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紫贻贝前足丝牵缩肌粗肌丝中的副肌球蛋白结构。

Paramyosin structures in the thick filaments of the anterior byssus retractor muscle of Mytilus edulis.

作者信息

Heumann H G

出版信息

Eur J Cell Biol. 1980 Oct;22(2):780-8.

PMID:7449779
Abstract

Freeze-substituted cells of the anterior byssus retractor muscle of Mytilus edulis contain paramyosin filaments which exhibit a characteristic fine structure. Longitudinally sectioned filaments show a variety of band patterns, those occurring most frequently being cross, oblique or double oblique striations. The periodic spacings within one pattern are precise as can be demonstrated by Markham analysis and optical diffractometry. The patterns arise from structures in the interior of the filament since they persist in serially sectioned filaments and a layered structure is visible in cross-sectioned filaments. The different patterns are found to be convertible by rotating the grid around the filament axis. The observations led to the conclusion that the paramyosin core has some kind of helical arrangement. A model is proposed which consists of concentric layers of parallel paramyosin molecules which are displaced along the molecular axis in such a way that the characteristic Bear-Selby net structure results.

摘要

紫贻贝前足丝收缩肌经冷冻置换处理的细胞含有副肌球蛋白丝,这些丝呈现出独特的精细结构。纵向切片的丝呈现出多种带状模式,最常见的是交叉、倾斜或双斜条纹。通过马克姆分析和光学衍射法可以证明,一种模式内的周期性间距是精确的。这些模式源自丝内部的结构,因为它们在连续切片的丝中持续存在,并且在横截面的丝中可见分层结构。发现通过围绕丝轴旋转网格,不同的模式是可以转换的。这些观察结果得出结论,副肌球蛋白核心具有某种螺旋排列。提出了一个模型,该模型由平行副肌球蛋白分子的同心层组成,这些分子沿分子轴位移,从而形成特征性的贝尔-塞尔比网络结构。

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