GLUTATHIONE-PEROXIDASE ISOLATED FROM PLASMA REDUCES PHOSPHOLIPID HYDROPEROXIDES

被引：131
|
作者：
YAMAMOTO, Y [1 ]
TAKAHASHI, K [1 ]
机构：
[1] HOKKAIDO UNIV,FAC PHARMACEUT SCI,DEPT HYG CHEM,KITA 16,NISHI 6,KITA KU,SAPPORO,HOKKAIDO 060,JAPAN
来源：
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 1993年 / 305卷 / 02期
关键词：
D O I：
10.1006/abbi.1993.1458
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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. © 1993 Academic Press, Inc.
引用
收藏
页码：541 / 545
页数：5
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