Purification and properties of purine nucleoside phosphorylases from bird liver

J.C. Manzanero
M. Mora
J. Bozal
64

Abstract

Chicken and pigeon liver PNPases differ in their isoelectric points (5.40 and 5.15), in their molecular weights (125,000 +/- 5,000; 78,000 +/- 5,000, determined on Sephadex G-200) and in their subunit molecular weight (62,000 +/- 10%; 75,000 +/- 10%, determined by sodium dodecil sulfate-polyacrylamide gel electrophoresis).The related molecular weights show a dimeric structure for the chicken liver enzyme and a monomeric structure for the pigeon liver enzyme.Activation energies are similar but differ in delta H values.Both PNPases are irreversibly inactivated by p-chloromercuribenzoate and 5,5'-dithiobis-(2-nitrobenzoic acid) when incubated with these reagents; inactivation can be reverted totally or partially by dithiothreitol and 2-mercaptoethanol.

Keywords:
Animals, Chickens/metabolism, Columbidae/metabolism, Isoelectric Point, Kinetics, Liver/enzymology, Molecular Weight, Pentosyltransferases/isolation and purification, Purine-Nucleoside Phosphorylase/antagonists and inhibitors/isolation and purification, Species Specificity, Sulfhydryl Reagents/pharmacology

Authors

J.C. Manzanero
M. Mora
J. Bozal


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