高等学校化学学报 ›› 1998, Vol. 19 ›› Issue (3): 433.

• 论文 • 上一篇    下一篇

核糖核酸酶A在丁酸十二铵-环己烷反胶束溶液中的催化动力学

郭红, 黄文, 顾惕人   

  1. 北京航空航天大学化学教研室, 北京, 100083
  • 收稿日期:1996-12-06 出版日期:1998-03-24 发布日期:1998-03-24
  • 通讯作者: 郭红
  • 作者简介:郭红,女,38岁,副教授.
  • 基金资助:

    航空高等院校自选科研基金资助课题.

Kinetics of Catalysis by Ribonuclease A in Reverse Micelles Formed by Dodecylammonium Butyrate and Water in Cyclohexane

GUO Hong, HUANG Wen, GU Ti-Ren   

  1. Laboratory of Chemistry, Beijing University of Aeronautics and Astronautics, Beijing, 100083
  • Received:1996-12-06 Online:1998-03-24 Published:1998-03-24

摘要: 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,Rnase A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.

关键词: 核糖核酸酶A, 丁酸十二铵, 反胶束, Michaelis-Menten公式, 酶催化动力学

Abstract: The kinetics of hydrolysis of cytidine 2',3'-cyclic phosphate(CP) catalyzed by ribonuclease A(RNase A) solubilized in reverse micelles formed by dodecylammonium butyrate(DAB) in cyclohexane has been investigated. The results show that the Michaelis-Menten law can be applied to DAB-cyclohexane reverse micellar solutions as well as to aqueous solutions. The enzyme efficiency(expressed in terms of the ratio kcat/km) of RN ase A solubilized in DAB cyclohexane reverse micellar solutions is 14—30 times of that in aqueous solution. Under the conditions at constant concentration of DAB as well as at constant molecular ratio of H2O and DAB, the enzymetic activity of RN ase A in reverse micellar solutions decreases as the water content is increased. The results were explained briefly in terms of the changes in the conformation of the enzyme as well as in the concentrations of the enzyme and the substrate in inner water phase.

Key words: Ribonuclease A, Dodecylammonium butyrate, Reverse micelle, Michaelis-Menten law, Catalysis kinetics of enzyme

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