Analytical High-Performance Affinity Chromatography

Specific surface recognition of folded macromolecules is a recurrent and unifying theme in biology. This fact has stimulated the development of affinity chromatography as a powerful separation method for purifying biological macromolecules and small molecules, with a basic approach of attaching a known molecular interactor to an insoluble matrix and then using such a matrix to selectively absorb a sought-after molecular species, multimolecular assembly, or even cell from mixtures eluted through the affinity matrix. By the late 1960s, with the development of agarose matrix chemistry [ 1 , 2 ], the use of agar-ose-bound ligands to purify enzymes [ 3 ], and an elevated understanding of macromolecular structure in general, the explosive growth of affinity chromatography as a preparative method started in earnest (see Refs. 4 and 5 and references therein).