Abstract
AbstractThe influence of ionic strength on the adsorption capacity of seven commercial adsorbents used in downstream processing of monoclonal antibodies was examined. Affinity (MabSelect, Poros 50A High Capacity, ProSep-vA High Capacity), hydrophobic charge-induction (MEP HyperCel), and cation exchange adsorbents (FractoGel EMD SE Hicap (M), SP Sepharose Fast Flow, Ceramic HyperD F) were used to study the adsorption of polyclonal human immunoglobulin G at optimal pH values. The ionic strength, adjusted by sodium chloride concentrations in the range of 0–225 mM, strongly decreased the adsorption capacity of the cation exchangers. Equilibrium data were described in the form of the dependence of the ratio of protein concentrations in the solid and liquid phases on the total concentration of cation counter ions. They were successfully fitted and interpreted through a stoichiometric ion-exchange model.
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