the sperm, the percentage of sperm acrosomal defects and percentage of progressive motility. It could be concluded from the results of the current study, the possibility of storing goat semen for more than six days with alive sperm of more than 50% and the percentage of the progressive motility of more than 40% when adding bovine albumin serum to dilute goat semen at 1% level and this result has not reached by any previous study.

  20. Impact of Albumin on Coagulation Competence and Hemorrhage During Major Surgery: A Randomized Controlled Trial.

    Science.gov (United States)

    Rasmussen, Kirsten C; Højskov, Michael; Johansson, Pär I; Kridina, Irina; Kistorp, Thomas; Salling, Lisbeth; Nielsen, Henning B; Ruhnau, Birgitte; Pedersen, Tom; Secher, Niels H

    2016-03-01

    For patients exposed to a massive blood loss during surgery, maintained coagulation competence is important. It is less obvious whether coagulation competence influences bleeding during elective surgery where patients are exposed to infusion of a crystalloid or a colloid. This randomized controlled trial evaluates whether administration of 5% human albumin (HA) or lactated Ringer solution (LR) affects coagulation competence and in turn blood loss during cystectomy due to bladder cancer. Forty patients undergoing radical cystectomy were included to receive either 5% HA (n = 20) or LR (n = 20). Nineteen patients were analyzed in the HA group and 20 patients in the lactated Ringer group. Blinded determination of the blood loss was similar in the 2 groups of patients: 1658 (800-3300) mL with the use of HA and 1472 (700-4330) mL in the lactated Ringer group (P = 0.45). Yet, by thrombelastography (TEG) evaluated coagulation competence, albumin affected clot growth (TEG-angle 69 ± 5 vs 74° ± 3°, P blood loss (P = 0.042) while administration of albumin was related to the changes in TEG-MA (P = 0.029), aPPT (P blood loss as compared to infusion of LR. Also the use of HA did not affect the need for blood transfusion, the incidence of postoperative complications, or the hospital in-stay. Yet, albumin decreases coagulation competence during major surgery and the blood loss is related to TEG-MA rather than to plasma coagulation variables.

  1. Protein-calixarene interactions: complexation of Bovine Serum Albumin by sulfonatocalix[n]arenes.

    Science.gov (United States)

    Memmi, L; Lazar, A; Brioude, A; Ball, V; Coleman, A W

    2001-12-07

    The complexation of Bovine Serum Albumin with sulfonatocalix[n]arenes has been demonstrated by means of electrospray mass spectrometry, dynamic light scattering and atomic force microscopy; with sulfonatocalix[4]arene one strong and two weaker binding sites are detected; the effects on the structure of thin films formed by surface deposition of BSA show that the sulfonatocalix[n]arenes act to reticulate the films and produce essentially planar systems.

  2. Plasma volume, intravascular albumin and its transcapillary escape rate in patients with extensive skin disease

    DEFF Research Database (Denmark)

    Parving, H H; Worm, A M; Rossing, N

    1976-01-01

    less than 0-001). The transcapillary escape rate of albumin (TER alb) was significantly elevated, mean 8-6 +/- 1-1 (s.d.) % X h-1, as compared to normal subjects, mean 5-6 +/- 1-1 (s.d.) % X h-1, (+54%, P less than 0-001). The same patients were studied again after a 1-week treatment with prednisone...

  3. Phase behavior of mixtures of rods (tobacco mosaic virus) and spheres (polyethylene oxide, bovine serum albumin).

    OpenAIRE

    1998-01-01

    Aqueous suspensions of mixtures of the rodlike virus tobacco mosaic virus (TMV) with globular macromolecules such as polyethylene oxide (PEO) or bovine serum albumin (BSA) phase separate and exhibit rich and strikingly similar phase behavior. Isotropic, nematic, lamellar, and crystalline phases are observed as a function of the concentration of the constituents and ionic strength. The observed phase behavior is considered to arise from attractions between the two particles induced by the pres...

  4. TALEN-mediated modification of the bovine genome for large-scale production of human serum albumin.

    Science.gov (United States)

    Moghaddassi, Shaida; Eyestone, Will; Bishop, Colin E

    2014-01-01

    As an initial step towards creating genetically modified cattle as a biopharming source of recombinant human serum albumin (rHSA), we report modification of the bovine albumin (bA) locus by transcription activator-like effector nuclease (TALEN)-stimulated homology-directed repair (HDR). Pedigreed bovine fibroblasts were co-transfected with TALENs and an 11.5-kb human serum albumin (HSA) minigene donor construct, designed to simultaneously disrupt and replace bovine serum albumin (BSA) expression with controlled rHSA expression in both the liver and the milk. Targeted integration of the HSA minigene was confirmed in transfected fibroblasts at a frequency of approximately 11% and transgenic bovine embryos were produced from targeted fibroblasts using somatic cell nuclear transfer (SCNT). The research delineated here lays the foundation for the future generation of transgenic rHSA cattle with the potential to provide a large-scale, reliable, and quality-controlled source of rHSA.

  5. Formation, stability, and mechanical properties of bovine serum albumin stabilised air bubbles produced using coaxial electrodydrodynamic atomisation

    NARCIS (Netherlands)

    Mahalingham, S.; Meinders, M.B.J.; Edirisinghe, M.

    2014-01-01

    Bovine serum albumin (BSA) microbubbles were generated using coaxial electrohydrodynamic atomization (CEDHA) using various concentrations of BSA solutions. The bubble characteristics and the long-term stability of the microbubbles were studied through adjustment of processing parameters and the coll

  6. Albumin binding of anti-inflammatory drugs. Utility of a site-oriented versus a stoichiometric analysis

    DEFF Research Database (Denmark)

    Honoré, B; Brodersen, R

    1984-01-01

    Binding equilibria of 12 nonsteroidal, anti-inflammatory substances, salicylic acid, diflunisal, phenylbutazone, azapropazone, fenbufen, biphenylacetic acid, naproxen, flurbiprofen, ibuprofin, diclofenac, indomethacin, and benoxaprofen, to defatted human serum albumin has been investigated at 37...

  7. Characterization of isomeric VX nerve agent adducts on albumin in human plasma using liquid chromatography-tandem mass spectrometry.

    Science.gov (United States)

    Saeidian, Hamid; Mirkhani, Valioallah; Mousavi Faraz, Sajjad; Taghi Naseri, Mohammad; Babri, Mehran

    2015-01-01

    This study includes the characterization of isomeric VX organophosphorus adducts on albumin in human plasma using liquid chromatography-tandem mass spectrometry (LC-MS/MS). VX or its structural isomers were spiked into a vial containing plasma in order to obtain phosphorylated albumin. After pronase and trypsin digestion, the resulting solutions were analyzed to confirm adduct formation with the amino acid tyrosine on the albumin in human plasma. The LC-MS/MS experiments show that VX and its isomers can be attached to tyrosine on the albumin in human blood. Mass spectrometric studies revealed some interesting fragmentation pathways during the ionization process, such as ethylene, formic acid and ammonia elimination and an intermolecular electrophilic aromatic substitution reaction. The proposed mechanisms for the formation of the fragments were confirmed through the analysis of fragments of deuterated adducts.

  8. Molecular Diagnosis of Analbuminemia: A New Case Caused by a Nonsense Mutation in the Albumin Gene

    Directory of Open Access Journals (Sweden)

    Lorenzo Minchiotti

    2011-10-01

    Full Text Available Analbuminemia is a rare autosomal recessive disorder manifested by the absence, or severe reduction, of circulating serum albumin (ALB. We report here a new case diagnosed in a 45 years old man of Southwestern Asian origin, living in Switzerland, on the basis of his low ALB concentration (0.9 g/L in the absence of renal or gastrointestinal protein loss, or liver dysfunction. The clinical diagnosis was confirmed by a mutational analysis of the albumin (ALB gene, carried out by single-strand conformational polymorphism (SSCP, heteroduplex analysis (HA, and DNA sequencing. This screening of the ALB gene revealed that the proband is homozygous for two mutations: the insertion of a T in a stretch of eight Ts spanning positions c.1289 + 23–c.1289 + 30 of intron 10 and a c.802 G > T transversion in exon 7. Whereas the presence of an additional T in the poly-T tract has no direct deleterious effect, the latter nonsense mutation changes the codon GAA for Glu244 to the stop codon TAA, resulting in a premature termination of the polypeptide chain. The putative protein product would have a length of only 243 amino acid residues instead of the normal 585 found in the mature serum albumin, but no evidence for the presence in serum of such a truncated polypeptide chain could be obtained by two dimensional electrophoresis and western blotting analysis.

  9. Physicochemical aspects of the energetics of binding of sulphanilic acid with bovine serum albumin

    Science.gov (United States)

    Banipal, Tarlok S.; Kaur, Amandeep; Banipal, Parampaul K.

    2017-01-01

    The thermodynamic study of the binding of sulphanilic acid with model transport protein bovine serum albumin is a promising approach in the area of synthesizing new sulfa drugs with improved therapeutic effect. Thus, such binding studies play an important role in the rational drug design process. The binding between sulphanilic acid and bovine serum albumin has been studied using calorimetry, light scattering in combination with spectroscopic and microscopic techniques. The calorimetric data reveals the presence of two sequential nature of binding sites where the first binding site has stronger affinity ( 104 M- 1) and second binding site has weaker affinity ( 103 M- 1). However, the spectroscopic (absorption and fluorescence) results suggest the presence of single low affinity binding site ( 103 M- 1) on protein. The contribution of polar and non-polar interactions to the binding process has been explored in the presence of various additives. It is found that sulphanilic acid binds with high affinity at Sudlow site II and with low affinity at Sudlow site I of protein. Light scattering and circular dichroism measurements have been used to study the effect on the molecular topology and conformation of protein, respectively. Thus these studies provide important insights into the binding of sulphanilic acid with bovine serum albumin both quantitatively and qualitatively.

  10. Interactions of hybrid gold-tannic acid nanoparticles with human serum albumin.

    Science.gov (United States)

    Sekowski, Szymon; Tomaszewska, Emilia; Soliwoda, Katarzyna; Celichowski, Grzegorz; Grobelny, Jaroslaw

    2017-01-01

    Nanoparticles present a wide spectrum of chemical, biological, and physical properties which result in their usage in many branches of science. We present an investigation of the interaction between human serum albumin and hybrid gold-tannic acid nanoparticles synthesized via a chemical reduction method. The results obtained demonstrate that tannic acid can be a very effective reducing and stabilizing agent and allows monodisperse hybrid gold nanomaterial to be obtained. The synthesized hybrid gold-tannic acid nanoparticles strongly interact with human serum albumin by formation of protein-corona complexes. The strength of the interaction with albumin depends on the number of tannic acid molecules on the surface of the nanoparticles and the presence of citric acid. Nanoparticles of large size and rich in tannic acid react more strongly with the protein [K SV = (8.00 ± 0.2) × 10(5) M(-1)] compared with smaller ones [K SV = (6.83 ± 0.5) × 10(4) M(-1)] containing citric acid and low concentration of tannic acid.

  11. 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.

  12. Interactions of zinc octacarboxyphthalocyanine with selected amino acids and with albumin

    Science.gov (United States)

    Kliber, Marta; Broda, Małgorzata A.; Nackiewicz, Joanna

    2016-02-01

    Effect of selected amino acids (glycine, L-histidine, L-cysteine, L-serine, L-tryptophan) and albumin on the spectroscopic properties and photostability of zinc octacarboxyphthalocyanine (ZnPcOC) was explored in the phosphate buffer at a pH of 7.0. The photodegradation of ZnPcOC alone and in the presence of amino acids or albumin has been investigated in aqueous phase using UV-366 nm and daylight irradiation. Kinetic analysis showed that the interaction with amino acids or albumin enhances the photostability of ZnPcOC. To answer the question of how zinc phthalocyanine interacts with amino acids extensive DFT calculations were performed. Analysis of the optimized geometry features of ZnPcOC: amino acids complexes in the gas phase and in water environment as well as the BSSE corrected interaction energies indicates that the more likely is the formation of equatorial complexes in which H-bonds are formed between the COOH groups of the phthalocyanine and carboxyl or amino groups of amino acids. UV-Vis spectra calculated by employing time dependent density functional theory (TD-DFT) are also consistent with this conclusion.

  13. ZnS nanosheets: Egg albumin and microwave-assisted synthesis and optical properties

    Science.gov (United States)

    Tian, Xiuying; Wen, Jin; Hu, Jilin; Chen, Zhanjun; Wang, Shumei; Peng, Hongxia; Li, Jing

    2016-09-01

    ZnS nanosheets were prepared via egg albumin and microwave-assisted method. The phases, crystalline lattice structures, morphologies, chemical and optical properties were characterized by X-ray diffraction (XRD), high resolution transmission electron microscopy (HRTEM), field-emission scanning electron microscope(FE-SEM), selected area electron diffraction (SAED), Fourier transform infrared (FTIR) spectroscopy, ultraviolet-visible (UV-Vis) spectroscopy and fluorescence(FL) spectrometer and growth mechanism of ZnS nanosheets was investigated. The results showed that all samples were pure cubic zinc blende with polycrystalline structure. The width of ZnS nanosheets with a rectangular nanostructure was in the range of 450-750 nm. The chemical interaction existed between egg albumin molecules and ZnS nanoparticles via the amide/carboxylate group. The band gap value calculated was 3.72 eV. The band at around 440 nm was attributed to the sulfur vacancies of the ZnS nanosheets. With increasing volumes of egg albumin, the photoluminescence (PL) intensity of ZnS samples firstly increased and then decreased, attributed to concentration quenching.

