Abstract
The reduction of linoleic acid hydroperoxide catalyzed by rat liver cytosol was previously shown to be catalyzed by a selenium-dependent glutathione peroxidase. In contrast, the activity in rabbit liver cytosol could also be attributed to a selenium-dependent peroxidase. The selenium-independent peroxidase copurified with glutathione transferase B and was completely inhibited by antitransferase B antiserum and transferase substrates. These results suggest that glutathione transferase B in rabbit liver cytosol is involved in the intracellular decomposition of lipid peroxide and could explain the lower selenium requirement of rabbits in comparison with other species.
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