Effect of ligand structure of stationary phase of high performance hydrophobic interaction chromatography on renaturation efficiency of GuHCl-denaturedα-chymotrypsin

The renaturation of the denaturedα-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 ofα-Chy in the order of the end ligands PEG-600<phenyl group<tetrahydrofurfuryl alcohol(THFA).