Physiochemical and immunochemical characterization of gamma-glutamyl transpeptidase from yolk sak tumor and ascitic hepatoma (AH-66) cells.
gamma-Glutamyl transpeptidases, purified from rat yolk sac tumor and AH-66 hepatoma cell lines resemble this enzyme system from rat kidney in their amino acid composition and antigenicity, but differ by having a higher carbohydrate content. The different carbohydrate contents resulted in the tumor cell and rat kidney enzymes having different molecular weights. Isoelectric focusing of the neuraminidase-treated enzymes showed that a substantial portion of the enzymes from yolk sac tumor and AH-66 cells shifted to a form with an isoelectric point at pH 7.4. However, a heterogeneous pattern was still found in the kidney enzyme even after extensive neuraminidase treatment.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D002460:Cell Line; D005260:Female; D005779:Immunodiffusion; D007525:Isoelectric Focusing; D007668:Kidney / Q000201:enzymology; D008114:Liver Neoplasms, Experimental / Q000201:enzymology*; D008649:Mesonephroma / Q000201:enzymology*; D008970:Molecular Weight; D009439:Neuraminidase / Q000378:metabolism; D010051:Ovarian Neoplasms / Q000201:enzymology*; D051381:Rats; D005723:gamma-Glutamyltransferase / Q000302:isolation & purification*
D000596:Amino Acids; D002241:Carbohydrates; D005723:gamma-Glutamyltransferase; D009439:Neuraminidase