Strong aqueous ammonium hydroxide used to remove N-acyl protecting groups from synthetic oligoribonucleotides causes removal of some alkylsilyl protecting groups from 2'-hydroxyls and leads to chain...Full Text Available
Cathodic reduction of non-terminal vinylaxides on Hg cathodes in the presence of electrophiles gives reasonable yields of N-acylated enamines in an electrochemically totally irreversible reaction. In the presence of added H-donors rather high selectivity for formation of saturated amides is achieveable. The influence of reaction conditions on product distribution is discussed.
The first-step formation constants of UO_2"2"+-complexes of some N-hydroxysuccinamic acids viz. N-phenyl N-hydroxysuccinamic acid (Rsub(p)H(sub(2))), N-o-toyl N-hydroxysuccinamic acid(Rsub(t)oHsub(2)) and N-m-tolyl N-hydroxysuccinamic acid (Rsub(t)mHsub(2)) have been determined spectrophotometrically. Stabilities are in the ligand order Risup(m)Hsub(2)>Rsub(t)oHsub(2)>Rsub(p)Hsub(2). The first-step hydrolysis constant k' of UO_2"2"+ ion has been determined spectrophotometrically and found to be pk'=4.00 at a constant ionic strength (#mu#=0.5) at 30deg-+0.5deg and the molar extinction coefficients of the species UO_2"2"+ and UO_2(OH)"+ at #LAMBDA#=385 nm are found to be 2.0 and 13.0 respectively. (author).
Human senescence marker protein 30 (SMP30), which functions enzymatically as a lactonase, hydrolyzes various carbohydrate lactones. The penultimate step in vitamin-C biosynthesis is catalyzed by this enzyme in nonprimate mammals. It has also been implicated as an organophosphate hydrolase, with the ability to hydrolyze diisopropyl phosphofluoridate and other nerve agents. SMP30 was originally identified as an aging marker protein, whose expression decreased androgen independently in aging cells. SMP30 is also referred to as regucalcin and has been suggested to have functions in calcium homeostasis. The crystal structure of the human enzyme has been solved from X-ray diffraction data collected to a resolution of 1.4 {angstrom}. The protein has a 6-bladed {beta}-propeller fold, and it contains a single metal ion. Crystal structures have been solved with the metal site bound with either a Ca{sup 2+} or a Zn{sup 2+} atom. The catalytic role of the metal ion has been ...