Burghardt T P, Ando T, Borejdo J
Proc Natl Acad Sci U S A. 1983 Dec;80(24):7515-9. doi: 10.1073/pnas.80.24.7515.
The linear dichroism of iodoacetylrhodamine labels attached to the single reactive thiol groups of myosin heads was measured to determine the spatial orientation of myosin cross-bridges in single glycerinated skeletal muscle fibers. We have shown previously that in rigor the chromophoric labels are well ordered and assume an orientation nearly perpendicular to the fiber axis; in the presence of MgADP, a large fraction of probe remains well ordered but the probe attitude assumes a more slanted orientation; in relaxed muscle, the probe order is largely lost, implying a high degree of cross-bridge disorder. In this paper, we report that during isometric contraction a large fraction of the probe shows a high degree of order, suggesting the attachment of approximately equal to 65% of the cross-bridges to actin. These ordered cross-bridges have a probe attitude similar to that of the MgADP-induced static state and hence are in a mechanical state quite distinct from rigor.
通过测量附着在肌球蛋白头部单个反应性巯基上的碘乙酰罗丹明标签的线性二色性,来确定单根甘油化骨骼肌纤维中肌球蛋白横桥的空间取向。我们之前已经表明,在僵直状态下,发色团标签排列良好,其取向几乎垂直于纤维轴;在MgADP存在的情况下,大部分探针仍排列良好,但探针的姿态呈现出更倾斜的取向;在松弛的肌肉中,探针的有序性基本丧失,这意味着横桥高度无序。在本文中,我们报告在等长收缩过程中,大部分探针显示出高度的有序性,这表明约65%的横桥附着于肌动蛋白。这些有序的横桥具有与MgADP诱导的静态相似的探针姿态,因此处于与僵直状态截然不同的机械状态。