  14. PEGylated Human Serum Albumin: Review of PEGylation, Purification and Characterization Methods

    Directory of Open Access Journals (Sweden)

    Parvin Akbarzadehlaleh

    2016-09-01

    Full Text Available Human serum albumin (HSA is a non-glycosylated, negatively charged protein (Mw: about 65-kDa that has one free cystein residue (Cys 34, and 17 disulfide bridges that these bridges have main role in its stability and longer biological life-time (15 to 19 days. As HSA is a multifunctional protein, it can also bind to other molecules and ions in addition to its role in maintaining colloidal osmotic pressure (COP in various diseases. In critical illnesses changes in the level of albumin between the intravascular and extravascular compartments and the decrease in its serum concentration need to be compensated using exogenous albumin; but as the size of HSA is an important parameter in retention within the circulation, therefore increasing its molecular size and hydrodynamic radius of HSA by covalent attachment of poly ethylene glycol (PEG, that is known as PEGylation, provides HSA as a superior volume expander that not only can prevent the interstitial edema but also can reduce the infusion frequency. This review focuses on various PEGylation methods of HSA (solid phase and liquid phase, and compares various methods to purifiy and characterize the pegylated form.

  15. PEGylated Human Serum Albumin: Review of PEGylation, Purification and Characterization Methods

    Science.gov (United States)

    Akbarzadehlaleh, Parvin; Mirzaei, Mona; Mashahdi-Keshtiban, Mahdiyeh; Shamsasenjan, Karim; Heydari, Hamidreza

    2016-01-01

    Human serum albumin (HSA) is a non-glycosylated, negatively charged protein (Mw: about 65-kDa) that has one free cystein residue (Cys 34), and 17 disulfide bridges that these bridges have main role in its stability and longer biological life-time (15 to 19 days). As HSA is a multifunctional protein, it can also bind to other molecules and ions in addition to its role in maintaining colloidal osmotic pressure (COP) in various diseases. In critical illnesses changes in the level of albumin between the intravascular and extravascular compartments and the decrease in its serum concentration need to be compensated using exogenous albumin; but as the size of HSA is an important parameter in retention within the circulation, therefore increasing its molecular size and hydrodynamic radius of HSA by covalent attachment of poly ethylene glycol (PEG), that is known as PEGylation, provides HSA as a superior volume expander that not only can prevent the interstitial edema but also can reduce the infusion frequency. This review focuses on various PEGylation methods of HSA (solid phase and liquid phase), and compares various methods to purifiy and characterize the pegylated form. PMID:27766215

  16. Neo-epitopes on methylglyoxal modified human serum albumin lead to aggressive autoimmune response in diabetes.

    Science.gov (United States)

    Jyoti; Mir, Abdul Rouf; Habib, Safia; Siddiqui, Sheelu Shafiq; Ali, Asif; Moinuddin

    2016-05-01

    Glyco-oxidation of proteins has implications in the progression of diabetes type 2. Human serum albumin is prone to glyco-oxidative attack by sugars and methylglyoxal being a strong glycating agent may have severe impact on its structure and consequent role in diabetes. This study has probed the methylglyoxal mediated modifications of HSA, the alterations in its immunological characteristics and possible role in autoantibody induction. We observed an exposure of chromophoric groups, loss in the fluorescence intensity, generation of AGEs, formation of cross-linked products, decrease in α-helical content, increase in hydrophobic clusters, FTIR band shift, attachment of methylglyoxal to HSA and the formation of N(ε)-(carboxyethyl) lysine in the modified HSA, when compared to the native albumin. MG-HSA was found to be highly immunogenic with additional immunogenicity invoking a highly specific immune response than its native counterpart. The binding characteristics of circulating autoantibodies in type 2 diabetes mellitus (DM) patients showed the generation of anti-MG-HSA auto-antibodies in the these patients, that are preferentially recognized by the modified albumin. We propose that MG induced structural perturbations in HSA, result in the generation of neo-epitopes leading to an aggressive auto-immune response and may contribute to the immunopathogenesis of diabetes type 2 associated complications.

  17. Synthesis and Characterization of Chitosan-Albumin Conjugates as pH-Sensitive Biodegradable Hydrogels

    Institute of Scientific and Technical Information of China (English)

    GUO Jin-shan; LI Jian-zheng; JING Xia-bin; CHEN Xue-si; HUANG Yu-bin

    2011-01-01

    A new kind of biodegradable pH-sensitive drug delivery system was developed via chitosan-albumin conjugate hydrogel. Through changing the feeding modes of reactants, two types of hydrogels(comb-type and reticular-type) were synthesized by amidation reactions between 6-O-succinoylated N-phthaloyl chitosan and albumin. The structures and morphologies of the hydrogels were characterized by SEM. And their water swelling capacity, drug loading and releasing properties at different pH values were also investigated. It was found that the comb-type of hydrogels with looser space construction had better water swelling ratio(more than 400% of its original mass) than the reticular-type of ones did(about 180% of its original mass). In vitro release experiments of Rifampicin show that the hydrogels provided the controlled release of the entrapped drug for more than 50 h. The drug release rates of both types of hydrogels under acidic condition were lower than those under neutral or basic condition. The introduction of albumin not only improved the hydrophilicity of chitosan, but also provided the possibility of the carrier system combining other biologically active materials more easily to fulfill the delivery and therapy functions.

  18. Renal handling of beta-2-microglobulin, amylase and albumin in acute pancreatitis.

    Science.gov (United States)

    Karlsson, F A; Jacobson, G

    1979-01-01

    The renal handling of beta-2-microglobulin, amylase and albumin was studied in patients with acute pancreatitis. The data were compared with results obtained from patients with glomerular proteinuria and from patients with tubular proteinuria. Initially during acute pancreatitis, the clearance ratio (clearance protein/clearance creatinine) for beta-2-microglobulin was increased dramatically (77-fold) compared to normals. After four to seven days this ratio had fallen and was elevated only 7-fold. The corresponding figures for amylase were 3.3 and 1.8 times and for albumin 9 and 5 times respectively. In glomerular disease, the clearance ratios for beta-2-microglobulin, amylase and albumin were increased 6, 1.1, and 154 times and in tubular disease 448, 1.1, and 28 times, respectively. The electrophoretic pattern of the urinary proteins during pancreatitis was mostly normal. In a few cases, slight tubular proteinuria was noticed. Amylase activity in serum and urine from patients with pancreatitis was found to sediment, (S20,W = 4.6) in a sucrose gradient, identical to amylase from normal serum and urine. The marked increase in the excretion of beta-2-microglobulin probably reflects interference of the kidney function at the proximal tubular level. Determinations of this protein in urine may be of value in studies of kidney dysfunction that can accompany pancreatitis.

  19. Protective effect of albumin on lung injury in traumatic/hemorrhagic shock in rats

    Institute of Scientific and Technical Information of China (English)

    DING Chen-yan; CHEN Zuo-bing; ZHENG Shu-sen; GAO Yuan; ZHANG Yun; ZHAO Xue-hong; NI Ling-mei

    2005-01-01

    Objective: To determine the effect of albumin administration on lung injury in traumatic/hemorrhagic shock (T/HS) in rats. Methods: Forty-eight adult Sprague-Dawley rats were divided into three groups randomly (n=16 in each group): Group A, Group B, Group C. In Group A, rats underwent laparotomy without shock. In Group B, rats undergoing T/HS were resuscitated with their blood plus lactated Ringer's (twice the volume of shed blood). In Group C, rats undergoing T/HS were resuscitated with their shed blood plus additional 3 ml of 5% human albumin. The expression of polymorphonuclear neutrophils CD18/CD11b in jugular vein blood was evaluated. The main lung injury indexes (the activity of myeloperoxidase and lung injury score) were measured. Results: Significant differences of the expression of CD18/11b and the severity degree of lung injury were found between the three groups.(P<0.05). The expression of CD18/CD11b and the main lung injury indexes in Group B and Goup C incresed significantly compared with those in Group A(P<0.05).At the same time, the expression of CD18/CD11b and the main lung injury indexes in Group C decreased dramatically, compared with those in Group B (P<0.05). Conclusions: The infusion of albumin during resuscitation period can protect lungs from injury and decrease the expression of CD18/CD11b in T/HS rats.

  20. Crystal structure of mature 2S albumin from Moringa oleifera seeds.

    Science.gov (United States)

    Ullah, Anwar; Mariutti, Ricardo Barros; Masood, Rehana; Caruso, Icaro Putinhon; Costa, Gustavo Henrique Gravatim; Millena de Freita, Cristhyane; Santos, Camila Ramos; Zanphorlin, Leticia Maria; Rossini Mutton, Márcia Justino; Murakami, Mario Tyago; Arni, Raghuvir Krishnaswamy

    2S albumins, the seed storage proteins, are the primary sources of carbon and nitrogen and are involved in plant defense. The mature form of Moringa oleifera (M. oleifera), a chitin binding protein isoform 3-1 (mMo-CBP3-1) a thermostable antifungal, antibacterial, flocculating 2S albumin is widely used for the treatment of water and is potentially interesting for the development of both antifungal drugs and transgenic crops. The crystal structure of mMo-CBP3-1 determined at 1.7 Å resolution demonstrated that it is comprised of two proteolytically processed α-helical chains, stabilized by four disulfide bridges that is stable, resistant to pH changes and has a melting temperature (TM) of approximately 98 °C. The surface arginines and the polyglutamine motif are the key structural factors for the observed flocculating, antibacterial and antifungal activities. This represents the first crystal structure of a 2S albumin and the model of the pro-protein indicates the structural changes that occur upon formation of mMo-CBP3-1 and determines the structural motif and charge distribution patterns for the diverse observed activities.

  1. Interactions of zinc octacarboxyphthalocyanine with selected amino acids and with albumin.

    Science.gov (United States)

    Kliber, Marta; Broda, Małgorzata A; Nackiewicz, Joanna

    2016-02-15

    Effect of selected amino acids (glycine, l-histidine, l-cysteine, l-serine, l-tryptophan) and albumin on the spectroscopic properties and photostability of zinc octacarboxyphthalocyanine (ZnPcOC) was explored in the phosphate buffer at a pH of 7.0. The photodegradation of ZnPcOC alone and in the presence of amino acids or albumin has been investigated in aqueous phase using UV-366nm and daylight irradiation. Kinetic analysis showed that the interaction with amino acids or albumin enhances the photostability of ZnPcOC. To answer the question of how zinc phthalocyanine interacts with amino acids extensive DFT calculations were performed. Analysis of the optimized geometry features of ZnPcOC: amino acids complexes in the gas phase and in water environment as well as the BSSE corrected interaction energies indicates that the more likely is the formation of equatorial complexes in which H-bonds are formed between the COOH groups of the phthalocyanine and carboxyl or amino groups of amino acids. UV-Vis spectra calculated by employing time dependent density functional theory (TD-DFT) are also consistent with this conclusion.

  2. Low doses of terlipressin and albumin in the type I hepatorenal syndrome

    Directory of Open Access Journals (Sweden)

    Davide Pulvirenti

    2013-05-01

    Full Text Available BACKGROUND Hepatorenal syndrome is a pre-renal like dysfunction that generally onsets in cirrhotic patients presenting ascites. MATERIALS AND METHODS We investigated the improvement of renal function in subjects with hepatorenal syndrome after terlipressin administration and the survival times after this treatment. 30 patients affected by cirrhosis, with diagnosis of type I hepatorenal syndrome were treated with intravenous terlipressin plus albumin (group A or with albumin alone (group B. Liver function, renal function, sodium plasma level and plasma renin activity were monitored. RESULTS Patients of group A showed a significant improvement (p < 0.001 of renal function valued by creatinine rate compared with the results obtained in group B. The probability of survival was higher in the group A (p < 0.0001. CONCLUSIONS Our results seem to confirm that the administration of terlipressin plus albumin improves renal function in patients with cirrhosis and type I hepatorenal syndrome and that a reversal of hepatorenal syndrome is strongly associated with an improved survival.

  3. Serum albumin promotes ATP-binding cassette transporter-dependent sterol uptake in yeast.

    Science.gov (United States)

    Marek, Magdalena; Silvestro, Daniele; Fredslund, Maria D; Andersen, Tonni G; Pomorski, Thomas G

    2014-12-01

    Sterol uptake in fungi is a multistep process that involves interaction between external sterols and the cell wall, incorporation of sterol molecules into the plasma membrane, and subsequent integration into intracellular membranes for turnover. ATP-binding cassette (ABC) transporters have been implicated in sterol uptake, but key features of their activity remain to be elucidated. Here, we apply fluorescent cholesterol (NBD-cholesterol) to monitor sterol uptake under anaerobic and aerobic conditions in two fungal species, Candida glabrata (Cg) and Saccharomyces cerevisiae (Sc). We found that in both fungal species, ABC transporter-dependent uptake of cholesterol under anaerobic conditions and in mutants lacking HEM1 gene is promoted in the presence of the serum protein albumin that is able to bind the sterol molecule. Furthermore, the C. glabrata ABC transporter CgAus1p expressed in S. cerevisiae requires the presence of serum or albumin for efficient cholesterol uptake. These results suggest that albumin can serve as sterol donor in ABC transporter-dependent sterol uptake, a process potentially important for growth of C. glabrata inside infected humans.

