摘要
The activity and conformation of ribonuclerse A (RNaseA) solubilized in cyclohexane via dodecylammonium butyrate(DAB) reverse Ancelles were investigated. The activity of RNaseA was studied using the cytidine 2’,3’-phosphate as the substrate, and it was found that kcat increases significantly with respect to that in water attended by an increased Km·FT-IR spectra of RNaseA in reverse Ancellax solution were investigated as a function of w0(= [H2O]/ [DAB]), and it was noted that the structure of RNaseA became looser in reverse micelles campared to that in aqueous solution. The relation between activity and conformation was discussed.
The activity and conformation of ribonuclerse A (RNaseA) solubilized in cyclohexane via dodecylammonium butyrate(DAB) reverse Ancelles were investigated. The activity of RNaseA was studied using the cytidine 2',3'-phosphate as the substrate, and it was found that kcat increases significantly with respect to that in water attended by an increased Km·FT-IR spectra of RNaseA in reverse Ancellax solution were investigated as a function of w0(= [H2O]/ [DAB]), and it was noted that the structure of RNaseA became looser in reverse micelles campared to that in aqueous solution. The relation between activity and conformation was discussed.
出处
《物理化学学报》
SCIE
CAS
CSCD
北大核心
1996年第4期353-356,共4页
Acta Physico-Chimica Sinica
关键词
核糖核酸酶
反胶束
构象
DAB
环己烷
活性
Bovine pancreatic ribonuclease A(RNaseA), Dodecylammonium butyrate,Reverse micelle, FT-IR spectra, Surfactant
