The protein A capture step for a monoclonal antibody (mAb) product was redeveloped to increase overall performance. The process of improving and characterizing the protein A capture step – which involved changing the resin, buffer system and wash strategy – is discussed here. The motivation for this work was to improve impurity clearance. Specifically, the goal was to improve host cell protein (HCP) impurity clearance and to gain a better understanding of HCP behavior in the updated protein A affinity step. Various small scale and high-throughput studies were completed to predict conditions for maximum impurity clearance and product quality and to provide a better overall understanding of the process. The results of the small scale and high-throughput studies were used to set initial column operating parameters. Larger scale studies were completed to assess the validity of the small scale models.

Development and characterization of a protein A capture step for improved impurity clearance

249th National Meeting (2015)

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