Abstract
The renaturation of the denatured α -chymotrypsin (α-Chy) with 1.7 mol · L−1 guanidine hydrochloride (GuHCl) 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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