Neuhaus J M, Wanger M, Keiser T, Wegner A
J Muscle Res Cell Motil. 1983 Oct;4(5):507-27. doi: 10.1007/BF00712112.
Actin filaments can assemble at the barbed end and disassemble simultaneously at the pointed end. A higher monomer concentration is required to balance the association of actin monomers and the dissociation of filament subunits at the pointed end than at the barbed end. This treadmilling reaction or disparity of the apparent affinity of the two ends for monomers is caused by a continuous hydrolysis of adenosine triphosphate occurring during the association of a monomer with a filament end. In this article, in vitro investigations on treadmilling are reviewed and emerging physiological implications are discussed.
肌动蛋白丝可在其带刺端组装，并同时在其尖端解聚。与带刺端相比，在尖端需要更高的单体浓度来平衡肌动蛋白单体的结合和丝状亚基的解离。这种踏车行为反应或两端对单体的表观亲和力差异是由单体与丝状末端结合过程中发生的三磷酸腺苷持续水解引起的。本文综述了关于踏车行为的体外研究，并讨论了其新出现的生理意义。
