Nicotinamide riboside–amino acid conjugates that are stable to purine nucleoside phosphorylase
نویسندگان
چکیده
منابع مشابه
Purine Nucleoside Phosphorylase
Purine nucleoside phosphorylase (EC 2.4.2.1) from bovine spleen is a trimeric enzyme that readily dissociates to the monomer. Dilution of enzyme from 20 to 0.02 pg of protein/ml is accompanied by a greater than 50-fold increase in the specific activity (utrimer = 0.23 nmol/min/pg; umonomer = 12.5 nmol/min/pg). Gel permeation chromatography in the presence of the substrate phosphate shows the en...
متن کاملRabbit Erythrocyte Purine Nucleoside Phosphorylase
1. Concave-downward double-reciprocal plots were obtained for rabbit erythrocyte purine nucleoside phosphorylase when the concentration of Pi was varied over a wide range at a fixed saturating concentration of either inosine or deoxyinosine. Similar behaviour was also displayed by the calf spleen enzyme. 2. The degree of curvature of double-reciprocal plots was greatly modified by the presence ...
متن کاملPurine Nucleoside Phosphorylase of Rabbit Liver
Initial velocity studies and product inhibition patterns for purine nucleoside phosphorylase from rabbit liver were examined in order to determine the predominant catalytic mechanism for the synthetic (forward) and phosphorolytic (reverse) reactions of the enzyme. Initial velocity studies in the absence of products gave intersecting or converging linear double reciprocal plots of the kinetic da...
متن کاملPurine nucleoside phosphorylase from human erythrocytes.
Purine nucleoside phosphorylase has been purified about 7,300-fold and crystallized from human erythrocytes (mol wt 81,000). The recrystallized enzyme exists in the form of needles and sometimes bundles of needles and has a specific activity of 96 pM units per mg of protein. A number of phenomena reported earlier for a less pure preparation of this enzyme are still seen with the crystalline enz...
متن کاملMonomeric Purine Nucleoside Phosphorylase from Rabbit Liver
Rabbit liver purine nucleoside phosphorylase (purine nucleoside: orthophosphate ribosyltransferase EC 2.4.2.1.) was purified to homogeneity by column chromatography and ammonium sulfate fractionation. Homogeneity was established by disc gel electroihoresis in presence and absence of sodium dodecyl sulfate, and isoelectric focusing. Molecular weights of 46,000 and 39,000 were determined, respect...
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ژورنال
عنوان ژورنال: Organic & Biomolecular Chemistry
سال: 2020
ISSN: 1477-0520,1477-0539
DOI: 10.1039/d0ob00134a