Hage D S
Department of Chemistry, University of Nebraska--Lincoln, 68588-0304, USA.
J Chromatogr A. 2001 Jan 12;906(1-2):459-81. doi: 10.1016/s0021-9673(00)00957-2.
Protein interactions are important in determining the transport, metabolism and/or activity of many chiral compounds within the body. This review examines data that have been obtained on these interactions by various chromatographic and electrophoretic methods, especially those based on either high-performance liquid chromatography or capillary electrophoresis. Zonal elution, frontal analysis and vacancy methods are each considered, as are approaches that employ either soluble or immobilized proteins. There are a variety of different items that can be learned about a solute-protein system through these techniques. This includes information on the binding constants and number of binding sites for a solute-protein system, as well as the thermodynamic parameters, rate constants, interaction forces and binding site structure for the protein and solute. Numerous examples are provided throughout this review, as taken from the literature and from work performed within the author's laboratory.
