Affinity Chromatography of Lectins

Affinity chromatography is a technique used to purify compounds, such as proteins, that have the ability to non-covalently and reversibly bind specific molecules, known as ligands. This method differs from the classical chromatography techniques in that the protein is purified on the basis of a unique biochemical property. In affinity chromatography, the ligand is covalently attached to a matrix, which must be chemically inert, porous, and have a variety of functional groups suitable for coupling with diverse ligands. Various matrices and ligands are used in affinity chromatography, depending on the protein to be purified (Voet & Voet, 1995). A particular affinity chromatography technique, which uses carbohydrate adsorbents (ligands or matrices) for purification of glycan-binding proteins or lectins, is called carbohydrate affinity chromatography.