Activity and Structure Changes of Arginine Kinase from Shrimp Feneropenaeus chinensis Muscle in Trifluoroethanol Solutions  

作　　者：于振行 高丹 潘继承 陆捷 周海梦 

机构地区：[1]Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China [2]School of Chemical Engineering and Materials Science, Beijing Institute of Technology, Beijing 100081, China

出　　处：《Tsinghua Science and Technology》2003年第4期460-465,共6页清华大学学报（自然科学版（英文版）

基　　金：Supported by the National Key Basic Research Specific Foundation of China(No.G19990 75 6 0 7)

摘　　要：Trifluoroethanol has often been used in protein folding studies. The changes in activity and unfolding of arginine kinase from shrimp Feneropenaeus chinensis muscle during denaturation in different concentrations of trifuoroethanol were investigated using far ultraviolet circular dichroism and fluorescence emission spectra. Arginine kinase was inactivated in trifluoroethanol solutions. The tertiary and secondary structures of arginine kinase were also destroyed in the trifluoroethanol solutions. The unfolding and inactivation courses were measured and compared. Inactivation occurred prior to unfolding, which suggests that the arginine kinase active site is more easily damaged by the denaturant than the enzyme as a whole. The result also indicates that the arginine kinase active site is situated in a limited and flexible region of the enzyme molecule.Trifluoroethanol has often been used in protein folding studies. The changes in activity and unfolding of arginine kinase from shrimp Feneropenaeus chinensis muscle during denaturation in different concentrations of trifuoroethanol were investigated using far ultraviolet circular dichroism and fluorescence emission spectra. Arginine kinase was inactivated in trifluoroethanol solutions. The tertiary and secondary structures of arginine kinase were also destroyed in the trifluoroethanol solutions. The unfolding and inactivation courses were measured and compared. Inactivation occurred prior to unfolding, which suggests that the arginine kinase active site is more easily damaged by the denaturant than the enzyme as a whole. The result also indicates that the arginine kinase active site is situated in a limited and flexible region of the enzyme molecule.

关 键 词：arginine kinase TRIFLUOROETHANOL ACTIVITY UNFOLDING 

分 类 号：Q55[生物学—生物化学]