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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
[One-step purification of monoclonal antibody against gp130 by cation exchange liquid chromatography]
Hong-bing Ma1, Yu-mei Zhuang, Ying Xu
1Institute of Medical Biotechnology, Suzhou University, Suzhou 215007, China. ma_hongbing@yahoo.com.cn
Aim:
To develop a one-step purification method of anti-gp130 monoclonal antibody (mAb) B-S12 from mouse ascites.
Methods:
After filtrated by centrifugation, the ascites sample was loaded on a cation exchange column and purified by using ion-strength gradient elution buffer. The effects of pH of the loading buffer and ion strength gradients of the elution buffer on the purity of antibody obtained were investigated. The antibody's biological activity was tested by MTT colorimetry.
Results:
It was shown that the mAb B-S12 with a purity of over 90% could be achieved by using 20 mmol/L HEPES buffer (pH 4.0) as loading buffer and 0-1.0 mol/L NaCl as elution buffer. The total recovery rate of the mAb was 52%. The purified antibody could stimulate the proliferation of XG-2 cell line.
Conclusion:
The established one-step purification method was simple and suitable for purification of mAb B-S12.
