Selenium-independent glutathione peroxidase activity in rabbit liver.
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.
D000818:Animals; D003600:Cytosol / Q000201:enzymology; D005979:Glutathione Peroxidase / Q000302:isolation & purification / Q000378:metabolism*; D005982:Glutathione Transferase / Q000378:metabolism; D007118:Immunoassay; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D010544:Peroxidases / Q000378:metabolism*; D011817:Rabbits; D012643:Selenium / Q000494:pharmacology*
D010544:Peroxidases; D005979:Glutathione Peroxidase; D005982:Glutathione Transferase; D012643:Selenium