PMID: 6413205Oct 3, 1983Paper

Non-reactivity of the selenoenzyme glutathione peroxidase with enzymatically hydroperoxidized phospholipids

European Journal of Biochemistry
A Grossmann, A Wendel

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-alpha-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.

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Citations

Jan 1, 1988·Chemico-biological Interactions·J Meijer, J W DePierre
Jul 1, 1987·Chemistry and Physics of Lipids·F Ursini, A Bindoli
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