Studies on the Glutathione Stability of Normal and Glucose-6-Phospate-Dehydrogenase-Deficient Human Erythrocytes

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Abstract
The activities of glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, NADPH2 glutathione oxidoreductase, and the concentration and stability of glutathione in erythrocytes from normal men and from a case of glucose-6-phosphate dehydrogenase deficiency (Gd(-)‘Aarhus’) have been studied. The anticoagulant used was found to have a remarkable influence on the glutathione stability test. In Gd(-)‘Aarhus’ the glutathione stability was about normal when blood was collected in ACD, and substantially lower when blood was collected in heparin, heparin + glucose, and EDTA + glucose. The erythrocytes from Gd(-)‘Aarhus’ showed a lower utilization of glucose for the reduction of glutathione than normal human erythrocytes. The ability of normal and G6PD-deficient erythrocytes to utilize different substrates in the reduction of oxidized glutathione has been studied. Evidence of the presence of a glutathione-stability-depressing factor in plasma is presented.