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

Enzyme
P SelvarajP G Hill

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.

Citations

Jun 1, 1992·International Journal of Developmental Neuroscience : the Official Journal of the International Society for Developmental Neuroscience·B JankáskováF Stastný
Jan 1, 1984·International Journal of Developmental Neuroscience : the Official Journal of the International Society for Developmental Neuroscience·M Pajari
Jun 3, 1982·Clinica Chimica Acta; International Journal of Clinical Chemistry·P Selvaraj, K A Balasubramanian

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