Liver purine nucleoside phosphorylase in Camelus dromedarius: purification and properties.
1. Purine nucleoside phosphorylase (purine nucleoside:orthophosphate ribosyl transferase, EC 2.4.2.1) was purified to electrophoretic homogeneity from the liver of Camelus dromedarius. 2. The enzyme appears to be a dimer with a 44,000 subunit mol. wt and displays non-linear kinetics with concave downward curvature in double reciprocal plots with respect to both inosine and orthophosphate as variable substrates. 3. The effect of thiol compounds on the enzyme activity and of pH on kinetic parameters is reported.
Osman
A M
AM
Department of Physiology and Biochemistry, University of Pisa, Italy.
Del Corso
A
A
Mohamed
A S
AS
Ipata
P L
PL
Mura
U
U
D000818:Animals; D002162:Camelus / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D011683:Purine-Nucleoside Phosphorylase / Q000302:isolation & purification / Q000378:metabolism*; D013438:Sulfhydryl Compounds / Q000494:pharmacology
D013438:Sulfhydryl Compounds; D011683:Purine-Nucleoside Phosphorylase