Purification and characterization of purine nucleoside phosphorylase from Proteus vulgaris
نویسندگان
چکیده
منابع مشابه
Purification and properties of purine nucleoside phosphorylase from Salmonella typhimurium.
Purine nucleoside phosphorylase (inosine + Pi ti hypoxanthine + a-D-ribose l-phosphate, EC 2.4.2.1) from Salmonella typhimurium LT-2 has been purified 230-fold. High speed sedimentation equilibrium studies showed that the molecular weight of the native enzyme was 141,000. A molecular weight of 130,000 i 10% was determined by Sephadex G-150 filtration. Disc gel electrophoresis of the enzyme in t...
متن کاملPurine 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 کاملPurification and characterization of human erythrocyte purine nucleoside phosphorylase and its subunits.
Purine nucleoside phosphorylase (EC 2.4.2.1; purine nucleoside:orthophosphate ribosyltransferase) from fresh human erythrocytes has been purified to homogeneity in two steps with an overall yield of 56%. The purification involves DEAE-Sephadex chromatography followed by affinity chromatography on a column of Sepharose/formycin B. This scheme is suitable for purification of the phosphorylase fro...
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: Applied and Environmental Microbiology
سال: 1990
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.56.5.1435-1439.1990