General physiology and biophysics, 15(5), 403-413 (1996-10-01)
The initial rate kinetics of rat kidney gamma-glutamyl transpeptidase were measured using L-gamma-glutamyl-p-nitroanilide and glycyl-glycine as the donor and the acceptor substrate, respectively. Experimental data were fitted with the initial rate equation, and the obtained results indicated that: (1) Michaelis
The Biochemical journal, 304 ( Pt 3), 869-876 (1994-12-15)
Acyl-transfer catalysed by gamma-glutamyltranspeptidase from bovine kidney was studied using gamma-L- and gamma-D-Glu-p-nitroanilide as the donor and GlyGly as the acceptor. The transfer of the gamma-Glu group to GlyGly was shown to be accompanied by transfer of the gamma-Glu group
Bioscience, biotechnology, and biochemistry, 61(10), 1621-1625 (1997-11-15)
Two isozymes of gamma-glutamyltranspeptidase, GGT-A and GGT-B, were purified to electrophoretic homogeneity from a culture broth of Bacillus subtilis TAM-4, which produces poly(gamma-glutamic acid) (PGA) de novo. GGT-A was composed of three subunits with molecular weights of 23,000 (I), 39,000
Clinica chimica acta; international journal of clinical chemistry, 175(2), 129-134 (1988-07-15)
In this paper we compare the measurement of catalytic activity concentrations of gamma-glutamyltransferase with the non-carboxylated and the carboxylated substrate in preparations of different origin. Fresh human sera, commercial test sera and preparations of gamma-glutamyltransferase purified from human liver, porcine
The effect of thyroid hormone administration on liver glutathione (GSH) content and gamma-glutamyltransferase activity in the isolated perfused liver was studied for a period of 1-7 days in fed rats following a single dose of 0.1 mg 3,5,3'-L-triiodothyronine (T3)/kg. T3