高等学校化学学报 ›› 1996, Vol. 17 ›› Issue (8): 1269.

• 论文 • 上一篇    下一篇

盐酸胍对反胶束中RNase A活性的影响

黄文, 毕只初, 顾惕人   

  1. 北京航空航天大学化学教研室, 北京 100083
  • 收稿日期:1995-08-11 出版日期:1996-08-24 发布日期:1996-08-24
  • 通讯作者: 黄文,男,28岁,博士,讲师.
  • 作者简介:黄文,男,28岁,博士,讲师.

Effect of Guanidine Hydrochloride on the Activity of RNase A in DAB Reverse Micelles

HUANG Wen, BI Zhi-Chu, Gu Ti-Ren   

  1. Labarotary of Chemistry, Peking University of Aeronautics and Astronautics, Beijing 100083
  • Received:1995-08-11 Online:1996-08-24 Published:1996-08-24

摘要: 以胞嘧啶核苷酸2',3'-环单磷酸酯为底物研究了变性剂盐酸胍对十二胺丁酸盐-环己烷反胶束溶液中核糖核酸酶A活性的影响,同水溶液相比,盐酸胍对反胶束中酶活性的抑制作用很小。反胶束的大小限制了酶分子天然态构象的改变,从而保证了其活性中心的完整性。核糖核酸酶A的内源荧光研究发现,同水溶液相比,反胶束中蛋白的最大发射波长没有发生变化,但荧光偏振极化度增加,也表明了在反胶束中酶分子的运动自由度较在水溶液中有所降低。

关键词: 反胶束, 核糖核酸酶A, 盐酸胍, 酶催化活性

Abstract: The effect of guanidine hydrochloride on the activity of Bovine Pancreatic ribonuclease Asolubilized in reverse micelles formed in cyclohexane by dodecylammonium butyrate(DAB) and water has been investigated using cytidine 2',3',-phosphate as the substrate, It was noted that the enzyme entrapped in DABreverse micelles maintained more activity compared to aqueous solution at the same guanidine concentration, because protein molecule was constrained by the micellar enviroment into a conformation close to the native.Fluorescence studies showed that the degree of polarization of protein fluorescence in the micelles increased with respect to that in water which also suggested a lower mobility of the protein.

Key words: Reverse micelles, RNAse A, Guanidine hydrochloride, Enzymatic activity

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