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High-Performance Affinity Chromatography for Protein Separation and Purification

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Practical Protein Chromatography

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 11))

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Abstract

Affinity chromatography (1,2), the most powerful of all protein-fractionation techniques, relies on the formation of reversible specific complexes between a ligand immobilized on an insoluble polymer support, termed affinity adsorbent, and the species to be isolated free in solution. The modern support materials (natural, synthetic, or inorganic), consist of macroporous hydrophilic beaded particles, usually bearing free hydroxyl groups available for ligand immobilization. When the support is made of noncompressible particles of small diameter (e.g., 5–20 µm) and narrow size distribution (e.g., 0.2–2 µm) the technique is termed high-performance affinity chromatography (HPAC) (35).

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© 1992 Humana Press Inc., Totowa, NJ

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Clonis, Y.D. (1992). High-Performance Affinity Chromatography for Protein Separation and Purification. In: Kenney, A., Fowell, S. (eds) Practical Protein Chromatography. Methods in Molecular Biology™, vol 11. Humana Press. https://doi.org/10.1385/0-89603-213-2:105

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  • DOI: https://doi.org/10.1385/0-89603-213-2:105

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-213-2

  • Online ISBN: 978-1-59259-498-6

  • eBook Packages: Springer Protocols

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