Abstract
Hydrophobic interaction chromatography (HIC) is one of many separation techniques that can be used to analyze proteins. The separation mechanism is based on the adsorption of the hydrophobic region of the protein to the hydrophobic ligands attached to the column in the presence of high salt. The proteins are then eluted by descending salt concentration. Here we describe the use of this HIC technique to evaluate the hydrophobicity of different monoclonal antibodies (mAbs) and to separate different heterogeneities that occur in mAb.
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Acknowledgments
The author would like to thank our colleagues in purification Bioprocess R&D for providing us with material and technical support. We gratefully thank Roxana Butoi for hydrophobicity index, Yang Wang for support of this work, and Lisa McCormick for critical reading of the manuscript.
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Rustandi, R.R. (2013). Hydrophobic Interaction Chromatography to Analyze Glycoproteins. In: Beck, A. (eds) Glycosylation Engineering of Biopharmaceuticals. Methods in Molecular Biology, vol 988. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-327-5_13
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DOI: https://doi.org/10.1007/978-1-62703-327-5_13
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Publisher Name: Humana Press, Totowa, NJ
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Online ISBN: 978-1-62703-327-5
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