Fuchs F
Biophys J. 1978 Mar;21(3):273-7. doi: 10.1016/S0006-3495(78)85524-6.
The formation of rigor complexes between the thick and thin filaments of glycerinated rabbit psoas muscle fibers causes the fibers to bind more calcium at any given level of free calcium. I studied the maximum amount of calcium bound as a function of filament overlap under rigor conditions. Fibers stretched to zero filament overlap (sarcomere length greater than 3.8 micron) bound exactly 75% as much calcium as fibers with maximum overlap. Between these extremes a linear relationship was found between maximum bound calcium and the length of the overlap zone. The results support the hypothesis that in the intact filament lattice one of the four calcium-binding sites of troponin depends for its existence on attachment between myosin and actin. In addition, the linear relation between maximum bound calcium and filament overlap is consistent with the assumption that the cooperative effect of rigor complex formation on calcium binding is limited to the binding site in the immediate vicinity of the rigor complex.
甘油处理的兔腰大肌纤维的粗、细肌丝之间形成强直复合物,使得纤维在任何给定的游离钙水平下能结合更多的钙。我研究了在强直条件下结合钙的最大量与肌丝重叠的函数关系。拉伸至肌丝重叠为零(肌节长度大于3.8微米)的纤维结合的钙量恰好是最大重叠纤维的75%。在这两个极端情况之间,发现结合钙的最大量与重叠区长度呈线性关系。这些结果支持了这样的假说,即在完整的肌丝晶格中,肌钙蛋白的四个钙结合位点之一的存在依赖于肌球蛋白和肌动蛋白之间的附着。此外,结合钙的最大量与肌丝重叠之间的线性关系与以下假设一致,即强直复合物形成对钙结合的协同效应仅限于强直复合物紧邻区域的结合位点。