Abstract
Immunoaffinity chromatography offers to the chromatographer the exquisite specificity of the antibody’s complementarity determining regions (CDRs), or hypervariable regions (1,2). These highly selective loops on the antibody surface capture an antigen with high affinity, while having little interaction with impurities that may also be present. When appropriately immobilized, an antibody retains its affinity for its antigen while being held covalently on the chromatographic support. With appropriate wash conditions, 1000-fold or higher impurity clearances are common. With appropriate elution conditions, 90% or more of the activity present in the chromatographic injection may be recovered in the elution peak. And, quite frequently, it is possible to regenerate the immunoaffinity column to allow its use for 100 or more cycles depending on the impurity levels in the injection.
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Gallant, S.R. (2004). Immunoaffinity Chromatography of Proteins. In: Aguilar, MI. (eds) HPLC of Peptides and Proteins. Methods in Molecular Biology™, vol 251. Springer, Totowa, NJ. https://doi.org/10.1385/1-59259-742-4:103
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DOI: https://doi.org/10.1385/1-59259-742-4:103
Publisher Name: Springer, Totowa, NJ
Print ISBN: 978-0-89603-977-3
Online ISBN: 978-1-59259-742-0
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