Specific adenosine phosphorylase from hepatopancreas of gastropod Helix pomatia.
1. Specific adenosine phosphorylase from Helix pomatia hepatopancreas was separated from inosine-guanosine phosphorylase and purified 100-165 times; molecular weights were found to be 71,000 and 90,000, respectively. 2. The enzyme is specific for deoxy- and adenosine; it is inactive for 5'-methylthioadenosine and 5-amino-4-imidazole-carboxyamide riboside. Its sensitivity to several inhibitors differs from that of eucaryotic and bacterial purine nucleoside phosphorylases, and is not identical with the sensitivity of the S. mansoni adenosine-splitting enzyme. 3. H. pomatia adenosine phosphorylase differs in its mol. wt and Km values for P(i), ribose 1P, Ado and Ade from adenosine phosphorylase of B. subtilis.
Trembacz
H
H
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw.
Jezewska
M M
MM
D000818:Animals; D004064:Digestive System / Q000201:enzymology; D006372:Helix, Snails / Q000201:enzymology*; D010271:Parasites / Q000201:enzymology; D011387:Prokaryotic Cells / Q000201:enzymology; D011683:Purine-Nucleoside Phosphorylase / Q000302:isolation & purification*; D013379:Substrate Specificity
C019603:adenosine phosphorylase; C028449:xanthosine phosphorylase; D011683:Purine-Nucleoside Phosphorylase