Isolation and properties of gamma-glutamyltranspeptidase from Morris hepatoma 5123D.
gamma-Glutamyltranspeptidase was purified 600-fold from Morris hepatoma 5123D by six-step procedure. Its apparent molecular weight estimated by centrifugation in sucrose gradient with Triton X-100 amounts to 108 000. Some dipeptides particularly glycylglycine and several amino acids considerably increase the enzyme activity but L-serine with borate decreases it. Usually transfer activity of the enzyme towards gamma-L-glutamyl substrates was much higher than hydrolytic. The best substrate for the hepatoma enzyme is reduced glutathione.
D000818:Animals; D001881:Borates / Q000494:pharmacology; D006528:Carcinoma, Hepatocellular / Q000201:enzymology*; D004789:Enzyme Activation / Q000187:drug effects; D005978:Glutathione; D006033:Glycylglycine / Q000494:pharmacology; D008113:Liver Neoplasms / Q000201:enzymology*; D008970:Molecular Weight; D009374:Neoplasms, Experimental / Q000201:enzymology; D051381:Rats; D012694:Serine / Q000494:pharmacology; D013379:Substrate Specificity; D005723:gamma-Glutamyltransferase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*
D001881:Borates; D006033:Glycylglycine; D012694:Serine; D005723:gamma-Glutamyltransferase; D005978:Glutathione