Higashi-Fujime S
J Biochem. 1983 Nov;94(5):1539-45.
In vitro movement of fibrils composed of actin and myosin filaments purified from skeletal muscle was observed by dark field microscopy during superprecipitation at low ionic strengths at room temperature. The movement was activated by phosphorylation of light chain (LC2) of myosin. The activity of the movement was evaluated in terms of the spreading of the area where the fibrils were moving. Adenosine triphosphatase activity of actomyosin was also enhanced by phosphorylation of LC2 and was correlated with the activity of the in vitro movement.
在室温下低离子强度的超沉淀过程中，通过暗视野显微镜观察了从骨骼肌中纯化的由肌动蛋白和肌球蛋白丝组成的原纤维的体外运动。该运动由肌球蛋白轻链（LC2）的磷酸化激活。根据原纤维运动区域的扩展来评估运动活性。肌动球蛋白的三磷酸腺苷酶活性也因LC2的磷酸化而增强，并且与体外运动活性相关。
