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


Selenium-containing glutathione peroxidase (EC was purified 6000-fold from bovine red blood cells to apparent homogeneity. Lipoxygenase (EC 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 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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@article{Grossmann1983NonreactivityOT, title={Non-reactivity of the selenoenzyme glutathione peroxidase with enzymatically hydroperoxidized phospholipids.}, author={Angelika Grossmann and Albrecht Wendel}, journal={European journal of biochemistry}, year={1983}, volume={135 3}, pages={549-52} }