Phosphorolytic and transferase activities of the purine nucleoside phosphorylase from human erythrocytes

Abstract
Purine nucleoside phosphorylase obtained from human erythrocytes was purified 600 to 800 fold by acid precipitation and filtration through p-cellulose and DEAE- cellulose columns.
The enzyme was found to contain both phosphorylase and transferase activities and the ratio of the two activities remaind constant throughout the purification pro cedure. Apparently different molecular aggregates were obtained by sucrose gradient centrifugation. No interconversion of the two activities was found.
Keywords:
Carbon Isotopes, Centrifugation, Chemical Precipitation, Chromatography, DEAE-Cellulose, Density Gradient, Erythrocytes/enzymology, Humans, Hydrogen-Ion Concentration, Molecular Weight, N-Glycosyl Hydrolases/blood/isolation and purification, Paper, Sucrose, Transferases/blood/isolation and purification, Xanthine Oxidase/metabolism, Xanthines/metabolism
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