  4. Cranberry phytochemicals inhibit glycation of human hemoglobin and serum albumin by scavenging reactive carbonyls.

    Science.gov (United States)

    Liu, Haiyan; Liu, Hanwei; Wang, Wei; Khoo, Christina; Taylor, James; Gu, Liwei

    2011-08-01

    Protein glycation caused by sugars and reactive carbonyls is a contributing factor to diabetic complications, aging, and other chronic diseases. The objective of this study was to investigate the inhibitory effects of cranberry phytochemicals on protein glycation. Cranberries, purified to yield sugar-free phytochemical powder, were fractionated into ethyl acetate and water fractions. Water fraction was further separated into water fraction I, II, and III on a Sephadex LH-20 column. Cranberry phytochemical powder and its fractions significantly inhibited the formation of glycated hemoglobin. The concentrations of cranberry phytochemicals required to inhibit 50% of albumin glycation (EC(50)) in albumin-glucose assay were lower than that of aminoguanidine except for water fraction I. Cranberry phytochemicals inhibited glycation of human serum albumin mediated by methylglyoxal, but the EC(50) were higher than that of aminoguanidine. Carbonyl scavenging assay showed that water fraction II scavenged 89.3% of methylglyoxal at 6 h of reaction. Fractions enriched with procyanidins showed higher antiglycation activities, suggesting procyanidins were the major active components. The hypothesis whether cranberry procyanidins scavenged reactive carbonyls by forming adducts was tested. Epicatechin was used as a model compound to react with methylglyoxal and glyoxal at pH 7.4. Five adducts were detected and their structures were tentatively identified using HPLC-ESI-MS/MS.

  5. Albumin microparticles as the carriers for allopurinol and applicable for the treatment of ischemic stroke

    Science.gov (United States)

    Aganyants, Hovsep Alexandr; Nikohosyan, Gayane; Danielyan, Kristine Edgar

    2016-11-01

    Albumin nanoparticles are already used for the treatment of the cancer. In our current work, it is presented the technique for the preparation of small-size 1- to 5-micron particles coated with the allopurinol. We propose that this combination of the compounds might be useful for the ischemic stroke treatment as the agent preventing formation of the brain edema, reactive oxygen species, and initiation of cells regeneration. Glutaraldehyde was used for the polymerization of albumin. Determination of the particle size was performed by the light as well as phase contrast microscopies and analyzed by Pixcavator 6.0 and Image Tool programs. Modification and establishment of iodine-based method served as the base for quantification of bound with the particles and free allopurinol. As a consequence of the experiments, the best formulation of glutaraldehyde ratio and albumin quantity as well as conditions for the formation of the smallest sized spheroid-shaped particles were found for the further in vivo application.

  6. Investigation of the interaction of deltamethrin (DM) with human serum albumin by multi-spectroscopic method

    Science.gov (United States)

    Wang, Jiaman; Ma, Liang; Zhang, Yuhao; Jiang, Tao

    2017-02-01

    The interaction of Deltamethrin (DM) with human serum albumin (HSA) under the condition of simulating human blood pH environment (pH = 7.4) was investigated by fluorescence, UV-Vis absorbance and circular dichroism (CD) spectroscopy. It was shown that DM was a static quencher of HSA. The binding constants (Ka) are 3.598 × 104 L mol-1 (25 °C); the thermodynamic parameters (ΔH = -3.269 × 104 kJ mol-1, ΔS = -22.81 kJ mol-1 k-1, ΔG = -25889.8 kJ mol-1) obtained with the thermodynamic equation. The hydrogen bond and Vander Waals were the main driving force. The effect of DM on the conformation of HSA was observed by three-dimensional (3D) fluorescence and circular dichroism spectra, indicating that the interaction between DM and HSA was achieved through the binding of DM with the tryptophan and tyrosine residues of HSA. The study on the interaction of DM and Bovine Serum Albumin (BSA) was researched and compared. Difference exists in the interactions of with each of the serum albumins. We will verify and supplement that DM residue in animals and human metabolism, toxicology and other mechanisms are different.

  7. Urinary albumin excretion and 24-hour blood pressure as predictors of pre-eclampsia in Type I diabetes

    DEFF Research Database (Denmark)

    Ekbom, P; Damm, P; Nøgaard, K;

    2000-01-01

    To evaluate the value of 24-h blood pressure monitoring compared to office blood pressure and urinary albumin excretion in predicting pre-eclampsia in Type I (insulin-dependent) diabetes mellitus.......To evaluate the value of 24-h blood pressure monitoring compared to office blood pressure and urinary albumin excretion in predicting pre-eclampsia in Type I (insulin-dependent) diabetes mellitus....

  8. A step toward simplified detection of serum albumin on SDS-PAGE using an environment-sensitive flavone sensor.

    Science.gov (United States)

    Liu, Bin; Pang, Yi; Bouhenni, Rachida; Duah, Ernest; Paruchuri, Sailaja; McDonald, Lucas

    2015-07-14

    In this study, we report a series of novel flavone-based sensors that exhibit a superior fluorescence response when interacting with serum albumin in real serum samples and in acrylamide gels. The detection limit of probe 4 for serum albumin solution is 0.09 μg mL(-1), and the detectable volume for monkey serum reaches as low as 0.03 μL.

  9. A step toward simplified detection of serum albumin on SDS-PAGE using an environment-sensitive flavone sensor

    OpenAIRE

    Liu, Bin; Pang, Yi; Bouhenni, Rachida; Duah, Ernest; Paruchuri, Sailaja; McDonald, Lucas

    2015-01-01

    In this study, we report a series of novel flavone-based sensors that exhibit superior fluorescence response when interacting with serum albumin in real serum samples and in acrylamide gel. The detection limit of probe 4 for serum albumin solution is 0.09 μg/mL, and the detectable volume for monkey serum reaches as low as 0.03 μL.

  10. 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.

  11. Evaluation of non-covalent interactions between serum albumin and green tea catechins by affinity capillary electrophoresis.

    Science.gov (United States)

    Zinellu, Angelo; Sotgia, Salvatore; Scanu, Bastianina; Pisanu, Elisabetta; Giordo, Roberta; Cossu, Annalisa; Posadino, Anna Maria; Carru, Ciriaco; Pintus, Gianfranco

    2014-11-07

    The natural antioxidant-associated biological responses appear contradictory since biologically active dosages registered in vitro experiments are considerably higher if compared to concentrations found in vivo. The recent research indicates that natural antioxidants, including the major catechins of green tea epicatechin (EC), epigallocatechin (EGC), epicatechingallate (ECG) and epigallocatechingallate (EGCG) form non-covalent complexes with albumin, a crucial aspect that may modulate their plasma concentration, tissue delivery and biological activity. Affinity capillary electrophoresis (ACE) was used to characterize the binding of the four catechins to human serum albumin (HSA) and bovine serum albumin (BSA) at near-physiological conditions: 10 mmol/L phosphate buffer, HEPES 50 mmol/L (pH 7.5), temperature 37°C. The studied flavonoids displayed affinities toward the albumin with binding constants in the range 10(3)-10(5)M(-1), with a greater affinity of catechins toward HSA than BSA (between 3 and 3.5 fold higher). We also confirmed that catechins having a galloyl moiety (ECG and EGCG) have a higher binding affinity toward albumin than the catechins lacking the galloyl moiety (EC and EGC), and that for both albumins the order of affinity is EC

  12. Albumin-normalized serum zinc: a clinically useful parameter for detecting taste impairment in patients undergoing dialysis.

    Science.gov (United States)

    Tsutsumi, Rie; Ohashi, Kie; Tsutsumi, Yasuo M; Horikawa, Yousuke T; Minakuchi, Jyun; Minami, Sachi; Harada, Nagakatsu; Sakaue, Hiroshi; Sakai, Tohru; Nakaya, Yutaka

    2014-01-01

    Patients with renal failure often experience decreased serum zinc that remains uncorrected after dialysis. A complication of this depletion is taste impairment, which can detrimentally influence diet and nutrition. However, because more than half of all serum zinc is bound to albumin, we hypothesized that normalizing serum zinc to albumin levels may be associated with taste impairment. A total of 65 patients undergoing dialysis but not receiving supplementary zinc and 120 control patients not undergoing dialysis (60 malnourished patients and 60 healthy controls) were tested for their receptiveness to saltiness using various salt concentrations. Patients' total protein and albumin levels were measured, and linear regressions were extrapolated between serum zinc levels and total protein or albumin. Patients undergoing dialysis had significantly lower levels of total serum zinc compared with control patients. However, uncorrected zinc levels were not correlated with taste impairment. Normalizing zinc levels against total protein or albumin resulted in extrapolated equations that revealed a significant correlation with taste impairment. Our data suggest a statistical correlation between zinc and albumin in both healthy subjects and patients undergoing maintenance hemodialysis, or protein-energy malnutrition without hemodialysis, allowing for a quantitative measure for taste impairment.

  13. A Comprehensive Spectroscopic and Computational Investigation to Probe the Interaction of Antineoplastic Drug Nordihydroguaiaretic Acid with Serum Albumins.

    Directory of Open Access Journals (Sweden)

    Saima Nusrat

    Full Text Available Exogenous drugs that are used as antidote against chemotheray, inflammation or viral infection, gets absorbed and interacts reversibly to the major serum transport protein i.e. albumins, upon entering the circulatory system. To have a structural guideline in the rational drug designing and in the synthesis of drugs with greater efficacy, the binding mechanism of an antineoplastic and anti-inflammatory drug Nordihydroguaiaretic acid (NDGA with human and bovine serum albumins (HSA & BSA were examined by spectroscopic and computational methods. NDGA binds to site II of HSA with binding constant (Kb ~105 M-1 and free energy (ΔG ~ -7.5 kcal.mol-1. It also binds at site II of BSA but with lesser binding affinity (Kb ~105 M-1 and ΔG ~ -6.5 kcal.mol-1. The negative value of ΔG, ΔH and ΔS for both the albumins at three different temperatures confirmed that the complex formation process between albumins and NDGA is spontaneous and exothermic. Furthermore, hydrogen bonds and hydrophobic interactions are the main forces involved in complex formation of NDGA with both the albumins as evaluated from fluorescence and molecular docking results. Binding of NDGA to both the albumins alter the conformation and causes minor change in the secondary structure of proteins as indicated by the CD spectra.

  14. Investigation into the interaction of losartan with human serum albumin and glycated human serum albumin by spectroscopic and molecular dynamics simulation techniques: A comparison study.

    Science.gov (United States)

    Moeinpour, Farid; Mohseni-Shahri, Fatemeh S; Malaekeh-Nikouei, Bizhan; Nassirli, Hooriyeh

    2016-09-25

    The interaction between losartan and human serum albumin (HSA), as well as its glycated form (gHSA) was studied by multiple spectroscopic techniques and molecular dynamics simulation under physiological conditions. The binding information, including the binding constants, effective quenching constant and number of binding sites showed that the binding partiality of losartan to HSA was higher than to gHSA. The findings of three-dimensional fluorescence spectra demonstrated that the binding of losartan to HSA and gHSA would alter the protein conformation. The distances between Trp residue and the binding sites of the drug were evaluated on the basis of the Förster theory, and it was indicated that non-radiative energy transfer from HSA and gHSA to the losartan happened with a high possibility. According to molecular dynamics simulation, the protein secondary and tertiary structure changes were compared in HSA and gHSA for clarifying the obtained results.

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

    Science.gov (United States)

    Bardajee, Ghasem Rezanejade; 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 (ΔGCdTe-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.

  16. 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.)

  17. Design and development of in situ albumin binding surfaces: Evaluation in the paradigm of blood-biomaterial compatibility

    Science.gov (United States)

    Guha Thakurta, Sanjukta

    Biocompatibility of natural and synthetic implant materials as blood contacting devices is crucial to host response. Implantation often raises complications from thrombotic and thromboembolic events. The aspect of hemocompatibility concentrates on minimizing thrombotic and thromboembolic response of foreign materials in contact with blood. The initial layer of surface adsorbed proteins plays a pivotal role in the adhesion and subsequent aggregation of platelets and in the activation of the coagulation cascade. Therefore, an improved surface architecture is required to gain control over the initial protein adsorption events, thereby extending the sustainability of an implantable device. In general, surfaces with an ability to bind endogenous albumin has been known to minimize platelet adhesion and activation. While the scope of applicability is broad, in this study silicon-based surfaces were selected as model surfaces. A densely packed uniformly distributed silane monolayer was achieved on silicon based surfaces with -- NH2 functionality, upon a careful optimization of hydroxylation and the subsequent silanization with 2 vol% of 3-Aminopropyltriethoxy Silane (APTES). Two linear peptides with affinity for albumin over other serum proteins were selected to create affinity surfaces. Silanized surfaces covalently immobilized with albumin binding peptides were evaluated in the paradigm of blood-biomaterial compatibility. When compared to control surfaces, albumin binding surfaces prepared in this study: (a) possessed 2.0 to 3.0 mug/cm2 of surface bound albumin with minimal surface adsorbed fibrinogen, (b) depicted low levels of adhered platelets and supported a rounded platelet morphology, (c) displayed delayed clotting, (d) showed reduced platelet adhesion and activation under shearing, and (f) exhibited faster adsorption kinetics. Conclusively, in-situ albumin binding surfaces selectively and specifically interacted with albumin without being severely displaced by

  18. Chromatographic removal and heat inactivation of hepatitis A virus during manufacture of human albumin.

    Science.gov (United States)

    Adcock, W L; MacGregor, A; Davies, J R; Hattarki, M; Anderson, D A; Goss, N H

    1998-08-01

    CSL Limited, an Australian biopharmaceutical company, has recently converted its method of manufacture for human albumin from a traditional Cohn-ethanol fractionation method to a method employing chromatographic techniques. Studies were undertaken to determine the efficiency of the chromatographic and pasteurization steps used in the manufacture of Albumex(R) (CSL's trade name for albumin) in removing and inactivating the potential viral contaminant, hepatitis A virus (HAV). The manufacturing process for Albumex(R) includes three chromatographic steps, two of which are ion-exchange steps (DEAE-Sepharose(R) Fast Flow and CM-Sepharose(R) Fast Flow) and the third is a gel-filtration step (Sephacryl(R) S200 HR). The final stage of the Albumex(R) process involves a bulk pasteurization step where product is held at 60 degrees C for 10 h. HAV partitioning experiments on the DEAE-Sepharose(R) FF and CM-Sepharose(R) FF ion-exchange and Sephacryl(R) S200 HR gel-filtration columns were performed with scaled-down models of the production-scale chromatographic Albumex(R) process. Production samples collected before each of the chromatographic steps were spiked with HAV and processed through each of the scaled-down chromatographic columns. Samples collected during processing were assayed and the log10 reduction factors calculated. Inactivation kinetics of HAV were examined during the pasteurization of Albumex(R) 5 and 20 [5% and 20% (w/v) albumin solutions] held at 60 degrees C for 10 h. Log10 reductions for HAV through the DEAE-Sepharose(R) FF, CM-Sepharose(R) FF and Sephacryl(R) S200 HR chromatographic columns were 5.3, 1.5 and 4.2 respectively, whereas a 4.4 and a greater than 3.9 log10 reduction in HAV in Albumex(R) 5 and 20 respectively were achieved during pasteurization.

