The effect of copper on human erythrocyte glutathione reductase

Abstract

1. 1. The influence of copper on purified human erythrocyte glutathione reductase (E.C. 1.6.4.2) was studied. The holoenzyme was inhibited at low oxidized glutathione (GSSG) concentrations. At a glutathione concentration of 1 mM and higher no inhibition at all was found. The inhibition was independent of the concentration of NADPH.

2. 2. When the holoenzyme was preincubated with copper much more inhibition was found. This inhibition could be prevented by adding oxidized glutathione to the incubation mixture.

3. 3. The recombination of the apoenzyme with FAD was inhibited by copper. This inhibition by copper was competitive with respect to FAD.