Clinical Chemistry, Vol 26, 1523-1527, Copyright © 1980 by American Association for Clinical Chemistry

Electrophoretic, kinetic, and immunoinhibition properties of gamma- glutamyltransferase from various tissues compared

LM Shaw, L Petersen-Archer, JW London and E Marsh

gamma-Glutamyltransferase (EC 2.3.2.2) from human liver, kidney, pancreas, and duodenum migrated in acrylamide gels (65 g/L) as a single band with the following decreasing order of electrophoretic mobility: liver > pancreas > kidney > duodenum. The initial velocity kinetic constants of pancreatic and duodenal gamma-glutamyltransferase and of the enzyme in human serum were determined and compared with those we previously established for the enzyme from human kidney, liver, and serum. The greatest differences were in the glycylglycine competitive- inhibition constants: kidney gamma-glutamyltransferase was the most strongly inhibited and pancreatic enzyme the second most strongly inhibited by high concentrations of glycylglycine, with the liver and duodenal isoenzymes only slightly inhibited and the enzyme in serum not inhibited over the concentration range (0-150 mmol/L) of glycylglycine used. Differences between the other kinetic constants of these isoenzymes were much smaller. Human liver gamma-glutamyltransferase was obtained in a highly purified form by a six-step procedure that included papain digestion of the original homogenate. Rabbit antisera raised against this preparation inhibited liver, kidney, and pancreatic gamma-glutamyltransferase activity equally well (78, 76, and 78% inhibition, respectively), but inhibited the hog-kidney enzyme only slightly (1%). We conclude that the polypeptide portions of the isoenzyme molecules are structurally similar but that the carbohydrate moieties differ significantly in structure and topography.