Lin T I, Lambert P, Dowben R M
Biochem Biophys Res Commun. 1983 Jul 29;114(2):447-51. doi: 10.1016/0006-291x(83)90800-8.
Steady-state fluorescence anisotropy technique was used to determine the binding constant of troponin for IAEDANS-labeled tropomyosin under various conditions. In the absence of actin, Ca does not affect the binding between troponin and tropomyosin. The presence of actin greatly strengthens troponin-tropomyosin binding in the absence of Ca. However, Ca weakens troponin-tropomyosin binding by about 2.5-fold in the reconstituted filament. It is suggested that the Ca-regulated binding may serve as a molecular switch for the troponin molecule to get "on" and "off" the actin-myosin interaction site regulating muscle contraction-relaxation cycles.
采用稳态荧光偏振技术测定了不同条件下肌钙蛋白与碘乙酰胺标记的原肌球蛋白的结合常数。在没有肌动蛋白的情况下,钙离子不影响肌钙蛋白与原肌球蛋白之间的结合。在没有钙离子的情况下,肌动蛋白的存在极大地增强了肌钙蛋白与原肌球蛋白的结合。然而,在重组细丝中,钙离子使肌钙蛋白与原肌球蛋白的结合减弱约2.5倍。有人提出,钙离子调节的结合可能作为一种分子开关,使肌钙蛋白分子开启和关闭肌动蛋白-肌球蛋白相互作用位点,从而调节肌肉收缩-舒张周期。