Srivastava S K, Awasthi Y C, Beutler E
Biochem J. 1974 May;139(2):289-95. doi: 10.1042/bj1390289.
t-Butyl hydroperoxide and cumene hydroperoxide, both known to be substrates for glutathione peroxidase, were used to oxidize erythrocyte GSH. Addition of concentrations of hydroperoxides equimolar with respect to GSH in the erythrocytes or whole blood quantitatively oxidizes GSH in the erythrocytes with a half-time of 4.5s at 37 degrees C and about three times as long at 4 degrees C. In the presence of glucose, normal erythrocytes regenerate all the GSH in about 25min. However, glucose 6-phosphate dehydrogenase-deficient erythrocytes failed to regenerate GSH. Treatment of erythrocytes with hydroperoxides does not affect erythrocyte survival in rabbits. Oxidation of erythrocyte GSH with equimolar concentrations of hydroperoxides does not lead to formation of mixed disulphides of haemoglobin and GSH. The hydroperoxides do not affect erythrocyte glycolytic and hexose monophosphate-shunt-pathway enzymes. Previous studies on transport of GSSG from erythrocytes were confirmed by using t-butyl hydroperoxide to oxidize erythrocyte GSH.
叔丁基过氧化氢和异丙苯过氧化氢均为谷胱甘肽过氧化物酶的底物,被用于氧化红细胞中的谷胱甘肽(GSH)。在红细胞或全血中加入与GSH等摩尔浓度的氢过氧化物,可定量氧化红细胞中的GSH,在37℃时半衰期为4.5秒,在4℃时约为其3倍长。在有葡萄糖存在的情况下,正常红细胞在约25分钟内可使所有GSH再生。然而,葡萄糖6-磷酸脱氢酶缺乏的红细胞无法使GSH再生。用氢过氧化物处理红细胞不影响兔红细胞的存活。用等摩尔浓度的氢过氧化物氧化红细胞GSH不会导致血红蛋白与GSH形成混合二硫化物。氢过氧化物不影响红细胞糖酵解和磷酸戊糖途径的酶。通过使用叔丁基过氧化氢氧化红细胞GSH,证实了先前关于红细胞中氧化型谷胱甘肽(GSSG)转运的研究。