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Updated: Aug 18, 2026

Purification and Analytics of a Monoclonal Antibody from Chinese Hamster Ovary Cells Using an Automated Microbioreactor System
Published on: May 1, 2019
Optimization of monoclonal antibody purification by ion-exchange chromatography. Application of simple methods with
Takashi Ishihara1, Shuichi Yamamotob
1Kirin Brewery Co. Ltd., Takasaki, Gunma 370-0013, Japan. t-ishihara@kirin.co.jp
Abstract:
Simple methods for the optimization of ion-exchange chromatography of proteins in our previous papers were applied to cation-exchange chromatography purification of monoclonal antibodies (Mab). We carried out linear gradient elution experiments, and obtained the data for the peak salt concentration and the peak width. From these data, the distribution coefficient as a function of salt concentration, and the height equivalent to a theoretical plate (HETP) as a function of mobile phase velocity were calculated. The optimized linear gradient elution conditions were determined based on the relationship between buffer consumption and separation time. The optimal stepwise elution conditions were determined based on the relationship between the distribution coefficient and the salt concentration.
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