The myosin filament. VII Changes in internal structure along the length of the filament.
The myosin filament. VII Changes in internal structure along the length of the filament.
复制标题
肌球蛋白丝。
DOI：
10.1016/0022-2836(81)90213-8
复制
发表时间：
1981
影响因子：
5.6
通讯作者：
Stewart,M
中科院分区：
文献类型：
--
作者：
Pepe,FA;Ashton,FT;Dowben,P;Stewart,M
改进的固定程序，使子结构观察脊椎动物骨骼肌厚细丝的横截面，薄至140 nm的电子显微镜。光学衍射结合数字自相关分析，焦点系列和倾斜实验已经证实了一个规则的子结构的存在，具有重复近4 nm，并表明它是极不可能是一个与电子显微镜成像系统相关的工件。所获得的结果强烈地表明，粗丝是由一束棒状亚丝构成的，这些亚丝平行于粗丝轴排列，在小于一度的范围内。这与Squire（1973）提出的粗丝结构的一般理论不容易调和，但与Pepe，1966，Pepe，1967提出的模型是一致的。140 nm厚的连续横截面的光学衍射也表明了沿着丝的长度沿着的结构变化，其通过在一个、两个或三个方向上显示出强衍射最大值的丝的比例的变化来证明。
Improved fixation procedures have enabled substructure to be observed by electron microscopy in transverse sections of vertebrate skeletal muscle thick filaments as thin as 140 nm. Optical diffraction combined with digital autocorrelation analysis, focal series and tilting experiments have confirmed the presence of a regular substructure having a repeat near 4 nm and shown that it is highly unlikely to be an artifact associated with the electron microscope imaging system. The results obtained strongly suggest that the thick filament is constructed from a bundle of rod-like subfilaments arranged parallel to the thick filament axis to within less than a degree. This cannot easily be reconciled with the general theory of thick filament structure proposed by Squire (1973), but it is consistent with the model proposed by Pepe, 1966, Pepe, 1967. Optical diffraction of 140 nm thick serial transverse sections has also suggested a structural change along the length of the filament that is manifest by a variation in the proportion of filaments showing strong diffraction maxima in one, two or three directions.