[Changes in glyceraldehydephosphate dehydrogenase, glucose-6-phosphate dehydrogenase, superoxide dismutase, and catalase activity in erythrocytes depending upon the rate of glucose utilization].

Content of glucose as well as activities of glyceraldehyde phosphate dehydrogenase (alpha-GPD), glucose-6-phosphate dehydrogenase (G6PD), superoxide dismutase (SOD) and catalase were studied in whole blood, in intact and hemolyzed erythrocytes of 57 volunteers within 120 min after sucrose loading. Direct correlation was found between the activity of the enzymes studied and level of glucose as well as the rate of its utilization in erythrocytes. These data suggest that reduced NAD- and NADP-containing oxidoreductases alpha-GPD and G6PD are donors of H+ used in biosynthesis of H2O2 catalyzed by SOD. Intact and hemolyzed erythrocytes are involved in destruction of H2O2 accompanied by liberation of O2, which reacted with Hb more readily as compared with atmospheric oxygen.