Partial purification and some properties of gamma-glutamyl transpeptidase from human bile.
1. Gamma-Glutamyl transpepetidase ((5-glutamyl)-peptide: amino acid 5-glutamyltransferase, EC 2.3.2.2) from human bile has been partially purified using protamine sulphate treatment, DEAE-cellulose chromatography and Sephadex G-200 filtration. The procedure resulted in 150-fold increase in specific acitivity with a 37% yield. 2. The partially purified enzyme showed a single zone of enzyme activity by polyacrylamide gel electrophoresis and eluted in the inner volume of Sephadex G-200. 3. The enzyme had a pH optimum of 8.1 and Km of 1.52 mM using gamma-glutamyl p-nitroanilide as substrate. 4. The effects of cations and different gamma-glutamyl acceptors on the activity of the enzyme are reported. 5. As bile gamma-glutamyl transpeptidase appears to be soluble in the absence of detergents, it is suggested that bile may prove to be a useful source for further studies of the kinetic properties and physiological role of human gamma-glutamyl transpeptidase.
D000596:Amino Acids / Q000378:metabolism; D000813:Anilides / Q000378:metabolism; D001646:Bile / Q000201:enzymology*; D002413:Cations, Divalent / Q000494:pharmacology; D002414:Cations, Monovalent / Q000494:pharmacology; D004151:Dipeptides / Q000378:metabolism; D005971:Glutamates / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011479:Protamines; D005723:gamma-Glutamyltransferase / Q000302:isolation & purification / Q000378:metabolism*
D000596:Amino Acids; D000813:Anilides; D002413:Cations, Divalent; D002414:Cations, Monovalent; D004151:Dipeptides; D005971:Glutamates; D011479:Protamines; D005723:gamma-Glutamyltransferase