Comparison of 5'-nucleotidase activities of isolated plasma membranes of two ascites cell variants.
The glycogen-containing ascites cell line was found to have a 3-5 times higher 5'-nucleotidase specific activity than the glycogen-free variant, resulting in different substrate affinity constants of Km = 0.14 mM and Km = 0.69 mM respectively. These activity differences were due to true 5'-nucleotidase as shown by its inactivation through specific inhibitors such as concanavalin A and alpha, beta-methylene adenosine diphosphate. Substrate specificity of the enzyme was similar in both cell lines, but differences were observed with respect to the pH optimum and stability.
D015720:5'-Nucleotidase; D000469:Alkaline Phosphatase / Q000378:metabolism; D000818:Animals; D002286:Carcinoma, Ehrlich Tumor / Q000201:enzymology*; D002458:Cell Fractionation; D002462:Cell Membrane / Q000201:enzymology / Q000648:ultrastructure; D003208:Concanavalin A / Q000494:pharmacology; D006003:Glycogen / Q000378:metabolism; D007527:Isoenzymes / Q000378:metabolism*; D007700:Kinetics; D008297:Male; D051379:Mice; D008815:Mice, Inbred Strains; D009708:Nucleotidases / Q000378:metabolism*; D013379:Substrate Specificity; D013696:Temperature
D007527:Isoenzymes; D003208:Concanavalin A; D006003:Glycogen; D009708:Nucleotidases; D000469:Alkaline Phosphatase; D015720:5'-Nucleotidase