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要旨:
In the course of the last decade the interest in therapeutic monoclonal antibodies has increased continuously. Consequently an effective purification scheme is of great interest. In most cases protein A affinity chromatography is used. However, due to the high costs of the stationary phases and the potential leakage of ligands there is a trend towards other modes of operation [1]. Simulated moving bed chromatography (SMB) has been considered as an interesting alternative [2]; applications however are still far from common.
In this work we present the separation of bovine Immunoglobulin G (IgG) from three model mixtures. Differently functionalised resins for ion-exchange, hydrophobic interaction and size-exclusion chromatography were investigated systematically regarding their adsorption and retention properties for IgG. The obtained parameters were used to calculate appropriate operating conditions for the separation in SMB chromatography.
