Application of neutral hydrophobic gels in hydrophobic chromatography

Summary

The adsorption of different serum proteins was chromatographically measured under standardized conditions. The results show that Sepharose 4B adsorbs serum proteins more strongly than a methyl-substituted sepharose gel (gel 2a). Gels with substituents with chain lengths from C₁ to C₅ show only relatively low adsorptivity. A protein dependent critical chain length of the substituents with stronger binding forces toward these proteins could be identified. A branching of the substituents and very voluminous groups reduce hydrophobic binding forces. Among the functional end groups investigated in this work, hydrophilic moieties, carboxylate, and cyano groups proved to be low serum protein adsorbing functional chemical groups.