Abstract
It has been commonly assumed that one function of glutathione in the tissues (others have been suggested) is to act, in virtue of its sulphur groupings, as a carrier of hydrogen from reducing systems to molecular oxygen. This assumption has hitherto been based upon its behaviour when added to washed tissue preparations. The observations of Meldrum and Dixon (1930), however, have shown that the tripeptide, after its separation from the tissues in crystalline form, while freely reduced by tissue preparations, undergoes oxidation by molecular oxygen only with the co-operation of two factors present as traces in most preparations of the substance ; not alone iron (or copper) of which the necessity was long ago shown by Warburg and Harrison, but also some substance able to form eatalytically active complexes with the metal. Unlike earlier, less pure, preparations the crystalline product when added to washed tissues entirely fails to produce a system capable of taking up oxygen.
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