Maruyama K, Abe S, Ishii T
J Biochem. 1975 Jan 1;77(1?):131-6.
Beta-Actinin, a regulatory protein of muscle, greatly decreased the dynamic rigidity modulus of an acto-heavy meromyosin solution. However, it was found that the mechanical mixing procedure used resulted in fragmentation of the decorated F-actin particles and beta-actinin inhibited the reassociation of the fragmented particles. This was the reason for the decrease of the dynamic rigidity modulus of the acto-heavy meromyosin complex caused by beta-actinin. When beta-actinin was added to the acto-heavy meromyosin solution in the presence of ATP, it did not affect the visco-elasticity. F-actin particles dissociated by ATP were not fragmented by the mixing procedure, which was responsible for the apparent inactivation of beta-actinin in the presence of ATP.
β-肌动蛋白是一种肌肉调节蛋白，它极大地降低了肌动蛋白-重酶解肌球蛋白溶液的动态刚性模量。然而，研究发现，所采用的机械混合程序导致了被标记的F-肌动蛋白颗粒发生碎片化，并且β-肌动蛋白抑制了碎片化颗粒的重新结合。这就是β-肌动蛋白导致肌动蛋白-重酶解肌球蛋白复合物动态刚性模量降低的原因。当在ATP存在的情况下将β-肌动蛋白添加到肌动蛋白-重酶解肌球蛋白溶液中时，它不会影响粘弹性。被ATP解离的F-肌动蛋白颗粒不会因混合程序而碎片化，这就是在ATP存在时β-肌动蛋白明显失活的原因。
