高等学校化学学报

高等学校化学学报 ›› 1996, Vol. 17 ›› Issue (5): 667.

• 论文 •    下一篇

氧钒(Ⅳ)离子与G-肌动蛋白的相互作用

安方1, 张伯彦1, 陈宝卫2, 王夔2   

  1. 1. 张家口医学院;
    2. 南京大学化学化工学院;
    3. 北京医科大学无机化学教研室, 北京 100083
  • 收稿日期:1995-07-11 出版日期:1996-05-24 发布日期:1996-05-24
  • 通讯作者: 陈宝卫
  • 作者简介:安方,男,30岁,讲师.
  • 基金资助:

    国家自然科学基金

The Interaction of Vanadyl Ions with G-Actin

AN Fang1, ZHANG Bo-Yan1, CNEN Bao-Wei2, WANG Kui2   

  1. 1. Zhangjiakou Medical College, Zhangjiakou;
    2. School of Chemistry and chemical Technology, Nanjing University, Nanjing;
    3. Inorganic Chemistry Department, Beijing Medical University, Beijing 100083
  • Received:1995-07-11 Online:1996-05-24 Published:1996-05-24

PDF (PC)

被引次数

6

摘要： 用凝胶色谱法以及荧光光谱和CD谱研究VO2+与G-肌动蛋白的作用。结果表明,在一个G-肌动蛋白分子上有一个VO2+的强结合部位和几个弱结合位点。随VO2+与肌动蛋白的摩尔比增加,VO2+先结合在强结合位点上,使α-螺旋含量增加,蛋白质构象变得更为紧密。更多的VO2+结合在弱结合位点上,使α-螺旋含量降低,构象变得更为开放。用光散射法测定G-肌动蛋白缔合动力学,发现在低浓度VO2+影响下,VO2+和Mg2+一样,促进缔合,而在浓度高时,缔合反而受到抑制。但是都未改变线性缔合本质。结果提示VO2+与Mg2+相似,可能结合在钙的强结合部位上。

关键词: 氧钒离子, 肌动蛋白, 构象, 缔合

Abstract: The interaction of VO2+ and G-actin was studied by gel-chromatography, fluorescence and CDspectroscopies.The results revealed that for one G-actin molecule, there is one strong-binding site and several weak-binding sites for VO2+, In low molar ratio of VO2+; G-actin vanadyl ions occupy the strong-binding site at first and cause an increase of α-helix content and transformation of the conformation to a more compact one.As the molar ratio increases, vanadyl ions bind to weak-binding sites, but the α-helix content decreases and the conformation becomes rather opened.By measuring light-scattering data as the function of time, the kinetics of G-actin association was studied.In a low concentration, the VO2+ ions, like Mg2+, promote the association, but in case of higher concentration, the effect turns to be inhibitive.However, the nature of linear association is not changed.

Key words: Vanadyl ions(Vo2+), G-actin, Conformation, Association

TrendMD: