Host cell protein impurities in chromatographic polishing steps for monoclonal antibody purification

摘要: Downstream purification of monoclonal antibodies (mAbs) is normally performed using a platform process that empirically tuned to optimize impurity removal for each new product. A more fundamental understanding impurities and the product itself would provide insights into rational design efficient downstream processes. This work examines chromatographic properties Chinese hamster ovary host cell protein (HCP) in non-affinity resins commonly used polishing steps antibody purification: ion-exchange, hydrophobic interaction, multimodal. Using proteomic analysis, specific HCP elute close mAb products are identified these at typical processing conditions. Additionally, interactions with profiled determine total extent association species form associative complexes under conditions encountered columns. Product co-elution were both as viable mechanisms retention tested here. relatively large sub-population was found co-elute or associate mAbs column, but only small population HCPs-including lipoprotein lipase, chrondroitin sulfate proteoglycan 4, nidogen-1, SPARC-were difficult remove across an entire process. Biotechnol. Bioeng. 2016;113: 1260-1272. © 2015 Wiley Periodicals, Inc.