title: Separation of dehydrogenases on polyaminomethylstyrene.
abstract: The binding of dehydrogenases, especially alcohol dehydrogenase, and other proteins to several ion exchangers and hydrophobic polymers was investigated. Quantitative parameters for the stability of the polymer-protein complexes (obtained form double reciprocal plots) indicate a high but different affinity of many proteins for polyaminomethylstyrene. The chromatography of a mixture of five dehydrogenases and human serum albumin on polyaminomethylstyrene is described.
mesh_terms: D000429:Alcohol Oxidoreductases / Q000032:analysis*; D002499:Centrifugation, Density Gradient; D002852:Chromatography, Ion Exchange; D006863:Hydrogen-Ion Concentration; D007475:Ion Exchange Resins; D008722:Methods; D008745:Methylation; D011073:Polyamines; D011137:Polystyrenes; D011485:Protein Binding; D012709:Serum Albumin / Q000032:analysis; D014465:Ultrasonics
chemical_list: D007475:Ion Exchange Resins; D011073:Polyamines; D011137:Polystyrenes; D012709:Serum Albumin; D000429:Alcohol Oxidoreductases