Utilizing Confocal Raman Spectroscopy To Understand Monoclonal Antibody Purification By A Strong Cation Exchanger | 18684
Journal of Analytical & Bioanalytical Techniques
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Monoclonal antibody (mAb) purification usually employs a template process, which often includes cation exchange
chromatography after the Protein A step. The mAb eluent from the Protein A column is at pH ~3-4, and should be
adjusted to have the optimal pH (~4-5) and conductivity (~2-100 mS/cm) for the subsequent cation exchange chromatography.
To obtain the optimized conditions for a mAb and a cation exchanger, the most common trial and error approach is to analyze
the loading and elution profiles of the mAb in solution state. In this presentation, a monoclonal antibody (Merck Millipore
mAb04) was loaded onto a strong cation exchanger (Fractogel EMD SO3 (M)) at pH 5 or 4 with a conductivity of 10 mS/cm
or 2 mS/cm. Confocal Raman spectroscopy was applied, for the first time, to measure protein distribution and conformational
changes in chromatographic particles. Both depend on the loading pH and conductivity. This approach therefore can help the
researcher to understand, on a very small scale using a single chromatography bead, how and why the loading conditions will
affect mAb purification by the cation exchanger at full scale.
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