Chromatographic Framework to Determine the Enantiomer Binding Mechanism on Pepsin Protein Surface
作者： C. André , M. Thomassin , J. F. Robert , Y. C. Guillaume
DOI: 10.1365/S10337-005-0551-6
关键词: Sodium 、 Hydrophobic effect 、 High-performance liquid chromatography 、 Derivatization 、 Enthalpy 、 Enantiomer 、 Chemistry 、 Chromatography 、 Solvent 、 Selectivity
摘要: This paper describes sodium chloride salt effects on both dansyl-D,L aminoacid derivatives-pepsin protein surface association and the selectivity process. The thermodynamic functions of this enantiomer were determined. variation plots data versus concentration (x) in bulk solvent indicated a change enantiomer-pepsin mechanisms. Enthalpy-entropy compensation confirmed observation. study shows importance taking into account, electrostatic interactions hydrophobic effect order to determinate optimum conditions for enantiomeric separation chromatographic system.
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