肌球蛋白头部的内部运动：ADP和ATP的作用
Internal motions in myosin head: effect of ADP and ATP.
作者信息
Belagyi J, Lörinczy D
机构信息
Central Research Laboratory, University Medical School, Pécs, Hungary.
出版信息
Biochem Biophys Res Commun. 1996 Feb 27;219(3):936-40. doi: 10.1006/bbrc.1996.0336.
Internal flexibility of myosin heads in glycerinated muscle fibres in the presence of MgADP plus orthovanadate and after addition of Ca-ATP was studied using an isothiocyanate-based spin label attached to the reactive sulfhydryl sites of myosin. The spin labels were immobilized on the microsecond time scale and exhibited significant orientational order in rigor. In AM+.ADP.V(i) state a smaller fraction of ordered population was found showing distinct orientation from rigor; the larger population of heads was in dynamically disordered state. This new ordered population of heads was detected even in contracting fibres.
利用附着在肌球蛋白反应性巯基位点上的异硫氰酸酯基自旋标记，研究了在存在MgADP加原钒酸盐的情况下以及添加Ca-ATP后甘油化肌纤维中肌球蛋白头部的内部柔韧性。自旋标记在微秒时间尺度上固定，并在僵直状态下表现出显著的取向有序性。在AM +.ADP.V(i)状态下，发现有序群体的比例较小，与僵直状态有明显不同的取向；较大比例的头部处于动态无序状态。即使在收缩的纤维中也能检测到这种新的有序头部群体。
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