Abstract

The nature and effects of bonded phases and analytical conditions on protein retention in high-performance hydrophobic-interaction chromatography (HIC) were investigated. Silica-based packing materials with different surface hydrophobicity were prepared and evaluated with respect to protein retention. The contact of proteins with the hydrophobic stationary phases caused conformational changes of proteins to some extent, but the extent of these changes was dependent on the hydrophobicity of the stationary phases, column temperature and the proteins themselves. Thermal behavior of some proteins in HIC on these phases is also shown.

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