Determination of Tryptophan-Human Serum Albumin Binding from Retention data and Separation of Tryptophan Enantiomer by High Performance Liquid Chromatography

Abstract

The retention volume of a ligand, injected onto a size exclusion chromatographic column and eluted by a macromolecular complexing solution, is theoretically analysed for evaluating the binding between the solute and the macromolecule. The binding of D- and L- tryptophan to human serum albumin is given as an example, and the separation of these enantiomers is then achieved