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Purification of liver gamma-glutamyltranspeptidase from the rat
Abstract:
Gamma-glutamyltranspeptidase (GGT) of adult rat liver was solubilized by treatment with papain and further purified by affinity column chromatography on concanavalin-A Sepharose 4B, followed by ion exchange chromatography on DEAE-cellulose. During DEAE-cellulose chromatography, liver GGT was adsorbed at 0.1M Tris-HCl buffer (pH8.0). The Km value of the liver GGT for L-gamma-glutamyl p-nitroanilide was 1.35mM.