THE AMPEROMETRIC DETERMINATION OF GLUTATHIONE REDUCTASE ACTIVITY IN HUMAN ERYTHROCYTES

Abstract
Glutathione reductase activity of hemolyzates of human erythrocytes was measured by an amperometric titration of the reduced glutathione that is formed from oxidized glutathione. The electron donor in the system was reduced triphosphopyridine nucleotide, produced by the glucose-6-phosphate dehydrogenase of the cells. Removal of the red-cell stromata from hemolyzates slightly increased the reductase activity. Addition of Na+, K+, or Ca++ had no effect on the enzyme. No marked inhibition was-observed in the presence of phenothiazine, phenothiazone, phenylhydrazine, or p-chloromercuribenzoate.