L-Glutamic acid γ-(3-carboxy-4-nitroanilide) ammonium salt has been used as a synthetic substrate for gamma-glutamyltransferase (GGT) to determine GGT activity.[1]
The kinetics of human serum gamma-glutamyltransferase (EC 2.3.2.2) were investigated, with use of glycylglycine as a gamma-glutamyl acceptor substrate and gamma-glutamyl-4-nitroanilide and its carboxy derivative, gamma-glutamyl-3-carboxy-4-nitroanilide, as donor substrates. The simultaneous occurrence of both gamma-glutamyltransfer and autotransfer was established by
A kinetic study of gamma-glutamyltransferase (GGT)-mediated S-nitrosoglutathione catabolism.
Angeli V
Archives of Biochemistry and Biophysics, 481(2), 191-196 (2009)
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