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        Purification of Antibodies Using Affinity Chromatography

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        730
        The effectiveness of affinity chromatography relies on the ability of a molecule in solution to recognize specifically an immobilized ligand (1 3 ). This type of separation, unlike other chromatographic methods, uses the intrinsic biological activity of a molecule to bind to a substrate, hapten, or antigen. Principles of matrix selection, gel preparation, and coupling of ligands have been reviewed extensively by Ostrove (2 ). Antibody affinity chromatography has been employed to isolate antigen-specific antibodies (antibodies raised against a particular protein), hapten-specific antibodies (antipeptide antibodies, antiphosphotyrosine antibodies, anti-TNP antibodies), or species-specific immunoglobulins, or to separate crossreacting immunoglobulins from the antibody of interest (3 7 ). Several types of affinity matrices are commercially available. The most common matrix for coupling of molecules is CNBr-activated Sepharose (Pharmacia-LKB, Piscataway, NJ) (8 ). It is ideally suited for affinity chromatography for several reasons. Sepharose exhibits little nonspecific protein adsorption, is stable over a wide pH range, and can be used with denaturants or detergents. Because of its large pore size (exclusion limit of 2 � 107 ), the matrix has a high capacity and, therefore, allows for internal ligand attachment.
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