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Related Concept Videos

Ion-Exchange Chromatography01:09

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Ion-exchange chromatography, or IEC, is a technique for separating ions based on their affinity for the stationary phase. The stationary phase is a cross-linked polymer resin with covalently attached ionic functional groups. The functional groups can be either positively charged (cation exchangers) or negatively charged (anion exchangers). A cation exchanger consists of a polymeric anion and active cations, while an anion exchanger is a polymeric cation with active anions. The choice of...
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Affinity chromatography is a powerful technique extensively utilized for separating and purifying specific biomolecules from complex mixtures. It capitalizes on the highly selective binding between an analyte and its counterpart, such as antibody-antigen interactions. The counterpart is immobilized on the stationary phase, forming an affinity column. The stationary phase typically consists of solid support, such as agarose or porous glass beads, immobilizing the affinity ligand. The mobile...
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Immunoprecipitation, or IP, is a widely used technique that employs protein-antibody interactions to isolate proteins or protein complexes in their native state for studying protein-protein interactions, quaternary structures, or supramolecular complexes. Various modifications of the technique, including chromatin IP, cross-linking IP, and fluorescence IP, are commonly used.
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The stability and compatibility of column material with samples are crucial for efficient purification in chromatographic techniques. Various operating parameters such as pH, temperature, or solvent affect the packing of the column material, thereby determining the purification efficiency. The choice of column material also plays an essential role in deciding the operating parameters and can be modified based on the proteins that need to be purified.
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Related Experiment Video

Updated: Mar 27, 2026

Purification and Analytics of a Monoclonal Antibody from Chinese Hamster Ovary Cells Using an Automated Microbioreactor System
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Multimodal charge-induction chromatography for antibody purification.

Hong-Fei Tong1, Dong-Qiang Lin1, Wen-Ning Chu1

  • 1Key Laboratory of Biomass Chemical Engineering of Ministry of Education, College of Chemical and Biological Engineering, Zhejiang University, Hangzhou 310027, China.

Journal of Chromatography. A
|January 10, 2016
PubMed
Summary

A novel multimodal charge-induction chromatography (MCIC) using the W-ABI ligand enhances antibody purification. This method offers high capacity and selectivity, presenting a cost-effective alternative to Protein A for antibody purification.

Keywords:
AntibodyHydrophobic charge-induction chromatographyLigand designPurification

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Last Updated: Mar 27, 2026

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Area of Science:

  • Biochemistry
  • Chromatography
  • Protein Purification

Background:

  • Hydrophobic charge-induction chromatography (HCIC) offers high capacity and salt tolerance but can be improved in binding specificity.
  • Multimodal molecular interactions can enhance chromatographic separation selectivity.

Purpose of the Study:

  • To develop a novel multimodal charge-induction chromatography (MCIC) system with improved binding specificity for antibody purification.
  • To evaluate the performance of a new W-ABI ligand for IgG adsorption and elution.

Main Methods:

  • Design and synthesis of the W-ABI ligand, combining tryptophan and 5-amino-benzimidazole functionalities.
  • Coupling of the W-ABI ligand onto agarose gel for chromatographic applications.
  • Investigation of IgG adsorption behavior, including capacity and impact of flow rate.
  • Evaluation of elution efficiency at acidic pH and assessment of purity and recovery in separation cases.

Main Results:

  • The W-ABI ligand demonstrated high affinity for IgG with a saturated adsorption capacity of 70.4 mg/ml at pH 7.
  • Flow rate had minimal impact on dynamic binding capacity.
  • Efficient elution of IgG was achieved at mild acidic pH with high recovery rates.
  • Successful purification of IgG from albumin and monoclonal antibodies from cell culture supernatant with high purity.

Conclusions:

  • The developed MCIC system with the W-ABI ligand expands upon HCIC, offering enhanced adsorption selectivity.
  • This approach provides a potential cost-effective alternative to Protein A-based methods for antibody purification.