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研究了核糖核酸酶Ａ（ＲＮａｓｅＡ）在丁酸十二铵（ＤＡＢ）－环己烷反胶束溶液中催化水解胞苷２，３－环单磷酸酯的动力学，数据符合Ｍｉｃｈａｅｌｉｓ－Ｍｅｎｔｅｎ酶催化机理．以ｋｃａｔ／Ｋｍ表示酶催化活性时，ＲＮａｓｅＡ在反胶束溶液中的催化活性是在水溶液中的１４～３０倍．无论是固定ＤＡＢ浓度还是固定Ｈ２Ｏ与ＤＡＢ浓度之比，随增溶水量的增加，ｋｃａｔ／Ｋｍ呈下降趋势．
The kinetics of enzymatic hydrolysis of cytidine 2, 3-cyclic monophosphate catalyzed by RNaseA in DAB-cyclohexane reverse micellar solution was studied. The data were in accordance with Michaelis-Menten Enzyme catalysis mechanism. The catalytic activity of RNaseA in reverse micellar solution is 14 to 30 times higher than that in aqueous solution when kcat / Km indicates the catalytic activity of the enzyme. Both the fixed DAB concentration and the fixed H 2 O / DAB concentration ratio, kcat / Km showed a decreasing trend with the increase of solubilized water.