Non‐reactivity of the selenoenzyme glutathione peroxidase with enzymatically hydroperoxidized phospholipids
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Open Access
- 1 October 1983
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 135 (3) , 549-552
Abstract
Selenium‐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‐α‐glycerophosphocholine and with natural bovine heart cardiolipin. The peroxidized phospholipids were reactive with glutathione peroxidase only after enzymatic attack by phospholipase A2 (EC 3.1.1.4). This result implies that the membrane‐protective function of glutathione peroxidase includes preceeding phospholipase action and excludes a direct interaction of this enzyme with membrane‐bound lipid hydroperoxides.Keywords
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