title: Purification and properties of gamma-glutamyl transferase from normal rat liver.
abstract: gamma-Glutamyl transferase ((5-glutamyl)-peptide: amino-acid 5-glutamyltransferase, ED 2.3.2.2) has been partially purified from both whole rat liver (600-fold) and from isolated biliary tract (1200-fold). The most highly purified fraction gave two protein bands on polyacrylamide gel electrophoresis, the major band alone having enzyme activity. The enzyme purified from biliary tract appears identical to that from whole liver preparation according to molecular weight, kinetic parameters and the effects of various inhibitors. Three liver cell-types; parenchymal, Kupffer and biliary tract were isolated by perfusion of the rat liver in situ with collagenase, followed by selective cell isolation. Approx. 80-90% of the total recovered enzyme activity was found in the biliary tract. Nearly 50% of the apparent enzyme activity in the parenchymal cell was attributable to a nonspecific hydrolase.
mesh_terms: D000818:Animals; D001659:Biliary Tract / Q000201:enzymology; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008274:Magnesium / Q000494:pharmacology; D008297:Male; D009928:Organ Specificity; D051381:Rats; D015032:Zinc / Q000494:pharmacology; D005723:gamma-Glutamyltransferase / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D005723:gamma-Glutamyltransferase; D008274:Magnesium; D015032:Zinc