Small zone gel chromatography of interacting systems: theoretical and experimental evaluation of elution profiles for kinetically controlled macromolecule-ligand reactions.

A phenomenological theory of small zone gel chromatography is elaborated for kinetically controlled macromolecule-ligand interactions. Chromatography, direct binding experiments, and rate measurements are used for successful comparison of experimental behavior with theoretical elution profiles for the interaction of MAP-2 with two synthetic peptide fragments from the C-terminal moieties of alpha- and beta-tubulin subunits. The results of this study provide guidelines for interpretation of experimental small zone elution profiles of total ligand.