Selenium-independent glutathione peroxidase activity in rabbit liver

Abstract
The reduction of linoleic acid hydroperoxide catalyzed by rat liver cytosol is catalyzed by a Se-dependent glutathione peroxidase. The activity in rabbit liver cytosol could also be attributed to a Se-independent glutathione peroxidase present in an amount approximately equal to the Se-dependent peroxidase. The Se-independent peroxidase copurified with glutathione transferase B and was completely inhibited by antitransferase B antiserum and transferase substrates. Glutathione transferase B in rabbit liver cytosol is involved in the intracellular decomposition of lipid peroxide and could explain the lower Se requirement of rabbits in comparison with other species.