On the existence of variant forms of gamma-glutamyl transferase in regenerating and neoplastic liver.
We attempted to identify variants of gamma-glutamyl transferase (GGT) which may differ in their affinity for Concanavalin A (Con A) in extracts of fetal, regenerating, neoplastic and normal adult rat liver. GGT activity was low in normal liver and did not increase after partial hepatectomy. Feeding a choline-deficient diet containing 0.05% ethionine caused a large increase in hepatic GGT activity which persisted throughout the feeding period of 23 weeks. Practically all of the GGT contained in extracts prepared with Triton X-100 from fetal, regenerating, pre-neoplastic and neoplastic rat liver as well as that from normal adult liver bound to Con A-Sepharose and was eluted from the columns with methyl-alpha-D-mannopyranoside. In contrast, GGT from bovine kidney extracts prepared in an identical way did not bind  to Con A-Sepharose. We conclude that if variants of rat liver GGT exist, they cannot be reliable separated by simple affinity chromatography on Con A-Sepharose of Agarose columns.
D000818:Animals; D002796:Choline Deficiency / Q000201:enzymology; D002846:Chromatography, Affinity; D003208:Concanavalin A; D005260:Female; D005333:Fetus; D007527:Isoenzymes / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D008113:Liver Neoplasms / Q000201:enzymology*; D008115:Liver Regeneration; D008297:Male; D009374:Neoplasms, Experimental / Q000201:enzymology; D011247:Pregnancy; D051381:Rats; D011919:Rats, Inbred Strains; D005723:gamma-Glutamyltransferase / Q000302:isolation & purification / Q000378:metabolism*
D007527:Isoenzymes; D003208:Concanavalin A; D005723:gamma-Glutamyltransferase