PMID: 6111348Feb 13, 1981Paper

Purification and properties of gamma-glutamyl transferase from normal rat liver

Biochimica Et Biophysica Acta
J L DingT J Peters

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.

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Citations

Jan 1, 1987·The International Journal of Biochemistry·S J Sulakhe, W W Lautt
Jan 1, 1985·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·B P Glynn, D B Johnson
Nov 1, 1990·Neurotoxicology and Teratology·F J RomeroJ Romá
Aug 1, 1989·The Journal of Clinical Investigation·R P ElferinkP L Jansen
Sep 28, 1984·Biochemical and Biophysical Research Communications·F J Romero, H Sies
May 1, 1990·Hepatology : Official Journal of the American Association for the Study of Liver Diseases·H SpeiskyY Israel
Jun 1, 1985·Pediatric Annals·J R Poley
Jun 7, 1982·FEBS Letters·J L DingT J Peters
Oct 13, 1981·Biochimica Et Biophysica Acta·J L DingT J Peters

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