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

    Energy Technology Data Exchange (ETDEWEB)

    Basu, Anirban; Kumar, Gopinatha Suresh, E-mail: gskumar@iicb.res.in

    2014-05-01

    Highlights: • Carmoisine binds to both the serum albumins with affinity of the order of 10{sup 6} M{sup −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{sup 6} M{sup −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.

  20. Interaction of VO2+ ion with human serum transferrin and albumin.

    Science.gov (United States)

    Sanna, Daniele; Garribba, Eugenio; Micera, Giovanni

    2009-04-01

    The complexation of VO(2+) ion with the high molecular mass components of the blood serum, human serum transferrin (hTf) and albumin (HSA), has been re-examined using EPR spectroscopy. In the case of transferrin, the results confirm those previously obtained, showing that VO(2+) ion occupies three different binding sites, A, B(1) and B(2), distinguishable in the X-band anisotropic spectrum recorded in D(2)O. With albumin the results show that a dinuclear complex (VO)(2)(d)HSA is formed in equimolar aqueous solutions or with an excess of protein; in the presence of an excess of VO(2+), the multinuclear complex (VO)(x)(m)HSA is the prevalent species, where x=5-6 indicates the equivalents of metal ion coordinated by HSA. The structure of the dinuclear species is discussed and the donor atoms involved in the metal coordination are proposed on the basis of the measured EPR parameters. Two different binding modes of albumin can be distinguished varying the pH, with only one species being present at the physiological value. The results show that the previously named "strong" site is not the N-terminal copper binding site, and some hypothesis on the metal coordination is discussed, with the (51)V A(z) values for the proposed donor sets obtained by DFT (density functional theory) calculations. Finally, preliminary results obtained in the ternary system VO(2+)/hTf/HSA are shown in order to determine the different binding strength of the two proteins. Due to the low VO(2+) concentration used, the recording of the EPR spectra through the repeated acquisition of the weak signals is essential to obtain a good signal to noise ratio in these systems.

  1. 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.

  2. Interaction of fibrinogen and albumin with titanium dioxide nanoparticles of different crystalline phases

    Science.gov (United States)

    Marucco, Arianna; Fenoglio, Ivana; Turci, Francesco; Fubini, Bice

    2013-04-01

    TiO2 nanoparticles (NPs) are contained in different kinds of industrial products including paints, self-cleaning glasses, sunscreens. TiO2 is also employed in photocatalysis and it has been proposed for waste water treatment. Micrometric TiO2 is generally considered a safe material, while there is concern on the possible health effects of nanometric titania. Due to their small size NPs may migrate within the human body possibly entering in the blood stream. Therefore studies on the interaction of NPs with plasma proteins are needed. In fact, the interaction with proteins is believed to ultimately influences the NPs biological fate. Fibrinogen and albumin are two of the most abundant plasma proteins. They are involved in several important physiological functions. Furthermore, fibrinogen is known to trigger platelet adhesion and inflammation. For these reasons the study of the interaction between these protein and nanoparticles is an important step toward the understanding of the behavior of NPs in the body. In this study we investigated the interaction of albumin and fibrinogen with TiO2 nanoparticles of different crystal phases (rutile and anatase) using an integrated set of techniques. The amount of adsorbed fibrinogen and albumin for each TiO2 surface was investigated by using the bicinchoninic acid assay (BCA). The variation of the surface charge of the NP-protein conjugates respect to the naked NPs was used to indirectly estimate both surface coverage and reversibility of the adsorption upon dilution. Surface charge was monitored by measuring the ζ potential with a conventional electrophoretic light scattering (ELS) system. The extent of protein deformation was evaluated by Raman Spectroscopy. We found that both proteins adsorb irreversibly against electrostatic repulsion, likely undergoing conformational changes or selective orientation upon adsorption. The size of primary particles and the particles aggregation rather than the crystal phase modulate the

  3. 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.

  4. Pharmaceutical potential of tacrolimus-loaded albumin nanoparticles having targetability to rheumatoid arthritis tissues.

    Science.gov (United States)

    Thao, Le Quang; Byeon, Hyeong Jun; Lee, Changkyu; Lee, Seunghyun; Lee, Eun Seong; Choi, Han-Gon; Park, Eun-Seok; Youn, Yu Seok

    2016-01-30

    Albumin is considered an attractive dug carrier for hydrophobic drugs to target inflamed joints of rheumatoid arthritis. This study focused on the pharmaceutical potential of albumin-based nanoparticles (NPs) on delivery of tacrolimus (TAC) to enhance targetability and anti-arthritic efficacy. TAC-loaded human serum albumin (HSA) nanoparticles (TAC HSA-NPs) were prepared using the nab™ technology. The resulting NPs were 185.8 ± 6.8 nm in diameter and had a zeta potential value of -30.5 ± 1.1 mV, as determined by dynamic light scattering. Particles were uniformly spherical in shape as determined by transmission electron microscopy. The encapsulation efficacy of TAC was 79.3 ± 3.7% and the water solubility was over 46 times greater than that of free TAC. TAC was gradually released from NPs over 24h, which is sufficient time for targeting and treatment of the NPs in inflamed arthritis via intravenous injection. In vitro study using splenocytes excised from spleens of mice following induction of arthritis using collagen clearly demonstrated the anti-proliferative activity of TAC HSA-NPs on activated T cells compared with non-activated T cells. Furthermore, TAC HSA-NPs displayed significantly more anti-arthritic activity than TAC formulations including intravenously administered TAC solution or oral TAC suspension, as reflected by the incidence of arthritis and clinical score (1.6 vs. 3.2 and 5.0, respectively). These improvements were due to the targetability of HSA that facilitated the accumulation of TAC HSA-NPs at inflamed arthritis sites. TAC HSA-NPs are a promising drug delivery system to enhance water solubility and increase accumulation in joints for treatment of rheumatoid arthritis.

  5. Serum Albumin Domain Structures in Human Blood Serum by Mass Spectrometry and Computational Biology.

    Science.gov (United States)

    Belsom, Adam; Schneider, Michael; Fischer, Lutz; Brock, Oliver; Rappsilber, Juri

    2016-03-01

    Chemical cross-linking combined with mass spectrometry has proven useful for studying protein-protein interactions and protein structure, however the low density of cross-link data has so far precluded its use in determining structures de novo. Cross-linking density has been typically limited by the chemical selectivity of the standard cross-linking reagents that are commonly used for protein cross-linking. We have implemented the use of a heterobifunctional cross-linking reagent, sulfosuccinimidyl 4,4'-azipentanoate (sulfo-SDA), combining a traditional sulfo-N-hydroxysuccinimide (sulfo-NHS) ester and a UV photoactivatable diazirine group. This diazirine yields a highly reactive and promiscuous carbene species, the net result being a greatly increased number of cross-links compared with homobifunctional, NHS-based cross-linkers. We present a novel methodology that combines the use of this high density photo-cross-linking data with conformational space search to investigate the structure of human serum albumin domains, from purified samples, and in its native environment, human blood serum. Our approach is able to determine human serum albumin domain structures with good accuracy: root-mean-square deviation to crystal structure are 2.8/5.6/2.9 Å (purified samples) and 4.5/5.9/4.8Å (serum samples) for domains A/B/C for the first selected structure; 2.5/4.9/2.9 Å (purified samples) and 3.5/5.2/3.8 Å (serum samples) for the best out of top five selected structures. Our proof-of-concept study on human serum albumin demonstrates initial potential of our approach for determining the structures of more proteins in the complex biological contexts in which they function and which they may require for correct folding. Data are available via ProteomeXchange with identifier PXD001692.

  6. Quarter variation and correlations of colostrum albumin, immunoglobulin G1 and G2 in dairy cows.

    Science.gov (United States)

    Samarütel, Jaak; Baumrucker, Craig R; Gross, Josef J; Dechow, Chad D; Bruckmaier, Rupert M

    2016-05-01

    A high variation in immunoglobulin G1 (IgG1) concentration in first milked quarter colostrum has been reported, but BSA quarter colostrum variation is not known. The occurrence of serum albumin in milk has been attributed to increased blood-milk barrier penetration. Reports of serum albumin binding to the Fc Receptor of the neonate, the receptor thought to be responsible for IgG1 transcytosis, suggested that a correlation with the appearance of IgG1 in colostrum of dairy cows was likely. The objective of the study was to establish the quarter colostrum concentration and mass of immunoglobulins and serum albumin. First colostrum was quarter collected within 4 h of parturition from healthy udders of 31 multiparous dairy cows. Individual quarter colostrum weight was determined and a sample of each was frozen for subsequent analysis. Concentrations of immunoglobulin G1, G2, and BSA were measured by ELISA and total mass of components was calculated. In addition, colostrum was also analysed for L-lactate dehydrogenase activity. Analysis of concentration and mass of BSA, immunoglobulin G1, G2 established that the quarter variations were different by cow, quarter and quarter within cow. Partial correlations corrected for colostrum weight indicated that BSA and IgG2 concentration and mass are closely correlated while that of BSA and IgG1 concentration and mass exhibited no correlation suggesting that BSA and IgG1 may have different transport mechanisms. Interestingly, immunoglobulin G1 and G2 concentration and mass exhibited strong correlations suggesting that also some unknown mechanism of immunoglobulin G2 appearance in colostrum is occurring. Finally, no measured protein exhibited any correlation with the activity of lactate dehydrogenase in colostrum.

  7. 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.

  8. Self-assembled albumin nanoparticles as a nanocarrier for aclacinomycin A

    Science.gov (United States)

    Gong, Guangming; Liu, Wenya; Wang, Shudong

    2016-11-01

    This study aimed to reduce the cytotoxicity and improve the targeting of aclacinomycin (ACM) by covalently coupling it with amino-oxyacetic acid (AOA) to generate an active intermediate, AOA-ACM. AOA-ACM was conjugated with self-assembled human serum albumin (HSA) nanoparticles constructed using tris(2-carboxyethyl)phosphine (TCEP) as disulfide bond breaking molecules in an ‘opening stage-intermediate-closing stage’ route, in which the hydrophobic interaction, interchange of sulfhydryl and hydrogen bond may be the key factors in the assembling process. Conjugation between ACM and albumin nanoparticles was found to occur at an ACM ketone site using 1H-NMR and 13C-NMR matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass analysis indicated that the drug loading efficiency of ACM conjugated with HSA nanoparticles (NPs-ACM) was 7.4% (molar ratio = 6:1). The release of NPs-ACM was pH dependent. In vivo studies indicated that NPs-ACM exhibited fourfold higher tumor targeting capability on S180-tumor-bearing mice compared with the free ACM (p ACM was reduced compared with the free ACM. Albumin carrier altered the blood pharmacokinetics and distribution of ACM. Hence, the NPs-ACM prodrug is ideal tumor targeting drug carriers for ACM, and the easy approach developed in this study for active intermediate and prodrug preparation can be applied to other pharmacological substances containing ketone groups. The method of preparing HSA-blank nanoparticles through TCEP reduction could be adopted to improve the water solubility of lipophilic drugs and their tumor-targeting specificity by fabricating HSA-lipophilic drug nanoparticles.

  9. Association between urinary albumin excretion and intraocular pressure in type 2 diabetic patients without renal impairment.

    Directory of Open Access Journals (Sweden)

    Jin A Choi

    Full Text Available BACKGROUND: To assess the relationship between urinary albumin excretion and intraocular pressure (IOP in type 2 diabetes patients without renal impairment. METHODS: We explored the effects of albuminuria on high IOP in 402 non-glaucomatous type 2 diabetes without renal impairment who participated in the 2011 Korean National Health and Nutrition Examination Survey (KNHANES. Multiple logistic regression analysis was used to assess the relationship between log-transformed albumin/creatinine ratio (ACR tertiles and an IOP of ≥ 18 mmHg after adjusting for age, gender, hypertension, body mass index, triglycerides, area of residence, and education level. RESULTS: Subjects with a high IOP ≥ 18 mmHg were more likely to be current smokers (P = 0.038, heavy drinkers (P = 0.006, and to have high systolic blood pressure (P = 0.016, triglycerides (P = 0.008, and a higher log-transformed ACR (P = 0.022.In multivariate regression analysis, ACR tertile was associated with the prevalence of high IOP significantly (P = 0.022. The associations between ACR tertiles and high IOP were significant in overweight patients and those with abdominal obesity (P = 0.003 and 0.003, respectively. In contrast, there were no associations in the subgroup of patients who were not overweight and those without abdominal obesity (P = 0.291 and 0.561, respectively. CONCLUSIONS: Urinary albumin excretion is associated with high IOP in the type 2 diabetes population without renal insufficiency. The effect of the albuminuria on IOP was evident in a subgroup of patients with components of metabolic syndrome.

  10. Albumin Test

    Science.gov (United States)

    Advertisement Proceeds from website advertising help sustain Lab Tests Online. AACC is a not-for-profit organization and does not endorse non-AACC products and services. Advertising & Sponsorship: Policy | Opportunities ...

