title: [Isolation and purification of glutathione peroxidase].
abstract: Electrophoretically homogeneous glutathione peroxidase (EC 1.11.1.9) preparation from rat liver with a specific activity of 1.46 U/mg of protein and a yield of 7.2% was obtained using the purification procedure developed. The K(M) values for reduced glutathione and hydrogen peroxide were 0.033 and 0.208 mM, respectively. The enzymatic reaction had the following characteristics: the temperature optimum, 32 degrees C; the pH optimum, 7.4; and the activation energy, 29.1 kJ/mol. The molecular weight of the enzyme was 88 kDa.
authors.forename: K K
authors.initials: KK
authors.lastname: Shul'gim
authors.forename: T N
authors.initials: TN
authors.lastname: Popova
authors.forename: T I
authors.initials: TI
authors.lastname: Rakhmanova
mesh_terms: D000818:Animals; D002384:Catalysis; D005978:Glutathione / Q000737:chemistry*; D005979:Glutathione Peroxidase / Q000737:chemistry* / Q000302:isolation & purification*; D006358:Hot Temperature; D006861:Hydrogen Peroxide / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008099:Liver / Q000201:enzymology*; D008297:Male; D051381:Rats
chemical_list: D006861:Hydrogen Peroxide; D005979:Glutathione Peroxidase; D005978:Glutathione