Role of tentacles and protein loading on pore accessibility and mass transfer in cation exchange materials for proteins.

In protein chromatography, the size of the protein determines which fraction of pores it can access within a resin and at which rate of diffusion. Moreover, in the presence of grafted polymers like in advanced materials, adsorbed proteins and electrolytes complicate the interaction pore-protein. In this study, we evaluated in a comparative way the behavior of Fractogel EMD SO3 (M) and (S), "tentacle"-type, strong cation exchangers, as well as a reference material without tentacles, all of which are commonly used for protein purification.

Cation-exchange chromatography of monoclonal antibodies: characterisation of a novel stationary phase designed for production-scale purification.

A novel cation-exchange resin, Eshmuno™ S, was compared to Fractogel® SO3(-) (M) and Toyopearl GigaCap S-650M. The stationary phases have different base matrices, and carry specific types of polymeric surface modifications. Three monoclonal antibodies (mAbs) were used as model proteins to characterize these chromatographic resins.