Reaction of ozone with sulfhydryls of human erythrocytes

Oxidation of GSH by ozone yielded 60% GSSG. Exposure of human erythrocytes to ozone caused oxidation of intracellular GSH. Between 4 and 6% of the administered ozone caused GSH oxidation. No more than 30% of the GSH oxidized by ozone could be accounted for by GSSG in the erythrocyte. The GSSG formed in the erythrocyte was rapidly reduced and the pentose phosphate pathway was stimulated. When GSH and unsealed erythrocyte ghosts were simultaneously exposed to ozone, 6–11% of the oxidized GSH could be accounted for as mixed disulfide of protein and GSH. When GSH and cytoplasmic proteins from the erythrocyte were simultaneously exposed to ozone, 5–7% of the oxidized GSH could be accounted for as mixed disulfide. Ozone generated membrane protein disulfide crosslinks when erythrocyte ghosts, but not intact erythrocytes, were exposed. Ozone had no effect on glucose uptake and did not change oxyhemoglobin content of the erythrocytes.