ABSTRACT
The use of affinity chromatography as an analytical tool to detect and measure molecular interactions is well-suited to the increasing demand to study these processes in biological systems of variable size and complexity. The zonal elution approach of analytical-affinity chromatography was developed essentially in parallel with the continuous elution/frontal analysis approach. Owing largely to its simplicity of experimental design, the zonal method has become widely applicable for biochemical analysis of molecular interactions when one of the molecular partners can be immobilized with retention of interaction properties. Since the method can be used to analyze very small amounts of the mobile interactant, it has important applicability as a micromethod for biochemical analysis of a vast array of biologically active molecules being discovered and isolated but available in only small amounts. The association of various organic acids with serum albumin is an excellent example of the case of multiple-independent binding sites for a ligand on the surface of a protein.
