Comparative studies on nucleoside diphosphatase of rat ascites hepatoma and rat liver: activity level, purification and properties.
1. The activities of nucleoside diphosphatase in various rat ascites cells of hepatoma, and fetal and neonatal rat liver were much lower than that of normal adult rat liver. 2. The enzyme was purified from ascites hepatoma (AH-66 cell lines) to an apparently homogeneous state and the enzymatic properties were studied in comparison with the enzyme from rat liver microsomes. 3. The hepatoma enzyme had less stability based on the results of heat-inactivation experiments. 4. However, the other properties of hepatoma enzyme; Km value, molecular weight, optimal pH, isoelectric point, substrate specificity and antigenicity, were similar to those of rat liver enzyme.
D017766:Acid Anhydride Hydrolases; D000818:Animals; D001202:Ascitic Fluid / Q000201:enzymology; D055598:Chemical Phenomena; D002621:Chemistry; D007120:Immunochemistry; D007700:Kinetics; D008114:Liver Neoplasms, Experimental / Q000201:enzymology*; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology*; D010744:Phosphoric Monoester Hydrolases / Q000302:isolation & purification*; D051381:Rats
D010744:Phosphoric Monoester Hydrolases; D017766:Acid Anhydride Hydrolases; C023837:nucleoside-diphosphatase