グルタチオンを基質にした血清γ-グルタミルトランスフェラーゼ活性のアンペロメトリー

概要

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The magnitude of the steady-state current by a sulfhydryl compound at a dialysis membrane(molecular cut off: 5000) coverd cobalt phthalocyanine-embedded electrode was inversly proportional to the molecular weight. That is, the currents by 1μM glutathione(GSH), glutamylcysteine and cysteine at 200 mM and at pH 8.3 were 0.07, 0.14 and 0.39 nA, respectively. The activity of γ-glutamyltransferase (γ-GT) in serum was determined by measuring the current increase for a given time due to the degradation of GSH to cysteinylglysine in a 0.1 M tris buffer of pH 8.3 containing 1.2 mM GSH, 50 mM glysylglysine and 5 mM EDTA. The activities of γ-GT determined amperometrically using GSH as a substrate for sixteen serum samples were in good agreement with those determined by a colorimetric method using γ-glutamyl-3-carboxy-4-nitroanilide (Glucana) a as substrate (r=0.98).
2002-12-05