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
依据欧洲电信标准协会(ETSI)提出的ETSI EN 300 401标准,设计了一种高性能DAB接收终端RF接收模块的设计方法,实现了DAB信号稳定同步和接收,达到了高灵敏度和低功耗,在移动速度达到200 km/h时能够稳定接收。该设计方法已经用于批量生产的...依据欧洲电信标准协会(ETSI)提出的ETSI EN 300 401标准,设计了一种高性能DAB接收终端RF接收模块的设计方法,实现了DAB信号稳定同步和接收,达到了高灵敏度和低功耗,在移动速度达到200 km/h时能够稳定接收。该设计方法已经用于批量生产的DAB接收终端中。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.
