Kinetics of Angiotensin I alteration of conformation on different hydrophobic interaction chromatographic surfaces
作者： Patrícia P. Aguilar , Catherine A. Nunes , José F. Cascalheira , Ana C. Dias-Cabral
DOI: 10.1016/J.CHROMA.2011.09.024
关键词:
摘要: In the present study, Angiotensin I (Ang I) will be used as model peptide to assess on-column alteration of conformation phenomena. Adsorptive behavior Ang on various commercial hydrophobic interaction surfaces (Butyl, Octyl and Phenyl – Sepharose), under different conditions, was investigated. order calculate cis–trans isomerization rate constants stationary phase's surface, first second moments proline elution profiles were determined. The activation energies for process Butyl Sepharose also calculated. Results suggest that phase catalyzes catalysis is dependent ligand nature.
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