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’-p...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.展开更多
The enzymetic activity of RNaseA solubilized in reverse micelles formed in cyclohexane by dodecylammonium butyrate(DAB) and water has been investigated with the use of cytidine 2’, 3’-phosphate as the substrate. In ...The enzymetic activity of RNaseA solubilized in reverse micelles formed in cyclohexane by dodecylammonium butyrate(DAB) and water has been investigated with the use of cytidine 2’, 3’-phosphate as the substrate. In the investigated concentration range, RNaseA exhibited a "superactivity" in the DAB reverse micelle.展开更多
文摘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.
文摘The enzymetic activity of RNaseA solubilized in reverse micelles formed in cyclohexane by dodecylammonium butyrate(DAB) and water has been investigated with the use of cytidine 2’, 3’-phosphate as the substrate. In the investigated concentration range, RNaseA exhibited a "superactivity" in the DAB reverse micelle.
