Glutathione reductases from a variety of sources are inhibited by physiological levels of glutathione.
1. Glutathione reductase from human platelets, bovine intestinal mucosa, yeast and E. coli were inhibited in vitro by physiological levels of reduced glutathione with IC50s of 6.61 mM, 2.92 mM, 2.40 mM and 12.11 mM, respectively. 2. A steady-state kinetic examination revealed that glutathione inhibited the NADPH oxidation (at constant [glutathione-disulphide]) catalysed by the eucaryotic enzymes uncompetitively, whereas the E. coli enzyme appeared unaffected by glutathione concentrations of up to 10 mM. 3. With respect to glutathione inhibition of glutathione-disulphide reduction (at constant [NADPH]), the human enzyme was inhibited uncompetitively; the bovine and yeast enzymes displayed apparent mixed hyperbolic inhibition; the E. coli enzyme was inhibited competitively.
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