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BACKGROUND: In the commercial‐scale purification of immunotherapeutics, Protein A chromatography is employed routinely for its high binding capacity and selectivity. Nevertheless, matrix cost and ligand leaching issues remain and there are many alternatives such as ion‐exchange and multi‐modal resins that are less expensive. However, binding capacities are lower than Protein A owing to the co‐adsorption of protein impurities. One solution involves removing impurities before chromatography by precipitation and a potential approach presented in the literature recently employs a dual‐salt precipitation technique. The current study explores the impact of this upon the capture of an antibody fragment by a multimodal cation exchange resin....
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