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Clinical Chemistry 31: 1380-1383, 1985;
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Clinical Chemistry, Vol 31, 1380-1383, Copyright © 1985 by American Association for Clinical Chemistry

Kinetic assay of gamma-glutamyltransferase with use of bilirubin oxidase as a coupled enzyme

S Satomura, Y Miki, T Hamanaka and Y Sakata

We studied the kinetic measurement of gamma-glutamyltransferase (EC.2.3.2.2), coupling the reaction with that catalyzed by bilirubin oxidase (EC 1.3.3.5), which oxidizes and combines a phenylenediamine derivative with an aniline derivative to produce a green pigment. We measured the formation of the pigment kinetically (at lambda max745 nm, epsilon = 75 000 L mol-1 cm-1), with L-gamma-glutamyl-N- hydroxyethylaminoanilide as substrate and N-ethyl-N-hydroxy-3- sulfopropyl)-m-toluidine as a the coupling derivative. The within-run CV for measuring this reaction in samples of normal sera was 2.4%. A calibration plot of the change in absorbance per minute vs enzyme activity concentration showed good proportionality in the range of 0- 1300 U/L. The results of this assay correlated well (r = 0.995) with those of the Boehringer method, in which L-gamma-glutamyl-3-carboxy-4- nitroanilide is the substrate. This new, highly sensitive procedure may be adapted to other assays involving phenylenediamine derivates as synthetic substrates.




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Copyright © 1985 by the American Association for Clinical Chemistry.