Koretz J F
Biophys J. 1979 Sep;27(3):423-32. doi: 10.1016/S0006-3495(79)85226-1.
Synthetic filaments prepared from column-purified rabbit skeletal myosin by slow dialysis exhibit characteristic bipolar organization and 14-nm axial subunit spacing. Backbone substructure can be discerned in high resolution micrographs in the form of striations of 3--4-nm width and slight angular tilt from the direction of the filament axis. Filament backbone diameters vary over the population, although remaining relatively constant for a single filament. Approximately 25% of the filaments appear poorly stained and frayed, which may be due to collapse on the electron microscope grid. Optical diffraction studies reveal a 43-nm axial repeat as well as the 14.3-nm subunit repeat, indicating a structural homology with natural filaments. A model for synthetic filament aggregation is presented that is consistent with observations of backbone diameter variation, absence of bare zones, and the presence of fraying filaments.
通过缓慢透析从柱纯化兔骨骼肌肌球蛋白制备的合成细丝呈现出典型的双极组织和14纳米的轴向亚基间距。在高分辨率显微照片中，可以辨别出主链亚结构，其形式为宽度为3 - 4纳米的条纹，并与细丝轴方向有轻微的角度倾斜。细丝主链直径在群体中有所变化，尽管单根细丝保持相对恒定。大约25%的细丝染色不佳且有磨损，这可能是由于在电子显微镜网格上塌陷所致。光学衍射研究揭示了43纳米的轴向重复以及14.3纳米的亚基重复，表明与天然细丝存在结构同源性。提出了一个合成细丝聚集模型，该模型与主链直径变化、无裸露区以及磨损细丝的存在的观察结果一致。
