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

作　　者：SHEN Yehua WANG Haibo BAI Quan GENG Xindu 

机构地区：[1]Institute of Modern Separation Science,Shaanxi Key Laboratory of Modern Separation Science,Northwest University,Xi'an 710069,China

出　　处：《Science China Chemistry》2005年第z1期33-36,共4页中国科学(化学英文版)

基　　金：supported by the National Natu-ral Science Foundation of China(Grant Nos.39880003&20175016).

摘　　要：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).

关 键 词：protein refolding RENATURATION Α-CHYMOTRYPSIN high performance hydrophobic interaction chromatography stationary phase 

分 类 号：N[自然科学总论]