NON-REACTIVITY OF THE SELENOENZYME GLUTATHIONE-PEROXIDASE WITH ENZYMATICALLY HYDROPEROXIDIZED PHOSPHOLIPIDS
NON-REACTIVITY OF THE SELENOENZYME GLUTATHIONE-PEROXIDASE WITH ENZYMATICALLY HYDROPEROXIDIZED PHOSPHOLIPIDS
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DOI:
10.1111/j.1432-1033.1983.tb07687.x
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发表时间:
1983-01-01
期刊:
影响因子:
--
通讯作者:
WENDEL, A
中科院分区:
文献类型:
--
作者:
GROSSMANN, A;WENDEL, A
Se-containing glutathione peroxidase (EC 1.11.1.9) was purified 6000-fold from bovine red blood cells to apparent homogeneity. Lipoxygenase (EC 1.13.11.12) was enriched 20-fold from soybean acetone powder. Linoleic acid was peroxidized with lipoxygenase and then used as a substrate in the glutathione peroxidase reaction. Analogous experiments were conducted with synthetic 1,2-dilinoleoyl-L-.alpha.-glycerophosphocholine and with natural bovine heart cardiolipin. The peroxidized phospholipids were reactive with glutathione peroxidase only after enzymatic attack by [pig pancreas] phospholipase A2 (EC 3.1.1.4). This result implies that the membrane-protective function of glutathione peroxidase includes preceding phospholipase action and excludes a direct interaction of this enzyme with membrane-bound lipid hydroperoxides.