Abstract
The principle of immunoaffinity or immunoadsorption chromatography is based on the highly specific interaction of an antigen with its antibody (1). Immunoaffinity chromatography is a specialized form of affinity chromatography and, as such, utilizes an antibody or antibody fragment as a ligand immobilized onto a solid support matrix in a manner that retains its binding capacity. Although the technique includes the separation of antibodies using immobilized antigens (2–4), it is more commonly performed for the identification, quantification, or purification of antigens (see Note 1 and refs. 5 and 6). The crude extract is pumped through the column and the unbound material washed clear prior to elution of the retained antigen by alterations to the mobile-phase conditions that weaken the antibody-antigen interaction.
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© 2004 Humana Press Inc., Totowa, NJ
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Cutler, P. (2004). Immunoaffinity Chromatography. In: Cutler, P. (eds) Protein Purification Protocols. Methods in Molecular Biology, vol 244. Humana Press. https://doi.org/10.1385/1-59259-655-X:167
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DOI: https://doi.org/10.1385/1-59259-655-X:167
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