Role of Haemoglobin in the Protection of Reduced Glutathione against Destruction by ‘Oxidant’ Drugs

Abstract

THE fact that the administration of haemolytic drugs such as primaquine results in methaemoglobin formation¹, as well as in the destruction of reduced glutathione (GSH)², has suggested that there might be a causal relationship between these alterations in the erythrocyte. Harley and Robin³ have proposed that oxyhaemoglobin serves as a redox buffer system which protects GSH against oxidation by nitrite. If this concept may be extended to oxidation by aromatic drugs⁴, one might expect that the GSH of methaemoglobin-containing cells would be more susceptible to destruction than that of oxyhaemoglobin-containing cells, the buffer system no longer being active. Studies of the effect of intracellular methaemoglobin formation on the stability of red cell GSH have not, to our knowledge, been reported previously.