Effect of ligand structure of stationary phase of high per-formance hydrophobic interaction chromatography on re-naturation efficiency of GuHCl-denatured α-chymotrypsin |
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Authors: | SHEN Yehua WANG Haibo BAI Quan GENG Xindu |
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Abstract: | The renaturation of the denatured α-chymotrypsin (α-Chy) with 1.7 mol · L-1 guanidine hydrochloride (GuHCI) by three kinds of stationary phase of high performance hydrophobic interaction chromatography (STHIC) with a comparable hydrophobicity but different ligand structures was investigated. The obtained result indicates that the ligand structures of the three STHIC contribute to the renaturation efficiency of α-Chy in the order of the end ligands PEG-600< phenyl group < tetrahydrofurfuryl alcohol (THFA). |
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Keywords: | protein refolding renaturation α-chymotrypsin high performance hydrophobic interaction chromatography stationary phase |
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