title: Purification and kinetics of bovine kidney cortex glutathione reductase.
abstract: Glutathione reductase was purified 34806-fold with a final yield of 85 % from the bovine kidney cortex. Some molecular and kinetic properties of purified enzyme are investigated. Product inhibition studies showed that the enzyme obeys 'branched" mechanism: Km(NADPH) 18 +/- 3 microM and Km(GSSG) 65 +/- 5 microM were determined.
authors.affiliation: Hacettepe University, Faculty of Medicine, Department of Biochemistry, 06100 Ankara, Turkey.
authors.forename: B
authors.initials: B
authors.lastname: Tandogan
authors.forename: N N
authors.initials: NN
authors.lastname: Ulusu
mesh_terms: D000818:Animals; D002417:Cattle; D002853:Chromatography, Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005978:Glutathione / Q000378:metabolism; D019803:Glutathione Disulfide / Q000378:metabolism; D005980:Glutathione Reductase / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007672:Kidney Cortex / Q000201:enzymology*; D007700:Kinetics; D009249:NADP / Q000378:metabolism; D017711:Nonlinear Dynamics
chemical_list: D009249:NADP; D005980:Glutathione Reductase; D005978:Glutathione; D019803:Glutathione Disulfide