Abstract
Ion-exchange chromatography (IEC) is one of the most popular LC separation methods. It has a higher loading capacity compared with RP-LC. Although RP-LC typically has high resolution, IEC is more compatible with proteins because the strong solvents in RP-LC can denature proteins, which is undesirable for preparative- and large-scale LC. Analytical RP-HPLC does not suffer when proteins are denatured since effluent is not fractionated any way. Thus, due to its high resolution and better reproducibility, RP-HPLC is widely used in analytical applications. SEC is good for protein stability, but its loading capacity is only a small fraction of its column volume. To elute proteins from an ion-exchange column, a gradient of salt and/or pH is required because proteins have a wide range of retentivity.
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Gu, T. (2015). Modeling of Ion-Exchange Chromatography. In: Mathematical Modeling and Scale-Up of Liquid Chromatography. Springer, Cham. https://doi.org/10.1007/978-3-319-16145-7_13
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DOI: https://doi.org/10.1007/978-3-319-16145-7_13
Publisher Name: Springer, Cham
Print ISBN: 978-3-319-16144-0
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