Glutathione peroxidase isolated from plasma reduces phospholipid hydroperoxides.
Glutathione peroxidase isolated from plasma reduces phospholipid hydroperoxides.
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DOI：
10.1006/abbi.1993.1458
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发表时间：
1993-09
影响因子：
3.9
通讯作者：
Y. Yamamoto;Koui Takahashi
中科院分区：
文献类型：
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作者：
Y. Yamamoto;Koui Takahashi
从血浆中分离的硒酶谷胱甘肽过氧化物酶对磷脂酰胆碱氢过氧化物和光过氧化红细胞鬼影的反应性进行了研究。从血浆中分离出的谷胱甘肽过氧化物酶可催化磷脂酰胆碱氢过氧化物还原为相应的羟基衍生物。这种酶还能在光过氧化物中还原氢过氧化物。酶处理鬼的薄层色谱分析显示血浆谷胱甘肽过氧化物酶可以减少磷脂衍生的氢过氧化物，但不能减少胆固醇的氢过氧化物。这些研究表明，三种已知的谷胱甘肽过氧化物酶（细胞、血浆和磷脂过氧化氢）在底物特异性上彼此不同。
The reactivities of a selenoenzyme, glutathione peroxidase isolated from plasma, against phosphatidylcholine hydroperoxides and photoperoxidized erythrocyte ghosts have been investigated. Glutathione peroxidase isolated from plasma was found to catalyze the reduction of phosphatidylcholine hydroperoxides to the corresponding hydroxy derivatives. The enzyme is also capable of reducing the hydroperoxides in photoperoxidized ghosts. Thin layer chromatographic analysis of enzyme-treated ghosts revealed that plasma glutathione peroxidase can reduce phospholipid-derived hydroperoxides but cannot reduce cholesterol hydroperoxides. These studies demonstrate that the three known glutathione peroxidase (cellular, plasma, and phospholipid hydroperoxide) differ from each other in substrate specificity.