A Novel Method for Diminishing Protein Aggregation during Denatuaration Process  

作　　者：Ye Hua SHEN Quan BAI Yang Jun ZHANG Yin Mao WEI Hai Bo WANG Xing Du GENG 

机构地区：[1]Institute of Modern Separation Science, The Key Lab of Modem Separation Science in Shaanxi Province, Northwest University, Xi＇an 710069

出　　处：《Chinese Chemical Letters》2006年第3期395-398,共4页中国化学快报（英文版）

基　　金：supported by the National Natural Science Foundation of China(No.39880003 and 20175016).

摘　　要：The addition of packing material for high performance hydrophobic interaction chromatograghy （HPHIC） into the denaturant solution to prevent, or depress protein aggregation in the denatuaration process is presented. The renaturation of α-chymotrypsin （α-Chy） denatured with guanidine hydrochloride （GuHCl） solution indicated that renaturation efficiency can be enhanced from 36.1% to 59.0% by this new method. The structure of the ligand linking of HPHIC packings is also important for the protein renaturation.The addition of packing material for high performance hydrophobic interaction chromatograghy （HPHIC） into the denaturant solution to prevent, or depress protein aggregation in the denatuaration process is presented. The renaturation of α-chymotrypsin （α-Chy） denatured with guanidine hydrochloride （GuHCl） solution indicated that renaturation efficiency can be enhanced from 36.1% to 59.0% by this new method. The structure of the ligand linking of HPHIC packings is also important for the protein renaturation.

关 键 词：Protein renaturation Α-CHYMOTRYPSIN hydrophobic interaction chromatography 

分 类 号：Q51[生物学—生物化学] Q503