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The protective function of alpha-tocopherol, glutathione (GSH), and glutathione peroxidase (GSH-Px) from tert-butyl hydroperoxide (t-BuOOH)-induced hemolysis was studied with the erythrocytes from male Wistar rats fed selenium (Se)-adequate or -deficient diet for 3 months. By the preincubation with a water-soluble radical initiator, 2,2'-azobis(2-amidinopropane) dihydrochloride (AAPH), at 10 mM for 6 h at 37 degrees C, alpha-tocopherol levels of the erythrocytes were decreased to 40% of the original level, that is, to the level insufficient for supporting the normal functions of the erythrocytes. With the Se-deficient cells, the hemolysis proceeded rapidly irrespective of the presence or absence of GSH in the incubation medium, and irrespective of the presence or absence of AAPH in the preincubation medium. Contrarily, GSH suppressed the hemolysis of Se-adequate cells which were preincubated with and without AAPH. These results are consistent with the notion that Se serves as the prime, important defense mechanism in the t-BuOOH-induced hemolysis through the activity of GSH-Px. Either alpha-tocopherol or GSH by itself, or both by themselves, may not play so significant a role as Se does in suppressing the hemolysis.

Tert-butyl hydroperoxide-induced hemolysis of .ALPHA.-tocopherol-decreased erythrocytes from selenium-deficient and selenium-adequate rats.