Abstract
Affinity chromatography’s main achievement has been to make use of a biologically significant interaction between a macromolecule and its ligand to separate the desired component from a complex mixture. Having used this interaction to pull out the required component, it is necessary to reverse the process so that it is liberated and the adsorbent regenerated. Although this can usually be done by a non-specific method, any contaminants that have also been attracted to the adsorbent are likely to be eluted along with the desired component. Use of biospecific affinity elution, in which the interaction is displaced by inclusion of free ligand in the eluting buffer, can minimize co-elution of unwanted contaminants.
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References
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© 1992 Humana Press Inc., Totowa, NJ
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Scopes, R.K. (1992). Biospecific Affinity Elution. In: Kenney, A., Fowell, S. (eds) Practical Protein Chromatography. Methods in Molecular Biology™, vol 11. Humana Press. https://doi.org/10.1385/0-89603-213-2:209
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DOI: https://doi.org/10.1385/0-89603-213-2:209
Publisher Name: Humana Press
Print ISBN: 978-0-89603-213-2
Online ISBN: 978-1-59259-498-6
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