Abstract
A study of the mechanism of inhibition of glutathione reductase activity by BCNU (1,3-bis(2-chloroethyl)-1-nitrosourea) demonstrated that the enzyme was protected from inhibition by mercaptoethanol. N-Ethylmaleimide competes with BCNU and also protects the enzyme from inhibition. The inhibited enzyme showed decreased affinity for NADPH. Our data suggest that the inhibition of glutathione reductase is due to an alteration of the redox state. Several other red cell enzymes were inhibited by high concentrations of BCNU; these enzymes were also protected by mercaptoethanol. Among alkylating agents tested, only BCNU inhibited glutathione reductase at therapeutic levels.
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