Separation of dehydrogenases on polyaminomethylstyrene.
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.
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
D007475:Ion Exchange Resins; D011073:Polyamines; D011137:Polystyrenes; D012709:Serum Albumin; D000429:Alcohol Oxidoreductases