[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.