Chem. J. Chinese Universities ›› 1996, Vol. 17 ›› Issue (5): 667.

• Articles •     Next Articles

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

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

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