ACTIVATION OF RED-BLOOD-CELL GLUTATHIONE-PEROXIDASE AND MORPHOLOGICALTRANSFORMATION OF ERYTHROCYTES UNDER THE ACTION OF TERT-BUTYL HYDROPEROXIDE

Susceptibility of control and diabetic erythrocytes to oxidative stres s was measured after incubation with various concentration of tert-but yl hydroperoxide (t-BHP). TBA-reactive substances (TEARS) formed were determined by the method of Stocks & Dormady [9] modified by Jain [2]. GSH and total glutathione were estimated by the procedure of Ellman [ 10] and Akerboom and Sies [11]. Activity of GSH peroxidase was determi ned by the method of Martinet et al. [12]. Protein SH groups were dete rmined after membrane isolation by the method of Dodge et al. [13]. Ce ll morphology was viewed under phase contrast microscope with a magnif ication of 500x. All results were analyzed by the unpaired two tailed Student's t-test. Oxidative treatment of erythrocytes with tert-butyl hydroperoxide significantly increases the reaction rate but decreases the affinity for substrate (tert-butyl hydroperoxide). The susceptibil ity of the enzyme from diabetic erythrocytes to oxidation is higher in comparison with normal cells. The oxidation of cellular reduced gluta thione (GSH) is not correlated with oxidation of membranous protein SH -groups. Oxidative damage of erythrocytes induces significant cell mor phological transformations.