  11. Copper Selenide Nanosnakes: Bovine Serum Albumin-Assisted Room Temperature Controllable Synthesis and Characterization

    OpenAIRE

    Huang Peng; Kong Yifei; Li Zhiming; Gao Feng; Cui Daxiang

    2010-01-01

    Abstract Herein we firstly reported a simple, environment-friendly, controllable synthetic method of CuSe nanosnakes at room temperature using copper salts and sodium selenosulfate as the reactants, and bovine serum albumin (BSA) as foaming agent. As the amounts of selenide ions (Se2−) released from Na2SeSO3 in the solution increased, the cubic and snake-like CuSe nanostructures were formed gradually, the cubic nanostructures were captured by the CuSe nanosnakes, the CuSe nanosnakes gre...

  12. Study on the Interaction between Lanthanide Cationic Porphyrin Complex and Bovine Serum Albumin

    Institute of Scientific and Technical Information of China (English)

    LIU, Peng; LIU, Yi; LI, Xi; HUANG, Wei-Guo

    2007-01-01

    The interaction between lanthanide cationic porphyrin and bovine serum albumin (BSA) was studied by fluorescence and UV-Vis spectrum. The static quenching of BSA was observed in the presence of YbTMPyP. According to the thermodynamic parameters, this binding was regarded as "enthalpy-driven" reaction. Furthermore,YbTMPyP is so close to the residues of BSA that molecular resonance energy transfer occurs between them. Besides, the red drift and hypochromicity of absorption spectrum of YbTMPyP were accompanied with the binding reaction.

  13. Antioxidant activity of bovine serum albumin binding amino acid Schiff-bases metal complexes

    Institute of Scientific and Technical Information of China (English)

    2007-01-01

    Glutamic acid-salicylaldehyde Schiff-base metal complexes are bound into bovine serum albumin (BSA), which afforded BSA binding Schiff-base metal complexes (BSA-SalGluM, M=Cu, Co, Ni, Zn). The BSA binding metal complexes were characterized by UV-vis spectra and Native PAGE. It showed that the protein structures of BSA kept after coordinating amino acid Schiff-bases metal complexes. The effect of the antioxidant activity was investigated. The results indicate that the antioxidant capacity of BSA increased more than 10 times after binding Schiff-base metal complexes.

  14. Impaired aerobic work capacity in insulin dependent diabetics with increased urinary albumin excretion

    DEFF Research Database (Denmark)

    Jensen, T; Richter, Erik; Feldt-Rasmussen, Bo;

    1988-01-01

    To assess whether decreased aerobic work capacity was associated with albuminuria in insulin dependent diabetics aerobic capacity was measured in three groups of 10 patients matched for age, sex, duration of diabetes, and degree of physical activity. Group 1 comprised 10 patients with normal...... were not explained by differences in metabolic control or the degree of autonomic neuropathy. Thus the insulin dependent diabetics with only slightly increased urinary albumin excretion had an appreciably impaired aerobic work capacity which could not be explained by autonomic neuropathy...

  15. Total protein, albumin and low-molecular-weight protein excretion in HIV-positive patients

    Directory of Open Access Journals (Sweden)

    Campbell Lucy J

    2012-08-01

    Full Text Available Abstract Background Chronic kidney disease is common in HIV positive patients and renal tubular dysfunction has been reported in those receiving combination antiretroviral therapy (cART. Tenofovir (TFV in particular has been linked to severe renal tubular disease as well as proximal tubular dysfunction. Markedly elevated urinary concentrations of retinal-binding protein (RBP have been reported in patients with severe renal tubular disease, and low-molecular-weight proteins (LMWP such as RBP may be useful in clinical practice to assess renal tubular function in patients receiving TFV. We analysed 3 LMWP as well as protein and albumin in the urine of a sample of HIV positive patients. Methods In a cross-sectional fashion, total protein, albumin, RBP, cystatin C, and neutrophil gelatinase-associated lipocalin (NGAL were quantified in random urine samples of 317 HIV positive outpatients and expressed as the ratio-to-creatinine (RBPCR, CCR and NGALCR. Exposure to cART was categorised as none, cART without TFV, and cART containing TFV and a non-nucleoside reverse-transcriptase-inhibitor (TFV/NNRTI or TFV and a protease-inhibitor (TFV/PI. Results Proteinuria was present in 10.4 % and microalbuminuria in 16.7 % of patients. Albumin accounted for approximately 10 % of total urinary protein. RBPCR was within the reference range in 95 % of patients while NGALCR was elevated in 67 % of patients. No overall differences in urine protein, albumin, and LMWP levels were observed among patients stratified by cART exposure, although a greater proportion of patients exposed to TFV/PI had RBPCR >38.8 μg/mmol (343 μg/g (p = 0.003. In multivariate analyses, black ethnicity (OR 0.43, 95 % CI 0.24, 0.77 and eGFR 2 (OR 3.54, 95 % CI 1.61, 7.80 were independently associated with upper quartile (UQ RBPCR. RBPCR correlated well to CCR (r2 = 0.71, but not to NGALCR, PCR or ACR. Conclusions In HIV positive patients, proteinuria was predominantly of

  16. Improved drug targeting of cancer cells by utilizing actively targetable folic acid-conjugated albumin nanospheres.

    Science.gov (United States)

    Shen, Zheyu; Li, Yan; Kohama, Kazuhiro; Oneill, Brian; Bi, Jingxiu

    2011-01-01

    Folic acid-conjugated albumin nanospheres (FA-AN) have been developed to provide an actively targetable drug delivery system for improved drug targeting of cancer cells with reduced side effects. The nanospheres were prepared by conjugating folic acid onto the surface of albumin nanospheres using 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDAC) as a catalyst. To test the efficacy of these nanospheres as a potential delivery platform, doxorubicin-loaded albumin nanospheres (DOX-AN) and doxorubicin-loaded FA-AN (FA-DOX-AN) were prepared by entrapping DOX (an anthracycline, antibiotic drug widely used in cancer chemotherapy that works by intercalating DNA) into AN and FA-AN nanoparticles. Cell uptake of the DOX was then measured. The results show that FA-AN was incorporated into HeLa cells (tumor cells) only after 2.0h incubation, whereas HeLa cells failed to incorporate albumin nanospheres without conjugated folic acid after 4.0h incubation. When HeLa cells were treated with the DOX-AN, FA-DOX-AN nanoparticles or free DOX, cell viability decreased with increasing culture time (i.e. cell death increases with time) over a 70h period. Cell viability was always the lowest for free DOX followed by FA-DOX-AN4 and then DOX-AN. In a second set of experiments, HeLa cells washed to remove excess DOX after an initial incubation for 2h were incubated for 70h. The corresponding cell viability was slightly higher when the cells were treated with FA-DOX-AN or free DOX whilst cells treated with DOX-AN nanoparticles remained viable. The above experiments were repeated for non-cancerous, aortic smooth muscle cells (AoSMC). As expected, cell viability of the HeLa cells (with FA receptor alpha, FRα) and AoSMC cells (without FRα) decreased rapidly with time in the presence of free DOX, but treatment with FA-DOX-AN resulted in selective killing of the tumor cells. These results indicated that FA-AN may be used as a promising actively targetable drug delivery system to improve drug

  17. Photophysical investigations of squaraine and cyanine dyes and their interaction with bovine serum albumin

    Science.gov (United States)

    Saikiran, M.; Sato, D.; Pandey, S. S.; Kato, T.

    2016-04-01

    A model far-red sensitive symmetrical squaraine dye (SQ-3) and unsymmetrical near infra-red sensitive cyanine dye (UCD-1) bearing direct-COOH functionalized indole ring were synthesized, characterized and subjected to photophysical investigations including their interaction with bovine serum albumin (BSA) as a model protein in phosphate buffer solution (PBS). Both of the dyes exhibit strong interaction with BSA in phosphate buffer with high apparent binding constant. A judicious tuning of hydrophobic main backbone with reactive functionality for associative interaction with active site of BSA has been found to be necessary for BSA detection in PBS.

  18. Long-term oral sodium bicarbonate supplementation does not improve serum albumin levels in hemodialysis patients.

    Science.gov (United States)

    Bossola, Maurizio; Giungi, Stefania; Tazza, Luigi; Luciani, Giovanna

    2007-01-01

    Metabolic acidosis, a frequent event in hemodialysis patients, has been implicated as a potential cause of protein-energy malnutrition. Unfortunately, correction of metabolic acidosis by means of high bicarbonate concentration in the dialysate does not seem to lead to significant changes in nutritional parameters. The project was a single-arm, open-label, 12-month pilot study at a university-based tertiary care center aimed at evaluating whether correction of metabolic acidosis through long-term oral sodium bicarbonate supplementation improves serum albumin levels and other nutritional parameters in patients undergoing maintenance hemodialysis. Twenty highly acidotic hemodialysis patients patients were invited to consume an oral supplementation of sodium bicarbonate (1 g, thrice daily), for 12 months. Patients were followed at baseline and every month, until month 12. At each follow-up visit, dry body weight, BMI, blood pressure, presence of edema, venous bicarbonate, and serum albumin were measured. Total lymphocyte count, fasting total cholesterol and C-reactive protein were assessed every 2 months. At baseline and at 12 months, the subjective global assessment of nutritional status and the protein equivalent of nitrogen appearance normalized to actual body weight were determined. Plasma bicarbonate level rose from 18.1 +/- 2.7 to 22.1 +/- 4.5 mmol/l after 10 months (p = 0.001). Mean serum albumin levels were 3.8 +/- 0.2 mg/dl at baseline and 3.9 +/- 0.2 at the end of the study. Repeated measure ANOVA showed that there was no significant effect of bicarbonate treatment on serum albumin levels (p = 0.29), dry weight (p = 0.1), serum total cholesterol (p = 0.97), total lymphocyte count (p = 0.69), or C-reactive protein (p = 0.85). Mean subjective global assessment score was 4.53 +/- 0.37 at baseline and 4.58 +/- 0.54 at 12 months (p = 0.1). Mean nPNA (g/kg/day) was 0.86 +/- 0.05 at baseline and 0.85 +/- 0.08 at month 12. The present study demonstrates that long

  19. Preparation of Arsenic Trioxide Albumin Microspheres and its Release Characteristics in Vitro

    Institute of Scientific and Technical Information of China (English)

    ZHOU Jie; ZENG Fuqing; GAO Xiang; XIE Shusheng; WEI Shuli

    2005-01-01

    Summary: Arsenic trioxide albumin microspheres (As2O3-BSA-NS) were prepared by using methods of chemical cross-linking. The desirability function (DF), calculated according to the size (0.05). The release experiment in vitro showed that As2O3 in As2O3-BSA-NS was released more slower than pure As2O3. It was concluded that regular As2O3-BSA-NS may be prepared by the methods of chemical cross-linking, which was optimized by orthogonal experimental analysis of different factors, and the microspheres can release As2O3 slowly.

  20. Interaction of potassium mono and di phosphates with bovine serum albumin studied by fluorescence quenching method.

    Science.gov (United States)

    Bakkialakshmi, S; Shanthi, B; Chandrakala, D

    2011-03-01

    The interactions between potassium mono and di phosphates and bovine serum albumin (BSA) were studied using fluorescence spectroscopy (FS) and ultraviolet spectroscopy (UV). The experimental results showed that the potassium mono and di phosphates could insert into the BSA and quench the inner fluorescence of BSA by forming the potassium mono phosphate-BSA and pottassium di phosphate-BSA complexes. It was found that the static quenching was the main reason leading to the fluorescence quenching. It was conformed by XRD and SEM techniques.

  1. Valproate and palmitate binding to serum albumin in valproate-treated patients. Relation to obesity

    DEFF Research Database (Denmark)

    Vorum, H; Gram, L; Honoré, B

    1993-01-01

    Binding of valproate and palmitate to serum albumin was studied in 29 valproate-treated epileptic patients. The results were compared with similar observations in a reference group of 43 non valproate-treated individuals. The binding affinity for palmitate was decreased (P ... in increased availability of long-chain fatty acids (P = 0.008) due to competitive valproate binding in the valproate-treated patients. The findings support a hypothesis on the pathogenesis of obesity as a complication of valproate treatment of epilepsy. Udgivelsesdato: 1993-Sep...

  2. 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.

  3. Investigation of the Interaction between Adenosine and Human Serum Albumin by Fluorescent Spectroscopy and Molecular Modeling

    Institute of Scientific and Technical Information of China (English)

    CUI Feng-Ling; WANG Jun-Li; LI Fang; FAN Jing; QU Gui-Rong; YAO Xiao-Jun; LEI Bei-Lei

    2008-01-01

    The binding interaction of adenosine with human serum albumin (HSA) was investigated under simulative physiological conditions by fluorescence spectroscopy in combination with a molecular modeling method. A strong fluorescence quenching reaction of adenosine to HSA was observed and the quenching mechanism was suggested as static quenching according to the Stern-Volmer equation. The binding constants (K) at different temperatures as well as thermodynamic parameters, enthalpy change (ΔH) and entropy change (ΔS), were calculated according to relevant fluorescent data and Vant'Hoff equation. The hydrophobic interaction was a predominant intermolecular force in order to stabilize the complex, which was in agreement with the results of molecular modeling study.

