[Detection of multiple molecular forms of the gamma-glutamyltransferase by concanavalin A affinity chromatography (author's transl)].
The separation of several forms of gamma-glutamyl-transferase was achieved by using concanavalin A-Sepharose columns. The enzyme of the adult liver was bound totally to the lectin, whereas only 5% of the kidney enzyme and 50% of the pancreas gamma-glutamyltransferase was adsorbed by concanavalin A. Due to a higher content of N-acetylneuraminic acid, the enzyme of the fetal liver does not show any affinity to concanavalin A. Within 8 days after birth the N-acetylneuraminic acid-rich fetal gamma-glutamyltransferase is substituted by the adult form.
D000818:Animals; D002417:Cattle; D002846:Chromatography, Affinity; D003208:Concanavalin A; D004285:Dogs; D006801:Humans; D007668:Kidney / Q000201:enzymology; D008099:Liver / Q000201:enzymology; D010179:Pancreas / Q000201:enzymology; D011817:Rabbits; D013552:Swine; D005723:gamma-Glutamyltransferase / Q000302:isolation & purification*
D003208:Concanavalin A; D005723:gamma-Glutamyltransferase
Nachweis mol-kularer Varianten der gamma-Glutamyltransferase mit differenter Concanavalin-A-Affinität