ABSTRACT
Affinity chromatography is a versatile method for the purification of various biological molecules, including enzymes, hormones, antibodies, and receptors [1-4]. In 1987, a technique known as receptor-affinity chromatography (RAC) was developed as an alternative to immunoaffinity chromatography [5]. Receptor-affinity chromatography makes use of the reversible interactions that occur between a matrix-bound receptor and a soluble protein target. In theory, receptor-affinity adsorbents are unique in their ability to bind only a fully active biomolecule in its native conformation. In contrast, immunoaffinity adsorbents often lack such specificity and bind to any form of a target that possesses the required epitope, irrespective of the target’s degree of renaturation or biological activity. This difference has been illustrated in the use of both methods to purify recombinant human interleukin-2 [5,6].
