Abstract
THE question of whether the activities of NADPH—or NADH—glutathione reductase are caused by a single enzyme or by two different enzymes has never been satisfactorily resolved1–4. We have devised a new method for detecting glutathione reductase (GSSGR) activity after starch gel electrophoresis. The study of subjects with an electrophoretically fast mutant glutathione reductase has enabled us to present findings which strongly favour the suggestion that glutathione reductase activities with respect to both pyridine nucleotide coenzymes reside in the same molecule. Some observations have also been made in glutathione reductase deficient and NADH-diaphorase (NADH methaemoglobin oxido-reductase) deficient subjects.
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