gamma-Glutamyltransferase from human hepatoma tissue in comparison with normal liver enzyme.
gamma-Glutamyltransferase was solubilized from human hepatoma tissues by bromelain treatment, and some of its properties were compared with those of the normal adult liver enzyme. An electrophoretic study showed a slightly different mobility between the two enzymes before and after neuraminidase treatment. The hepatoma tissue enzyme was distinguished from the normal liver enzyme by decreased affinity to Con A. However, the enzymes from the two sources were found to be very similar or identical with respect to molecular weight, Michaelis constant, pH optimum, thermostability, effect of various L-amino acids as acceptors, behavior to divalent cations or ethylenediaminetetraacetate, inhibition by urea or sodium dodecyl sulfate, and immunological properties. These results suggest that the hepatoma tissue gamma-glutamyltransferase is largely due to altered glycosylation of this glycoprotein in hepatoma cells.
D006528:Carcinoma, Hepatocellular / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D005779:Immunodiffusion; D007668:Kidney / Q000032:analysis; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008113:Liver Neoplasms / Q000201:enzymology*; D008970:Molecular Weight; D009363:Neoplasm Proteins / Q000032:analysis; D005723:gamma-Glutamyltransferase / Q000032:analysis*
D009363:Neoplasm Proteins; D005723:gamma-Glutamyltransferase