title: The binding by an NAD-affinity matrix of contaminating dehydrogenases in cytochrome c oxidase preparations.
abstract: An NAD-matrix is capable of the separation of three contaminant reductase activities from highly purified beef heart cytochrome c oxidase. Non-specific binding of cytochrome c oxidase occurs as well. When the matrix is saturated with respect to the non-specific binding, continued binding of the reductases can be observed. As a consequence of equilibration with the matrix, the turnover numbers of the unbound cytochrome c oxidase are increased.
mesh_terms: D002846:Chromatography, Affinity / Q000379:methods; D003576:Electron Transport Complex IV / Q000302:isolation & purification*; D005292:Ferricyanides / Q000378:metabolism; D006418:Heme / Q000302:isolation & purification; D007700:Kinetics; D009243:NAD; D009246:NADH Tetrazolium Reductase / Q000378:metabolism; D009247:NADH, NADPH Oxidoreductases / Q000302:isolation & purification* / Q000378:metabolism; D010446:Peptide Fragments / Q000302:isolation & purification; D012685:Sepharose
chemical_list: D005292:Ferricyanides; D010446:Peptide Fragments; D009243:NAD; D006418:Heme; D012685:Sepharose; D009246:NADH Tetrazolium Reductase; D009247:NADH, NADPH Oxidoreductases; D003576:Electron Transport Complex IV