Amos L A
J Cell Biol. 1977 Mar;72(3):642-54. doi: 10.1083/jcb.72.3.642.
The arrangement of the high molecular weight proteins associated with the walls of reconstituted mammalian brain microtubules has been investigated by electron microscopy of negatively stained preparations. The images are found to be consistent with an arrangement whereby the high molecular weight molecules are spaced 12 tubulin dimers apart, i.e., 960 A, along each protofilament of the microtubule, in agreement with the relative stoichiometry of tubulin and high molecular weight protein. Molecules on neighbouring protofilaments seem to be staggered so that they give rise to a helical superlattice, which can be superimposed on the underlying tubulin lattice. In micrographs of disintegrating tubules there is some indication of lateral interactions between neighbouring high molecular weight molecules. When the microtubules are depolymerized into a mixture of short spirals and rings, the high molecular weight proteins appear to remain attached to their respective protofilaments.
通过对负染色制剂的电子显微镜观察，研究了与重构哺乳动物脑微管管壁相关的高分子量蛋白质的排列方式。发现这些图像与一种排列方式相符，即高分子量分子沿微管的每条原纤维相隔12个微管蛋白二聚体，也就是960埃，这与微管蛋白和高分子量蛋白质的相对化学计量相符。相邻原纤维上的分子似乎是交错排列的，从而形成一个螺旋超晶格，该超晶格可以叠加在底层的微管蛋白晶格上。在解体微管的显微照片中，有迹象表明相邻高分子量分子之间存在横向相互作用。当微管解聚成短螺旋和环的混合物时，高分子量蛋白质似乎仍附着在它们各自的原纤维上。
