ABSTRACT
As a sequel to the successful exploitation of affinity chromatography for the purification of solutes, quantitative affinity chromatography was developed to take advantage of the same chromatographic matrix for determination of the binding constants responsible for the biospecific adsorption and desorption of the isolated solute. Although most quantitative affinity chromatography studies have employed zonal analysis, frontal affinity chromatography is the preferred procedure from the theoretical viewpoint. In frontal affinity chromatography the solution of partitioning solute is applied to the affinity column until the elution profile contains a plateau region in which the concentrations of all reactants equal those in the solution being applied. There have been relatively few reports of completely rigorous characterization of solute–matrix interactions by frontal affinity chromatography. After characterization of the solute–matrix interaction, the next focus of attention is clearly the evaluation of the binding constant for a competing ligand interaction.
