The reduction of glutathione by the Warburg-Christian system

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Abstract
Glutathione is reduced under both aerobic and anaerobic conditions by Warburg and Christian''s isolated dehydrogenase system with hexose- monophosphate as substrate; more slowly with phospho-hexonic acid as substrate; only slightly when fructose-diphosphate is used; and not at all when diphospho-glyceric acid, glucose or fructose are used as substrates. Glutathione functions as O carrier when hexose-mono-phosphoric acid is oxidized by the Warburg-Christian dehydrogenase system in presence of molecular O, the velocity of the reaction being ca. proportional to the amt. of added glutathione, and the limiting factor of the oxidation of the acid being the velocity of autoxidation of reduced glutathione. Cysteine also functions as O carrier in this system, but in this case the oxidation velocity is independent of the cysteine conc., the limiting factor being the rate of reduction of cystine. The dehydrogenase system is active when enzyme prepared from rat''s blood, baker''s or brewer''s yeast is used.