Mavelli I, Ciriolo M R, Rotilio G
Biochim Biophys Acta. 1985 Dec 12;847(3):280-4. doi: 10.1016/0167-4889(85)90032-1.
A significant inactivation of red blood cell glutathione peroxidase (25% less than the physiological value) was observed after exposure of intact erythrocytes to 2 mM divicine (an autoxidizable aminophenol from Vicia faba seeds) and 2 mM ascorbate for 3 h at 37 degrees C. Addition of catalase and conversion of Hb to the carbomonoxy derivative resulted in protection against enzyme inactivation. Oxidation of Hb was a concurrent phenomenon, and augmented the inactivating effect. In hemolysates, much stronger effects were observed at shorter times (2 h); divicine was effective also without ascorbate, and the presence of reductants (ascorbate or glutathione or NADPH) enhanced its inactivating power. Of the other antioxidant enzymes, superoxide dismutase was unaffected under the same experimental conditions. Catalase was found to be much less sensitive to the inactivation; it was almost unaffected in experiments with intact erythrocytes and specifically protected by NADPH in experiments with hemolysates. This specific damage of glutathione peroxidase, apparently involving interaction of H2O2 and HbO2, may be related to the pathogenesis of hemolysis in favism.
将完整红细胞在37℃下暴露于2 mM 蚕豆嘧啶（一种来自蚕豆种子的可自氧化氨基酚）和2 mM抗坏血酸盐3小时后，观察到红细胞谷胱甘肽过氧化物酶显著失活（比生理值低25%）。添加过氧化氢酶以及将血红蛋白转化为碳氧血红蛋白衍生物可防止酶失活。血红蛋白的氧化是一个同时发生的现象，并增强了失活作用。在溶血产物中，在更短的时间（2小时）观察到更强的作用；蚕豆嘧啶在没有抗坏血酸盐的情况下也有效，并且还原剂（抗坏血酸盐或谷胱甘肽或NADPH）的存在增强了其失活能力。在相同实验条件下，其他抗氧化酶超氧化物歧化酶未受影响。发现过氧化氢酶对失活的敏感性要低得多；在完整红细胞的实验中它几乎未受影响，而在溶血产物的实验中它受到NADPH的特异性保护。谷胱甘肽过氧化物酶的这种特异性损伤，显然涉及过氧化氢和氧合血红蛋白的相互作用，可能与蚕豆病溶血的发病机制有关。