  4. Uptake of albumin nanoparticle surface modified with glycyrrhizin by primary cultured rat hepatocytes

    Institute of Scientific and Technical Information of China (English)

    Sheng-Jun Mao; Shi-Xiang Hou; Ru He; Liang-Ke Zhang; Da-Peng Wei; Yue-Qi Bi; Hui Jin

    2005-01-01

    AIM: To investigate the uptake difference between bovine serum albumin nanoparticle (BSA-NP) and bovine serum albumin nanoparticles with their surface modified byglycyrrhizin (BSA-NP-GL) and to develop a novel hepatocyte targeting BSA-NP-GL based on active targeting technology mediated by specific binding site of GL on rat cellular membrane. METHODS: Calcein loaded bovine serum albumin nanoparticles (Cal-BSA-NP) were prepared by desolvation process. Glycyrrhizin was conjugated to the surface reactive amino groups (SRAG) of Cal-BSA-NP by sodium periodate oxidization, which resulted in calcein-loaded bovine serum albumin nanoparticles with their surface modified by glycyrrhizin (Cal-BSA-NP-GL). The morphology of the two types of prepared nanoparticles (NP) was observed by transmission electron microscopy. The diameter of NP was measured with a laser particle size analyzer. The interaction between Cal-BSA-NP-GL and primary cultured hepatocytes was studied through cellular uptake experiments. The uptake amount of Cal-BSA-NPGL and Cal-BSA-NP by rat hepatocytes was determinedby fluorospectrophotometry. Uptake characteristics were investigated through experiments of competitive inhibition of specific binding site of GL. RESULTS: Both Cal-BSA-NP-GL and Cal-BSA-NP had regular spherical surfaces. The average diameter of CalBSA-NP-GL and Cal-BSA-NP was 77 and 79 nm respectively. The uptake amount of the two NP by hepatocytes reached its maximum at 2 h after incubation. The uptake amount of Cal-BSA-NP-GL by rat hepatocytes was 4.43-fold higher than that of Cal-BSA-NP. There was a significant difference in the uptake of Cal-BSA-NP-GL and Cal-BSA-NP by hepatocytes (P<0.01). The uptake of Cal-BSA-NP-GL was inhibited when GL was added previously to isolated rat hepatocytes, and the uptake of Cal-BSA-NP was not affected by GL.CONCLUSION: A binding site of GL is present on the surface of rat hepatocytes, BSA-NP-GL may be internalized via this site by hepatocytes and can be used as

  5. Drug-induced immune hemolytic anemia associated with albumin-bound paclitaxel.

    Science.gov (United States)

    Thomas, Roby; Shillingburg, Alexandra

    2015-08-01

    Drug-induced immune hemolytic anemia (DIIHA) is rare, with only 1 patient in 1 million affected by the condition.1 Garratty identified 125 drugs indicated in DIIHA of which 11% were antineoplastic agents, and neither paclitaxel nor albumin-bound paclitaxel were included.2 In addition, we did not find any reports in our own search of the literature. Taxanes are known to cause anemia as a result of their myelosuppressive effects, but an immune hemolysis is rare. To our knowledge, we present here the first case of DIIHA with nab-paclitaxel.

  6. Bovine serum albumin detection and quantitation based on capacitance measurements of liquid crystals

    Science.gov (United States)

    Lin, Chi-Hao; Lee, Mon-Juan; Lee, Wei

    2016-08-01

    Liquid crystal (LC)-based biosensing is generally limited by the lack of accurate quantitative strategies. This study exploits the unique electric capacitance properties of LCs to establish quantitative assay methods for bovine serum albumin (BSA) biomolecules. By measuring the voltage-dependent electric capacitance of LCs under an alternating-current field with increasing amplitude, positive correlations were derived between the BSA concentration and the electric capacitance parameters of LCs. This study demonstrates that quantitative analysis can be achieved in LC-based biosensing through electric capacitance measurements extensively employed in LCD research and development.

  7. Nanoparticle Albumin Bound Paclitaxel in the Treatment of Human Cancer: Nanodelivery Reaches Prime-Time?

    Directory of Open Access Journals (Sweden)

    Iole Cucinotto

    2013-01-01

    Full Text Available Nanoparticle albumin bound paclitaxel (nab-paclitaxel represents the first nanotechnology-based drug in cancer treatment. We discuss the development of this innovative compound and report the recent changing-practice results in breast and pancreatic cancer. A ground-breaking finding is the demonstration that nab-paclitaxel can not only enhance the activity and reduce the toxicity of chromophore-diluted compound, but also exert activity in diseases considered refractory to taxane-based treatment. This is the first clinical demonstration of major activity of nanotechnologically modified drugs in the treatment of human neoplasms.

  8. Nanoparticle Albumin Bound Paclitaxel in the Treatment of Human Cancer: Nanodelivery Reaches Prime-Time?

    Science.gov (United States)

    Cucinotto, Iole; Fiorillo, Lucia; Gualtieri, Simona; Arbitrio, Mariamena; Ciliberto, Domenico; Staropoli, Nicoletta; Grimaldi, Anna; Luce, Amalia; Tassone, Pierfrancesco; Caraglia, Michele; Tagliaferri, Pierosandro

    2013-01-01

    Nanoparticle albumin bound paclitaxel (nab-paclitaxel) represents the first nanotechnology-based drug in cancer treatment. We discuss the development of this innovative compound and report the recent changing-practice results in breast and pancreatic cancer. A ground-breaking finding is the demonstration that nab-paclitaxel can not only enhance the activity and reduce the toxicity of chromophore-diluted compound, but also exert activity in diseases considered refractory to taxane-based treatment. This is the first clinical demonstration of major activity of nanotechnologically modified drugs in the treatment of human neoplasms. PMID:23738077

  9. Small angle neutron scattering studies on the interaction of cationic surfactants with bovine serum albumin

    Indian Academy of Sciences (India)

    Nuzhat Gull; S Chodankar; V K Aswal; Kabir-Ud-Din

    2008-11-01

    The structure of the protein–surfactant complex of bovine serum albumin (BSA) and cationic surfactants has been studied by small angle neutron scattering. At low concentrations, the CTAB monomers are observed to bind to the protein leading to an increase in its size. On the other hand at high concentrations, surfactant molecules aggregate along the unfolded polypeptide chain of the protein resulting in the formation of a fractal structure representing a necklace model of micelle-like clusters randomly distributed along the polypeptide chain. The fractal dimension as well as the size and number of micelles attached to the complex have been determined.

  10. Human serum albumin adsorption on TiO2 from single protein solutions and from plasma.

    Science.gov (United States)

    Sousa, S R; Moradas-Ferreira, P; Saramago, B; Melo, L Viseu; Barbosa, M A

    2004-10-26

    In the present work, the adsorption of human serum albumin (HSA) on commercially pure titanium with a titanium oxide layer formed in a H(2)O(2) solution (TiO(2) cp) and on TiO(2) sputtered on Si (TiO(2) sp) was analyzed. Adsorption isotherms, kinetic studies, and work of adhesion determinations were carried out. HSA exchangeability was also evaluated. Surface characterization was performed by atomic force microscopy (AFM), X-ray photoelectron spectroscopy (XPS), and wettability studies. The two TiO(2) surfaces have very distinct roughnesses, the TiO(2) sp having a mean R(a) value 14 times smaller than the one of TiO(2) cp. XPS analysis revealed consistent peaks representative of TiO(2) on sputtered samples as well as on Ti cp substrate after 48 h of H(2)O(2) immersion. Nitrogen was observed as soon as protein was present, while sulfur, present in disulfide bonds in HSA, was observed for concentrations of protein higher than 0.30 mg/mL. The work of adhesion was determined from contact angle measurements. As expected from the surface free energy values, the work of adhesion of HSA solution is higher for the TiO(2) cp substrate, the more hydrophilic one, and lower for the TiO(2) sp substrate, the more hydrophobic one. The work of adhesion between plasma and the substrates assumed even higher values for the TiO(2) cp surface, indicating a greater interaction between the surface and the complex protein solutions. Adsorption studies by radiolabeling of albumin ((125)I-HSA) suggest that rapid HSA adsorption takes place on both surfaces, reaching a maximum value after approximately 60 min of incubation. For the higher HSA concentrations in solution, a multilayer coverage was observed on both substrates. After the adsorption step from single HSA solutions, the exchangeability of adsorbed HSA molecules by HSA in solution was evaluated. The HSA molecules adsorbed on TiO(2) sp seem to be more easily exchanged by HSA itself than those adsorbed on TiO(2) cp after 24 h. In

  11. Interaction of Surface-active Fluorescence Probes with Bovine Serum Albumin

    Institute of Scientific and Technical Information of China (English)

    Tong Kuan XU; Xing Hai SHEN; Na LI; Hong Cheng GAO

    2005-01-01

    The binding between three surface-active substituted 3H-indole fluorescence probes and bovine serum albumin (BSA) in aqueous solution was studied using fluorescence quenching. The binding constants of 3H-indole molecules with BSA were obtained. According to the Forster resonance energy transfer theory, the distances between 3H-indole molecules and tryptophan of BSA were calculated. The results show that the oligoethyloxyethylene chain of 3H-indole molecules is longer, the binding between them is stronger, the energy transfer efficiency is higher,and the distance between tryptophan and 3H-indole is nearer.

  12. Role of oxidative stress in physiological albumin glycation: a neglected interaction

    OpenAIRE

    Vlassopoulos, A.; Lean, M.E.J.; Combet, E.

    2013-01-01

    Protein glycation is a key mechanism involved in chronic disease development in both diabetic and nondiabetic individuals. About 12–18% of circulating proteins are glycated in vivo in normoglycemic blood, but in vitro studies have hitherto failed to demonstrate glucose-driven glycation below a concentration of 30 mM. Bovine serum albumin (BSA), reduced BSA (mercaptalbumin) (both 40 g/L), and human plasma were incubated with glucose concentrations of 0–30 mM for 4 weeks at 37 °C. All were test...

  13. Phagocytic labelling of leukocytes with /sup 99m/Tc-albumin colloid for nuclear imaging

    Energy Technology Data Exchange (ETDEWEB)

    Marcus, C.S.; Kuperus, J.H.; Butler, J.A.; Henneman, P.L.; Salk, R.D.; Biying Chen; Vivian, M.R.P.; Yamanaka, L.M. (Harbor-UCLA Medical Center, Torrance, CA (USA))

    1989-01-01

    A procedure is described for the phagocytic labeling of white blood cells (WBC) with high specific activity /sup 99m/Tc-albumin colloid (TAC). The preparation contains approximately equal activities of granulocytes and monocytes. Heparinized whole blood (40 cm/sup 3/) yields a preparation containing a total of 148-222 MBq (4-6 mCi) TAC-WBC including about 20% free TAC. The complete preparation time is 75 min. Imaging is completed 30 min to 4h post administration of the TAC-WBC. Quality control methods and imaging protocols are described. (author).

  14. 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.

  15. Interaction between Janus Green B and bovine serum albumin:Electrochemistry and spectroscopy studies

    Institute of Scientific and Technical Information of China (English)

    Neslihan (O)zdemir; Serkan (O)zdemir; Ender Bicer

    2011-01-01

    In this study, voltammetric and spectroscopic investigation of the interaction between Janus Green B (JGB) and bovine serum albumin (BSA) was reported. The interaction was observed at Britton-Robinson buffer (pH 7.0). When JGB was added to solution containing BSA, the peak currents of BSA decrease with the increasing of JGB concentrations which is due to the interaction of JGB and BSA. The binding constant of JGB with BSA was obtained by voltammetric data. Also, this interaction was supported by means of UV-vis spectroscopic measurements. The UV-vis absorption spectra of JGB in the presence of BSA decrease with the increasing of BSA concentrations.

  16. [Study of the content of alpha-fetoprotein and serum albumin in the vitreous body of the eye of human embryos].

    Science.gov (United States)

    Panova, I G; Tatikolov, A S

    2011-01-01

    The content of serum albumin and alpha-fetoprotein in the vitreous body of the eyes of human embryos from the 16th through the 24th week was investigated. It was detected that albumin and alpha-fetoprotein in the vitreous body of human eyes are presented in equal molar concentrations in the 16th week. There is 1.5-fold increased concentration of alpha-fetoprotein in comparison to albumin during the 17th week. Seventeen weeks later, there was a reduction in the concentration of both proteins. It was reported that cyanine dye, used for detection of albumin, does not interact with alpha-fetoprotein.

  17. Increased transvascular escape rate and lymph drainage of albumin in pigs during intravenous diuretic medication. Relations to treatment in man and transport mechanisms

    DEFF Research Database (Denmark)

    Henriksen, Jens Henrik Sahl; Parving, H H; Lassen, N A;

    1982-01-01

    Transvascular escape rate of albumin (TERalb, i.e. the fraction of intravascular mass of albumin (IVMalb) passing to (or during steady state returning from) the extravascular space per unit time) was determined from the initial disappearance rate of i.v. injected radioiodinated serum albumin.......05). Pressures in artery, right atrium, hepatic and portal veins did not change significantly from control to diuretic period. TERalb equals the lymphatic return rate of albumin provided the transport mechanisms are filtrative-convective (i.e. no local back transport). Additional measurements in five pigs...

  18. Role of zinc along with ascorbic acid and folic acid during long-term in vitro albumin glycation.

    Science.gov (United States)

    Tupe, Rashmi Santosh; Agte, Vaishali Vilas

    2010-02-01

    The present study aimed to investigate the role of Zn alone and in the presence of ascorbic acid (AA) and folic acid (FA) in albumin glycation. Glycation was performed by incubations of bovine serum albumin with glucose at 37 degrees C along with Zn, AA or FA separately and Zn + AA or Zn + FA for 150 d. Glycation-mediated modifications were monitored as fluorescence of advanced glycation endproducts, carbonyl formation, beta aggregation (thioflavin T and Congo red dyes), albumin-bound Zn, thiol groups and glycated aggregate's toxicity in HepG2 cells. Zn inhibited glycation and beta aggregation, probably due to observed higher protein-bound Zn. It also protected protein thiols and increased cell survival. AA and FA enhanced glycation, which was lowered in Zn-co-incubated samples. FA increased albumin-bound Zn and showed maximum cell survival. Although these results warrant further in vivo investigation, the present data help in the understanding of the interplay of Zn with micronutrients in albumin glycation.

