Separation and purification of anti-HER2 monoclonal antibody with hydrophobic charge-induction chromatography

LI Jing; LIN Dongqiang; TONG Hongfei; YAO Shanjing; YE Shuaidong; CUI Jiayou

doi:10.3969/j.issn.0438-1157.2014.10.025

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Separation and purification of anti-HER2 monoclonal antibody with hydrophobic charge-induction chromatography

更新时间：2025-12-10

- Separation and purification of anti-HER2 monoclonal antibody with hydrophobic charge-induction chromatography
- CIESC Journal Issue 10, Pages: 3931-3937(2014)
- 作者机构：
  
  1. 生物质化工教育部重点实验室, 浙江大学化学工程与生物工程学系,浙江,杭州,310027
  2. 杭州安瑞普生物制品研究有限公司,浙江,杭州,310018
- 作者简介：
- 基金信息：
- DOI：10.3969/j.issn.0438-1157.2014.10.025
  CLC： Q028.8
- Online First：05 October 2014，
  
  Published：05 October 2014
- 稿件说明：
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LI Jing, LIN Dongqiang, TONG Hongfei, et al. Separation and purification of anti-HER2 monoclonal antibody with hydrophobic charge-induction chromatography[J]. CIESC Journal, 2014, (10): 3931-3937.
DOI：

LI Jing, LIN Dongqiang, TONG Hongfei, et al. Separation and purification of anti-HER2 monoclonal antibody with hydrophobic charge-induction chromatography[J]. CIESC Journal, 2014, (10): 3931-3937. DOI： 10.3969/j.issn.0438-1157.2014.10.025.

摘要

采用疏水性电荷诱导色谱（HCIC）新型生物分离方法，从CHO细胞培养液中高效分离抗HER2单克隆抗体（单抗）。选用典型HCIC介质MEP HyperCel，考察了细胞培养液中单抗稳定性，比较了不同pH下MEP HyperCel介质对抗HER2单抗的吸附性能，发现pH6～9范围内吸附容量均较高，酸性条件下吸附容量显著下降。进一步考察了抗HER2单抗的动态吸附载量，优化了上样和洗脱条件，确定了合适的分离条件，实现了细胞培养液中高效分离单抗，纯度达到94.6%，收率约0.1 mg·（ml料液）-1。结果表明，HCIC从哺乳动物细胞培养液中分离单抗是切实可行的，为单抗分离提供了新思路。

Abstract

Hydrophobic charge-induction chromatography (HCIC) is a new technology for biomolecule separation. In the present work HCIC was used to separate monoclonal antibody (mAb) anti-HER2 from Chinese Hamster ovary (CHO) cell culture broth with typical HCIC resin

MEP HyperCel. The stability of anti-HER2 mAb in cell culture broth was investigated firstly

and the adsorption of anti-HER2 mAb onto MEP HyperCel at different pH was compared. The adsorption capacities were high at the range of pH 6-9

but decreased significantly under acidic condition. The dynamic binding capacity of anti-HER2 mAb was determined with a packed bed

and the loading and elution conditions were optimized. The suitable separation conditions were obtained

and the purity of mAb could reach 94.6% with the yield of 0.1 mg·(ml broth)-1. It is feasible to separate mAb from mammalian cell culture broth with HCIC.

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