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Selvaraj, P. et al.

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.

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.[1]

References

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. Selvaraj, P., Balasubramanian, K.A., Hill, P.G. Enzyme (1981) [Pubmed]

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