REDUCED GLUTATHIONE AND SPONTANEOUS METHÆMOGLOBIN FORMATION IN HÆMOLYSATES

¹ The Department of Physiology, University of Edinburgh, and the Agricultural Research Council Institute of Animal Physiology, Babraham, Cambridge

1. The rates of both spontaneous methæmoglobin (MHb) formation and oxidation of reduced glutathione (GSH), and the extent of decomposition of easily hydrolysable (ATP) phosphorus compounds, were determined in hæmolysates either destromatized by treatment with carbon dioxide, or filtered (partially destromatized), and in untreated hæmolysates (ox and horse erythrocytes).

2. The formation of MHb, GSH oxidation, and the extent of ATP decomposition, were found to be slower in untreated than in destromatized hæmolysates. When deoxygenated, the untreated hæmolysates reduced oxidized glutathione more effectively than did destromatized hæmolysates.

3. GSH added to destromatized hæmolysates retards MHb formation.

4. "Stroma" (posthæmolytic residue) contains a mechanism which supports the optimal concentration of GSH. It is suggested that GSH serves as one of the main factors protecting Hb against oxidation by molecular oxygen.