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Affinity Chromatography

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Protein Purification Protocols

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 59))

Abstract

Affinity chromatography is a method of selectively and reversibly binding proteins to a solid support matrix based on the exploitation of known biological affinities between molecules. The interaction between the target protein and the matrix is not based on general properties, such as the isoelectric point (pI) or hydrophobicity, which are more commonly used in adsorption chromatography, but on individual structural properties, such as the interaction of antibodies with antigens, enzymes with substrate analogs, nucleic acids with binding proteins, and hormones with receptors. In order to exploit the interaction for the purposes of purification, one of the components, the ligand, must be immobilized onto a solid matrix in a manner that renders it stable and active. Once produced, the matrix can be used to purify its specific target from a suitable biological extract (1).

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© 1996 Humana Press Inc.

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Cutler, P. (1996). Affinity Chromatography. In: Doonan, S. (eds) Protein Purification Protocols. Methods in Molecular Biology™, vol 59. Humana Press. https://doi.org/10.1385/0-89603-336-8:157

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  • DOI: https://doi.org/10.1385/0-89603-336-8:157

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-336-8

  • Online ISBN: 978-1-59259-545-7

  • eBook Packages: Springer Protocols

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