Purification and Properties of Glutathione Peroxidase from Human Liver

Abstract

Human liver glutathione peroxidase was purified to homogeneity by using acetone precipitation, ammonium sulfate precipitation, DEAE-cellulose column chromatography, Sephadex G-150 gel filtration, and ECTEOLA-cellulose, CM-Sephadex, and DEAE-Sephadex column chromatographies. Its homogeneity was confirmed by polyacrylamide gel electrophoresis and SDS-polyacrylamide gel electrophoresis. Human liver glutathione peroxidase contained 3.7 g-atoms of selenium per mole of enzyme. The molecular weights of the enzyme and subunit were 90000 and 23000, respectively. Glutathione peroxidase consists of 4 subunits with equal subunit molecular weight. The properties of human liver glutathione peroxidase were compared with those of human placental glutathione peroxidase which was purified by the same method. In an immunological study, placental and erythrocyte glutathione peroxidases both reacted with the antibody to human liver glutathione peroxidase. © 1983, The Pharmaceutical Society of Japan. All rights reserved.