  19. Changes in albumin/platelet interaction with an artificial surface--due to a antibiotics, pyridoxal phosphate, and lymphocytes

    Energy Technology Data Exchange (ETDEWEB)

    Chandy, T.; Sharma, C.P.

    1988-04-01

    Protein adsorption and platelet adhesion are two important biological processes arising at the blood prosthetic interface. The effect of certain antibiotics, namely, neomycin, gentamicin, ampicillin, penicillin-G, and streptomycin to modulate the albumin polycarbonate surface interaction was investigated using /sup 125/I albumin from a protein mixture in the presence and absence of isolated calf lymphocytes. This study also demonstrated the changes in platelet-surface adhesion with these antibiotics. The effect of pyridoxal phosphate to modulate the red blood cell-mediated platelet-surface attachment was also attempted. It appears from pyridoxal phosphate studies that pyridoxal 5'-phosphate (PLP) could modify the surface-platelet attachment. It also inhibited the fibrinogen-induced platelet adhesion. It seems, the addition of antibiotics to the polymerprotein system increased the level of surface-bound albumin variably whereas lymphocytes incubated in the medium did not affect the surface-albumin concentration with time course. These antibiotics also inhibited the surface-induced platelet adhesion to variable degrees. Our earlier studies have indicated that certain antibiotics or antiplatelet drugs can inhibit the fibrinogen binding to an artificial surface. Therefore, it may be possible that the enhanced albumin-surface concentration or reduced fibrinogen-surface binding, in the presence of these antibiotics, may itself be one of the parameter for a reduced platelet-surface attachment, which may also improve the blood compatibility of the substrate. A better understanding of the mechanism of antibiotics is needed in in vivo conditions to correlate these findings.

  20. Unraveling the energetics and mode of the recognition of antibiotics tetracycline and rolitetracycline by bovine serum albumin.

    Science.gov (United States)

    Choudhary, Sinjan; Kishore, Nand

    2012-11-01

    An understanding of the detailed energetics and mechanism of the binding of drugs with target proteins is essential for devising guidelines to synthesize new drugs. Binding of the antibiotic drugs tetracycline and rolitetracycline with serum albumin has been studied by a combination of isothermal titration calorimetry, differential scanning calorimetry, steady-state and time-resolved fluorescence, and circular dichroism spectroscopies. Both tetracycline and rolitetracycline bind to bovine serum albumin in a sequential manner with first binding being the major binding event with an association constant of the order of 10(4) for tetracycline and 10(3) for rolitetracycline, respectively. Ionic strength dependence and binding in the presence of tetrabutylammonium bromide and sucrose indicate involvement of a mix of hydrophobic, ionic, and hydrogen bonding interactions. The isothermal titration calorimetry results for the binding of these drugs to bovine serum albumin in the presence of warfarin and in the presence of each other indicate that both these drugs share binding site 2 on bovine serum albumin. The differential scanning calorimetry results provide quantitative information on the effect of drugs on the stability of bovine serum albumin. A comparison of isothermal titration calorimetry and fluorescence results demonstrates that the former technique has been able to explain the sequential binding events that can be missed by the fluorescence measurements.

  1. Environment sensitive fluorescent analogue of biologically active oxazoles differentially recognizes human serum albumin and bovine serum albumin: Photophysical and molecular modeling studies

    Science.gov (United States)

    Maiti, Jyotirmay; Biswas, Suman; Chaudhuri, Ankur; Chakraborty, Sandipan; Chakraborty, Sibani; Das, Ranjan

    2017-03-01

    An environment sensitive fluorophore, 4-(5-(4-(dimethylamino)phenyl)oxazol-2-yl)benzoic acid (DMOBA), that closely mimics biologically active 2,5-disubstituited oxazoles has been designed to probe two homologous serum proteins, human serum albumin (HSA) and bovine serum albumin (BSA) by means of photophysical and molecular modeling studies. This fluorescent analogue exhibits solvent polarity sensitive fluorescence due to an intramolecular charge transfer in the excited state. In comparison to water, the steady state emission spectra of DMOBA in BSA is characterized by a greater blue shift ( 10 nm) and smaller Stokes' shift ( 5980 cm- 1) in BSA than HSA (Stokes'shift 6600 cm- 1), indicating less polar and more hydrophobic environment of the dye in the former than the latter. The dye-protein binding interactions are remarkably stronger for BSA than HSA which is evident from higher value of the association constant for the DMOBA-BSA complex (Ka 5.2 × 106 M- 1) than the DMOBA-HSA complex (Ka 1.0 × 106 M- 1). Fӧrster resonance energy transfer studies revealed remarkably less efficient energy transfer (8%) between the donor tryptophans in BSA and the acceptor DMOBA dye than that (30%) between the single tryptophan moiety in HSA and the dye, which is consistent with a much larger distance between the donor (tryptophan)-acceptor (dye) pair in BSA (34.5 Å) than HSA (25.4 Å). Site specific competitive binding assays have confirmed on the location of the dye in Sudlow's site II of BSA and in Sudlow's site I of HSA, respectively. Molecular modeling studies have shown that the fluorescent analogue is tightly packed in the binding site of BSA due to strong steric complementarity, where, binding of DMOBA to BSA is primarily dictated by the van der Waals and hydrogen bonding interactions. In contrast, in HSA the steric complementarity is less significant and binding is primarily guided by polar interactions and van der Waals interactions appear to be less significant in the

  2. 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

  3. A comparative study on the effect of docetaxel-albumin nanoparticles and docetaxel-loaded PEG-albumin nanoparticles against non-small cell lung cancer.

    Science.gov (United States)

    Jin, Guangming; Jin, Mingji; Yin, Xuezhe; Jin, Zhehu; Chen, Liqing; Gao, Zhonggao

    2015-11-01

    The present study mainly compared the effect of docetaxel-albumin nanoparticles (DANPs) and docetaxel-loaded PEG-albumin nanoparticles (PEG-DANPs) against non-small cell lung cancer (NSCLC). We made systematic assessments on these three drugs against NSCLC both in vitro and in vivo. With the purpose of eliminating side-effects of the commercial formulation (Tween-80) and prolonging the blood circulation time, we used emulsion-evaporation cross-link method to prepare DANPs and PEG-DANPs. The DANPs had an average particle size of 163.4 ± 3.76 nm, a zeta potential of -19.4 ± 0.18 mV, a polydispersity index of 0.143 ± 0.03, a drug loading of 8.71 ± 0.98%, and an encapsulation efficiency of 93.58 ± 0.86%; the average particle size of PEG-DANPs is 169.19 ± 2.36 nm, zeta potential is -18.2 ± 0.21 mV, with a polydispersity index of 1.56 ± 0.05, a drug loading of 8.72 ± 1.05% and an encapsulation efficiency of 95.4 ± 5.5%. PEG-DANPs showed a dose- and time-dependent efficacy in cytotoxicity studies in vitro; the hemolysis test indicated that PEG-DANPs had less hemocytolysis than Aisu® and DANPs; in addition, a more prolonged circulation time and sustained in vitro release behavior were observed in the PEG-DANPs compared with Aisu® and DANPs; the cellular uptake test in vitro demonstrated that PEG-DANPs could be absorbed easier into the nucleus; furthermore, the tumor growth of NSCLC-bearing nude mice in vivo was reduced the most by PEG-DANPs. In conclusion, the PEG-DANPs have the lowest side-effects, the highest antitumor activity with the longest blood circulation time of the three drugs, and it will provide an alternative to patients with NSCLC.

  4. 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.

  5. 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.

  6. 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.

  7. A proton NMR relaxation study of water dynamics in bovine serum albumin nanoparticles.

    Science.gov (United States)

    Belotti, Monica; Martinelli, Andrea; Gianferri, Raffaella; Brosio, Elvino

    2010-01-14

    Water dynamics and compartmentation in glutaraldehyde cross-linked bovine serum albumin nanoparticles have been investigated by an integrated nuclear magnetic resonance (NMR) protocol based on water relaxation times and self-diffusion coefficients measurements. Multi-exponentially of water relaxation curves has been accounted for according to a diffusive and chemical exchange model (see B. P. Hills, S. F. Takacs and P. S. Belton, Mol. Phys., 1989, 67(4), 903, and Mol. Phys., 1989, 67(4), 913; E. Brosio, M. Belotti and R. Gianferri, in Food Science and Technology: New Research, ed. L. V. Greco and M. N. Bruno, Nova Science Publishers, Hauppauge (NY), 2008) that made it possible to single out water molecules in the molecular spaces in the interior of albumin nanoparticles, in the meso-cavities formed by packed nanoparticles and in the meniscus on top of the nanoparticles suspension. A quantitative rationalization of T(2) values of water different components allowed morphological information to be acquired as for the size of water filled compartments, while self-diffusion coefficient measurements of water excess or fluxed packed nanoparticles suspensions are describers of transport properties of soft biomaterials. The paper reports an NMR approach that can be seen as a general and relevant method to characterize excess-water-swollen soft biomaterials.

  8. Human serum albumin binding to silica nanoparticles--effect of protein fatty acid ligand.

    Science.gov (United States)

    Ang, Joo Chuan; Henderson, Mark J; Campbell, Richard A; Lin, Jhih-Min; Yaron, Peter N; Nelson, Andrew; Faunce, Thomas; White, John W

    2014-06-07

    Neutron reflectivity shows that fatted (F-HSA) and defatted (DF-HSA) versions of human serum albumin behave differently in their interaction with silica nanoparticles premixed in buffer solutions although these proteins have close to the same surface excess when the silica is absent. In both cases a silica containing film is quickly established at the air-water interface. This film is stable for F-HSA at all relative protein-silica concentrations measured. This behaviour has been verified for two small silica nanoparticle radii (42 Å and 48 Å). Contrast variation and co-refinement have been used to find the film composition for the F-HSA-silica system. The film structure changes with protein concentration only for the DF-HSA-silica system. The different behaviour of the two proteins is interpreted as a combination of three factors: increased structural stability of F-HSA induced by the fatty acid ligand, differences in the electrostatic interactions, and the higher propensity of defatted albumin to self-aggregate. The interfacial structures of the proteins alone in buffer are also reported and discussed.

  9. Uncorrected and Albumin-Corrected Calcium, Phosphorus, and Mortality in Patients Undergoing Maintenance Dialysis.

    Science.gov (United States)

    Rivara, Matthew B; Ravel, Vanessa; Kalantar-Zadeh, Kamyar; Streja, Elani; Lau, Wei Ling; Nissenson, Allen R; Kestenbaum, Bryan; de Boer, Ian H; Himmelfarb, Jonathan; Mehrotra, Rajnish

    2015-07-01

    Uncorrected serum calcium concentration is the first mineral metabolism metric planned for use as a quality measure in the United States ESRD population. Few studies in patients undergoing either peritoneal dialysis (PD) or hemodialysis (HD) have assessed the association of uncorrected serum calcium concentration with clinical outcomes. We obtained data from 129,076 patients on dialysis (PD, 10,066; HD, 119,010) treated in DaVita, Inc. facilities between July 1, 2001, and June 30, 2006. After adjustment for potential confounders, uncorrected serum calcium excess mortality in patients on PD or HD (comparison group uncorrected calcium 9.0 to albumin concentration substantially attenuated the all-cause mortality hazard ratios (HRs) associated with uncorrected calcium Albumin-corrected calcium ≥10.2 mg/dl and serum phosphorus ≥6.4 mg/dl were also associated with increased risk for death, irrespective of dialysis modality. In summary, in a large nationally representative cohort of patients on dialysis, abnormalities in markers of mineral metabolism, particularly high concentrations of serum calcium and phosphorus, were associated with increased mortality risk. Additional studies are needed to investigate whether control of hypercalcemia and hyperphosphatemia in patients undergoing dialysis results in improved clinical outcomes.

  10. New horizon in dialysis depuration: Characterization of a polysulfone membrane able to break the 'albumin wall'.

    Science.gov (United States)

    Cuoghi, A; Caiazzo, M; Monari, E; Bellei, E; Bergamini, S; Sereni, L; Aucella, F; Loschiavo, C; Atti, M; Tomasi, A

    2015-05-01

    The uremic syndrome is attributed to the progressive retention of a large number of toxins, which under normal conditions are excreted by the healthy kidneys. Standard dialytic membranes do not purify middle-high molecular weight toxins. Haemodiafiltration with endogenous reinfusion coupled with a highly permeable membrane could break the limit of the 'albumin wall' improving the dialytic depuration without loss of important nutrients. The aim of this study was to evaluate the performance of a new polysulfone membrane, Synclear 0.2, to remove uremic molecules. Surface Enhanced Laser Desorption Ionization-Time of Flight was employed to evaluate the proteomic profile of ultrafiltrate and Electrospray Ionization-Quadruple-ToF coupled with on-chip elution was used for proteins identification. A high and specific permeability for middle-high molecular weight molecules was revealed by mass spectrometry for the investigated membrane. The identified proteins are mostly uremic toxins: their relative abundance, estimated in the ultrafiltrate by exponentially modified protein abundance index, showed a high purification efficiency of the new membrane when compared with conventional ones. In conclusion, Synclear 0.2, used as convective membrane in hemodiafiltration with endogenous reinfusion treatment, permits to break the 'albumin wall', clearing middle-high molecular weight uremic toxins, improving the dialytic treatment purification efficiency.

  11. Spectroscopic and molecular modelling studies of binding mechanism of metformin with bovine serum albumin

    Science.gov (United States)

    Sharma, Deepti; Ojha, Himanshu; Pathak, Mallika; Singh, Bhawna; Sharma, Navneet; Singh, Anju; Kakkar, Rita; Sharma, Rakesh K.

