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- W1988998244 abstract "Glutathione peroxidase (GSH:H2O2 oxidoreductase, EC 1.11.1.9) was purified 400-fold from rat liver by fractionation with (NH4)2SO4 and chromatography with DEAE-cellulose, Sepha dex G-200 and DEAE-Sephadex A-50 in the presence of 0.5 mM GSH. The purified enzyme was shown to be homogeneous in Sephadex chromatography and ultracentrifugation. The molecular weight of the enzyme was estimated to be 78 500 from s°20,w and D020,w, 76 000 from sedimentation equilibrium measurement and 75 000–76 000 by thin-layer gel filtration. In the presence of 1.0% sodium dodecylsulfate, the molecular weight was reduced to 19 000 from polyacrylamide-gel electrophoresis, indicating that the native enzyme consists of four subunits with the same molecular size. The molecular weight of the subunit was also calculated to be 17 000 from amino acid composition. It was also found that the enzyme contained 4 atoms of selenium ion and 8 moles of free sulfhydryl groups per mole of protein. No absorption spectrum characteristic of heme or flavin was observed. The enzyme activity was decreased gradually and significantly during the storage of the enzyme in the absence of dithiothreitol even at the frozen state, probably due to the denaturation of the enzyme." @default.
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- W1988998244 date "1974-08-01" @default.
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- W1988998244 title "Purification and properties of rat liver glutathione peroxidase" @default.
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- W1988998244 doi "https://doi.org/10.1016/0005-2744(74)90455-0" @default.
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