Purification and Immunochemical Analysis of Rat Liver Glutathione Peroxidase

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Abstract
Glutathione peroxidase (EC 1.11.1.9) was purified about 1500-fold from rat liver cytosol by means of ammonium sulfate fractionation and chromatographies on CM-Sephadex C-50, Sephacryl S-200 and activated thiol-Sepharose 4B. The final enzyme preparation proved to be homogeneous on polyacrylamide gel electrophoresis and to be composed of four identical subunits with a molecular weight of 20,000. The rabbit antiserum against the purified enzyme gave a single fused precipitation line between the crude and purified enzymes. A quite similar displacement curve was observed for both liver cytosols from rats fed 20% casein diets with and without selenium supplementation, as a result of immunochemical titration with the antiserum. It therefore is apparent that an immunochemically recognizable protein other than glutathione peroxidase does not accumulate in a detectable quantity, if there is any in rat liver; dietary selenium-induced increase of glutathione peroxidase activity in the liver is accompanied with protein synthesis.

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