Abstract
The unique high specificity of antibodies, both polyclonal and monoclonal, makes them extremely valuable tools for rapid, selective purification of antigens. In principle, the antibody immobilized on a column support is used to selectively adsorb antigen from a mixture containing many other proteins (1,2). The other proteins, for which the antibody has no affinity, may be washed away, and the purified antigen then eluted from the immunoadsorbent. In order to dissociate the antigen from its high affinity antibody, the conditions for elution are necessarily extreme (1–3) and thus must be carefully chosen to permit isolation of active protein.
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References
Livingston, D. M. (1974) Immunoaffinity Chromatography of Proteins in Methods in Enzymology (eds. W. B. Jakoby and M. Wilchek) vol. 34, pp. 723–731, Academic Press, New York.
Dalchau, R., and Fabre, J. W. (1982) The Purification of Antigens and Other Studies with Monoclonal Antibody Affinity Columns: the Complimentary New Dimension of Monoclonal Antibodies in Monoclonal Antibodies in Clinical Medicine (eds. A. J. McMichael and J. W. Fabre) pp. 519–556, Academic Press, New York.
Affinity Chromatography. Principles and Methods. Technical brochure available from Pharmacia Fine Chemicals, Sweden.
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© 1984 Humana Press
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Mayes, E.L.V. (1984). Immunoaffinity Purification of Protein Antigens. In: Walker, J.M. (eds) Proteins. Methods in Molecular Biology™, vol 1. Humana Press. https://doi.org/10.1385/0-89603-062-8:13
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DOI: https://doi.org/10.1385/0-89603-062-8:13
Publisher Name: Humana Press
Print ISBN: 978-0-89603-062-6
Online ISBN: 978-1-59259-488-7
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