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Immunoaffinity chromatography (IAC) has long been regarded as a highly specific method for the purification of biological agents. In this technique, a chromatographic column is used that contains antibodies or antibody-related reagents as the stationary phase. The high selectivity of antibodies in their interactions with other molecules, and the ability to produce antibodies against a wide range of solutes, has made IAC popular as a tool for the purification of biomolecules like hormones, peptides, enzymes, recombinant proteins, receptors, viruses, and subcellular components (
1
–
8
). In recent years, the high selectivity of IAC has also made it appealing as a means for developing a variety of specific analytical methods (
3
,
9
,
10
). An important item to consider in the development of any IAC method is the technique used for coupling the antibodies to the chromatographic support material. One common approach