    2016-08-01

    Metformin is a biguanide class of drug used for the treatment of diabetes mellitus. It is well known that serum protein-ligand binding interaction significantly influence the biodistribution of a drug. Current study was performed to characterize the binding mechanism of metformin with serum albumin. The binding interaction of the metformin with bovine serum albumin (BSA) was examined using UV-Vis absorption spectroscopy, fluorescence, circular dichroism, density functional theory and molecular docking studies. Absorption spectra and fluorescence emission spectra pointed out the weak binding of metformin with BSA as was apparent from the slight change in absorbance and fluorescence intensity of BSA in presence of metformin. Circular dichroism study implied the significant change in the conformation of BSA upon binding with metformin. Density functional theory calculations showed that metformin has non-planar geometry and has two energy states. The docking studies evidently signified that metformin could bind significantly to the three binding sites in BSA via hydrophobic, hydrogen bonding and electrostatic interactions. The data suggested the existence of non-covalent specific binding interaction in the complexation of metformin with BSA. The present study will certainly contribute to the development of metformin as a therapeutic molecule.

  12. Binding of ring-substituted indole-3-acetic acids to human serum albumin.

    Science.gov (United States)

    Soskić, Milan; Magnus, Volker

    2007-07-01

    The plant hormone, indole-3-acetic acid (IAA), and its ring-substituted derivatives have recently attracted attention as promising pro-drugs in cancer therapy. Here we present relative binding constants to human serum albumin for IAA and 34 of its derivatives, as obtained using the immobilized protein bound to a support suitable for high-performance liquid chromatography. We also report their octanol-water partition coefficients (logK(ow)) computed from retention data on a C(18) coated silica gel column. A four-parameter QSPR (quantitative structure-property relationships) model, based on physico-chemical properties, is put forward, which accounts for more than 96% of the variations in the binding affinities of these compounds. The model confirms the importance of lipophilicity as a global parameter governing interaction with serum albumin, but also assigns significant roles to parameters specifically related to the molecular topology of ring-substituted IAAs. Bulky substituents at ring-position 6 increase affinity, those at position 2 obstruct binding, while no steric effects were noted at other ring-positions. Electron-withdrawing substituents at position 5 enhance binding, but have no obvious effect at other ring positions.

  13. Analysis of binding ability of two tetramethylpyridylporphyrins to albumin and its complex with bilirubin

    Science.gov (United States)

    Solomonov, Alexey V.; Shipitsyna, Maria K.; Vashurin, Arthur S.; Rumyantsev, Evgeniy V.; Timin, Alexander S.; Ivanov, Sergey P.

    2016-11-01

    An interaction between 5,10,15,20-tetrakis-(N-methyl-x-pyridyl)porphyrins, x = 2; 4 (TMPyPs) with bovine serum albumin (BSA) and its bilirubin (BR) complex was investigated by UV-Viz and fluorescence spectroscopy under imitated physiological conditions involving molecular docking studies. The parameters of forming intermolecular complexes (binding constants, quenching rate constants, quenching sphere radius etc.) were determined. It was showed that the interaction between proteins and TMPyPs occurs via static quenching of protein fluorescence and has predominantly hydrophobic and electrostatic character. It was revealed that obtained complexes are relatively stable, but in the case of TMPyP4 binding with proteins occurs better than TMPyP2. Nevertheless, both TMPyPs have better binding ability with free protein compared to BRBSA at the same time. The influence of TMPyPs on the conformational changes in protein molecules was studied using synchronous fluorescence spectroscopy. It was found that there is no competition of BR with TMPyPs for binging sites on protein molecule and BR displacement does not occur. Molecular docking calculations have showed that TMPyPs can bind with albumin via tryptophan residue in the hydrophilic binding site of protein molecule but it is not one possible interaction way.

  14. Photo-isomerization and oxidation of bilirubin in mammals is dependent on albumin binding.

    Science.gov (United States)

    Goncharova, Iryna; Jašprová, Jana; Vítek, Libor; Urbanová, Marie

    2015-12-01

    The bilirubin (BR) photo-conversion in the human body is a protein-dependent process; an effective photo-isomerization of the potentially neurotoxic Z,Z-BR as well as its oxidation to biliverdin in the antioxidant redox cycle is possible only when BR is bound on serum albumin. We present a novel analytical concept in the study of linear tetrapyrroles metabolic processes based on an in-depth mapping of binding sites in the structure of human serum albumin (HSA). A combination of fluorescence spectroscopy, circular dichroism (CD) spectroscopy, and molecular modeling methods was used for recognition of the binding site for BR, its derivatives (mesobilirubin and bilirubin ditaurate), and the products of the photo-isomerization and oxidation (lumirubin, biliverdin, and xanthobilirubic acid) on HSA. The CD spectra and fluorescent quenching of the Trp-HSA were used to calculate the binding constants. The results of the CD displacement experiments performed with hemin were interpreted together with the findings of molecular docking performed on the pigment-HSA complexes. We estimated that Z,Z-BR and its metabolic products bind on two independent binding sites. Our findings support the existence of a reversible antioxidant redox cycle for BR and explain an additional pathway of the photo-isomerization process (increase of HSA binding capacity; the excess free [unbound] BR can be converted and also bound to HSA).

  15. EVALUATION OF ISCHEMIA MODIFIED ALBUMIN AND NITRIC OXIDE LEVELS AND THEIR INTER - RELATIONSHIP IN HYPERTHYROIDISM

    Directory of Open Access Journals (Sweden)

    Rangaswamy

    2014-02-01

    Full Text Available BACKGROUND: Ischemia Modified Albumin (IMA is an ischemia/reperfusion injury marker which has been considered to be formed under oxidative stress conditions. Endothelial L - Arginine/NO pathway dysfunction can lead to oxidative stress which has deleterious effects seen on the vascular wall causing ischemia. AIM: 1 The study was conducted to estimate the levels of IMA and NO in hyperthyroidism patients. 2 To evaluate the relationship bet ween IMA and NO levels in hyperthyroidism. MATERIALS AND METHODS: A cross sectional study was done with 30 newly diagnosed hyperthyroid patients as cases and 30 age and sex matched healthy controls. Serum levels of IMA and NO were estimated by colorimetric methods and thyroid profile was done by ELIFA methodology. STATISTICAL ANALYSIS: Data were analyzed using SPSS. Values were expressed as Mean±SD. RESULTS: Nitric Oxide levels were significantly decreased in hyperthyroid patients (7.08±1.57μmol/L as compa red to healthy controls (39.76±4.98μmol/L (p=0.001. Ischemia Modified Albumin levels were found to be significantly increased in hyperthyroid patients (0.73±0.10 ODU when compared to healthy controls (0.28±0.01 ODU (p=0.001. CONCLUSION: In our study t here was increase in IMA levels with decreased NO levels which could be due to the consequence of oxidative stress and ischemia which is present in hyperthyroidism

  16. 1HNMR study of methotrexate serum albumin (MTX SA) binding in rheumatoid arthritis

    Science.gov (United States)

    Sułkowska, A.; Maciążek-Jurczyk, M.; Bojko, B.; Równicka, J.; Sułkowski, W. W.

    2008-11-01

    Rheumatoid arthritis (RA) is an immunologically depended disease. It is characterized by a chronic, progressive inflammatory process. Methotrexate (4-amino-10-methylfolic acid, MTX) is the modifying drug used to treat RA. The aim of the presented studies is to determine the low affinity binding site of MTX in bovine (BSA) and human (HSA) serum albumin with the use of proton nuclear magnetic resonance ( 1HNMR) spectroscopy. The analysis of 1HNMR spectra of MTX in the presence of serum albumin (SA) allows us to observe the interactions between aromatic rings of the drug and the rings of amino acids located in the hydrophobic subdomains of the protein. On the basis of the chemical shifts σ [ppm] and the relaxation times T1 [s] of drug protons the hydrophobic interaction between MTX-SA and the stoichiometric molar ratio of the complex was evaluated. This work is a part of a spectroscopic study on MTX-SA interactions [A. Sułkowska, M. Maciążek, J. Równicka, B. Bojko, D. Pentak, W.W. Sułkowski, J. Mol. Struct. 834-836 (2007) 162-169].

  17. Adsorption characteristics of bovine serum albumin onto alumina with a specific crystalline structure.

    Science.gov (United States)

    Kawashita, Masakazu; Hayashi, Junpei; Li, Zhixia; Miyazaki, Toshiki; Hashimoto, Masami; Hihara, Hiroki; Kanetaka, Hiroyasu

    2014-02-01

    Bone cement containing alumina particles with a specific crystalline structure exhibits the ability to bond with bone. These particles (AL-P) are mainly composed of delta-type alumina (δ-Al2O3). It is likely that some of the proteins present in the body environment are adsorbed onto the cement and influence the expression of its bioactivity. However, the effect that this adsorption of proteins has on the bone-bonding mechanism of bone cement has not yet been elucidated. In this study, we investigated the characteristics of the adsorption of bovine serum albumin (BSA) onto AL-P and compared them with those of its adsorption onto hydroxyapatite (HA), which also exhibits bone-bonding ability, as well as with those of adsorption onto alpha-type alumina (α-Al2O3), which does not bond with bone. The adsorption characteristics of BSA onto AL-P were very different from those onto α-Al2O3 but quite similar to those onto HA. It is speculated that BSA is adsorbed onto AL-P and HA by interionic interactions, while it is adsorbed onto α-Al2O3 by electrostatic attraction. The results suggest that the specific adsorption of albumin onto implant materials might play a role in the expression of the bone-bonding abilities of the materials.

  18. Mechanistic Studies on the Photoallergy Mediated by Fenofibric Acid: Photoreactivity with Serum Albumins.

    Science.gov (United States)

    Vayá, Ignacio; Andreu, Inmaculada; Monje, Vicente T; Jiménez, M Consuelo; Miranda, Miguel A

    2016-01-19

    The photoreactivity of fenofibric acid (FA) in the presence of human and bovine serum albumins (HSA and BSA, respectively) has been investigated by steady-state irradiation, fluorescence, and laser flash photolysis (LFP). Spectroscopic measurements allowed for the determination of a 1:1 stoichiometry for the FA/SA complexes and pointed to a moderate binding of FA to the proteins; by contrast, the FA photoproducts were complexed more efficiently with SAs. Covalent photobinding to the protein, which is directly related to the photoallergic properties of the drug, was detected after long irradiation times and was found to be significantly higher in the case of BSA. Intermolecular FA-amino acid and FA-albumin irradiations resulted in the formation of photoproducts arising from coupling between both moieties, as indicated by mass spectrometric analysis. Mechanistic studies using model drug-amino acid linked systems indicated that the key photochemical step involved in photoallergy is formal hydrogen atom transfer from an amino acid residue to the excited benzophenone chromophore of FA or (more likely) its photoproducts. This results in the formation of caged radical pairs followed by C-C coupling to give covalent photoaducts.

  19. Liver repair and hemorrhage control using laser soldering of liquid albumin in a porcine model

    Science.gov (United States)

    Wadia, Yasmin; Xie, Hua; Kajitani, Michio; Gregory, Kenton W.; Prahl, Scott A.

    2000-05-01

    The purpose of this study was to evaluate laser soldering using liquid albumin for welding liver lacerations and sealing raw surfaces created by segmental resection of a lobe. Major liver trauma has a high mortality due to immediate exsanguination and a delayed morbidity and mortality from septicemia, peritonitis, biliary fistulae and delayed secondary hemorrhage. Eight laceration injuries (6 cm long X 2 cm deep) and eight non-anatomical resection injuries (raw surface 6 cm X 2 cm) were repaired. An 805 nm laser was used to weld 53% liquid albumin-ICG solder to the liver surface, reinforcing it with a free autologous omental scaffold. The animals were heparinized to simulate coagulation failure and hepatic inflow occlusion was used for vascular control. For both laceration and resection injuries, eight soldering repairs each were evaluated at three hours. A single suture repair of each type was evaluated at three hours. All 16 laser mediated liver repairs were accompanied by minimal blood loss as compared to the suture controls. No dehiscence, hemorrhage or bile leakage was seen in any of the laser repairs after three hours. In conclusion laser fusion repair of the liver is a quick and reliable technique to gain hemostasis on the cut surface as well as weld lacerations.

  20. Effects of fluorinated and hydrogenated surfactants on human serum albumin at different pHs.

    Science.gov (United States)

    Sabín, Juan; Prieto, Gerardo; González-Pérez, Alfredo; Ruso, Juan M; Sarmiento, Félix

    2006-01-01

    Complexation between human serum albumin (HSA) and two different surfactants, one fully fluorinated (sodium perfluorooctanoate, SPFO) and one fully hydrogenated (sodium caprylate, SO), was studied using zeta-potential measurements and difference spectroscopy. The study was carried out at three different pHs, 3.2, 6.7, and 10.0. The spectroscopy study was performed at pHs 6.7 and 10.0, given that at pH 3.2 high turbidity was observed in the wide range of surfactant concentrations. The results were interpreted in terms of the electrostatic and hydrophobic contributions to the stability of the different phases formed in the water-surfactant-HSA system. Solutions and precipitates were observed in the concentration range investigated in more detail. Using Pace methods, the thermodynamic values of the surfactant-induced conformational changes in HSA were determined for sodium perfluorooctanoate in the concentration range 2-12 mmol dm(-3) at pH 6.7 and 5-22 mmol dm(-3) at pH 10.0. Electrophoretic measurements were used to characterize surfactant adsorption by determining the number of molecules adsorbed on the surface of HSA and the Gibbs energy of adsorption. Finally, the interactions between human serum albumin and other anionic surfactants studied by other authors were compared with those observed in the present work.