Hydrophobic interaction chromatography on noncharged sepharose® derivatives: Binding of a model protein, related to ionic strength, hydrophobicity of the substituent, and degree of substitution (determined by NMR)

摘要: Abstract A series of agarose gels, substituted with hydrophobic groups, has been synthesized and used for binding studies the coloured model protein, phycoerythrin. The degrees substitution derivatives can easily be estimated proton magnetic resonance (NMR). It found that capacity phycoerythrin increases increasing hydrophobicity substituent, degree ionic strength. For column experiments should lie in range 40–100 mmol substituent/mol galactose. When it is excessively high, flow characteristics columns are unsatisfactory difficulties to achieve complete desorption may arise.