title: Sheep brain glutathione reductase: purification and general properties.
abstract: Sheep brain glutathione reductase was purified about 11,000-fold with an overall yield of 40%. The method included ammonium sulphate fractionation, heat denaturation, 2',5'-ADP Sepharose 4B and Sephadex G-200 chromatography steps. Specific activity at the final step was 193 IU/mg. The Mr of the enzyme was found to be 116,000 by gel filtration chromatography. On SDS-PAGE, two identical subunits of Mr 64,000 were obtained. From the spectral data, about 2 mol FAD per mol of enzyme were calculated.
authors.affiliation: Department of Biochemistry, Faculty of Medicine, Hacettepe University, Ankara, Turkey.
authors.forename: N L
authors.initials: NL
authors.lastname: Acan
authors.forename: E F
authors.initials: EF
authors.lastname: Tezcan
mesh_terms: D000818:Animals; D001921:Brain / Q000201:enzymology*; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D005980:Glutathione Reductase / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D012756:Sheep
chemical_list: D005980:Glutathione Reductase