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Isolation of gamma-glutamyl transpeptidase from human primary hepatoma and comparison of its kinetic and catalytic properties with the enzyme from normal adult and fetal liver.

Abstract
gamma-Glutamyl transpeptidase (gamma-GT) from human primary hepatoma was solubilised and purified 290-fold with 25% recovery. The kinetic and catalytic properties were compared with those purified from human fetal and normal adult liver. Hepatoma gamma-GT did not differ from the fetal and adult liver gamma-GT in its pH optima for transpeptidation and auto-transfer reaction, heat stability, Km for the two substrates and inhibition by L-serine + borate. Enzyme from the three sources behaved in a similar manner towards various cations, sulphhydryl reagents, amino acid dipeptides. Adult liver enzyme showed a 4 time higher Ki value for anthglutin than hepatoma and fetal liver. The hepatoma gamma-GT could not be differentiated from that of adult and fetal liver by concanavalin-A Sepharose 4B column chromatography. The tissue concentration of gamma-GT was 3 to 13 times higher in hepatoma and fetal liver than in adult liver.
AuthorsP Selvaraj, K A Balasubramanian, P G Hill
JournalEnzyme (Enzyme) Vol. 26 Issue 2 Pg. 57-63 ( 1981) ISSN: 0013-9432 [Print] Switzerland
PMID6113139 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Glutamates
  • gamma-Glutamyltransferase
  • anthglutin
Topics
  • Adult
  • Aging
  • Carcinoma, Hepatocellular (enzymology)
  • Drug Stability
  • Female
  • Glutamates (pharmacology)
  • Humans
  • Kinetics
  • Liver (embryology, enzymology)
  • Liver Neoplasms (enzymology)
  • Pregnancy
  • gamma-Glutamyltransferase (isolation & purification, metabolism)

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