Abstract
Summary
Glutathione reductase from rabbit erythrocytes was purified to homogeneity and found to be a monomer with a mol wt of 60,000. Both NADPH and NADH were capable of acting as cofactors for the reduction of GSSG and the following kinetic values were obtained: K m, gssg =120 μM; K m, nadph = 37 μM; V max = 23 μmoles NADPH/min/mg protein, K m, nadh = 420 μM; V max = 3 jumoles NADH/min/mg protein. Rabbit erythrocyte GR exhibited substrate inhibition, and was susceptible to inhibition by p-hydroxymercuribenzoate under certain conditions.
The invaluable assistance of Mrs. Mary E. Bayliss and Mrs. Stella H. Wilkes with some of the experiments is gratefully acknowledged.
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