Binding Capacity for Protein A Chromatography

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Ghose et al. (2014) explain that understanding the process of purification of monoclonal antibodies (mAbs) via analyzing the affinity of Protein A chromatography aids the scientists in establishing the mAbs in mammalian cells. This process is utilized to yield results that are highly reduced and vigorously purified. However, the past decade showed challenges in purifying a large volume of cell culture titers. In association with this, the researchers investigated the processes and factors that can maximize the binding capacity for protein chromatography (p. 1335).
The study analyzed mAbs A to E from the ovary of a Chinese Hamster, which produced recombinant humanized IgG1 Abs. They diluted a drug substance and used this as a loading material to mimic a typical cell culture fluid. For the experiment proper, the researchers utilized the MabSelect SuRe LX. Initially, the researchers estimated the dynamic binding capacity (DBC) to ensure minimum variance and a minimum margin of error (MOE), limited to +/-5. This was followed by creating the central composite design (CCD) to augment the dual flow loading on the resin used. Lastly, the Protein A experiment ensued (Ghose et al., 1336-1337).
The study focuses on Protein A, but initially, the researchers compared the results of the DBC of mAbs A and B with MabSelect Sure, the control resin, versus MabSelect Sure LX, the experimental resin, under similar conditions of chromatography. The former resin is the predecessor of the latter. The results revealed that MabSelect Sure LX has a higher e...