Shimizu H, Yano M
J Biochem. 1978 Nov;84(5):1093-102. doi: 10.1093/oxfordjournals.jbchem.a132223.
The order--disorder phase transition in the chemo-mechanical process in our streaming system, which was reported in the preceding paper [Yano, M. & Shimizu, H., J. Biochem, 84, 1087--1092], was studied in detail. Starting from the hypothesis that a new type of cooperativity, dynamic cooperativity, is present in the elementary cycles of the chemo-mechanical conversion, quantitative and consistent agreement was obtained between the theoretical and experimental data on the temperature dependences of the streaming velocity and the ATPase activity, including the presence of the phase transition. The hypothesis was also supported by observations of the temperature dependence of the ATPase activity in resisted streaming. The physical and physiological significance of dynamic cooperativity is considered. It is shown that dynamic cooperativity arises in actomyosin system which have a polarized arrangement of F-actin by directed streaming of the solution, because the rate of the elementary cycle can be accelerated by the streaming. Furthermore, dynamic cooperativity is the key mechanism of self-organization of a dynamical order such that in ordered motions, and is one of the essential conditions for the direct conversion of the chemical energy of ATP to the mechanical energy of ordered and directed motion.
在前一篇论文[矢野,M. & 清水,H.,《生物化学杂志》,84,1087 - 1092]中报道的我们的流动系统中化学机械过程的有序 - 无序相变,在此进行了详细研究。从化学机械转化的基本循环中存在一种新型协同性即动态协同性这一假设出发,在流动速度和ATP酶活性的温度依赖性方面,包括相变的存在,理论数据与实验数据之间获得了定量且一致的吻合。在受阻流动中对ATP酶活性的温度依赖性的观察也支持了该假设。文中考虑了动态协同性的物理和生理意义。结果表明,动态协同性出现在肌动球蛋白系统中,该系统通过溶液的定向流动使F - 肌动蛋白呈极化排列,因为流动可加速基本循环的速率。此外,动态协同性是动态秩序自组织的关键机制,使得在有序运动中,并且是ATP化学能直接转化为有序定向运动机械能的必要条件之一。