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连接及其片段的电子显微镜下细丝长度

Electron microscopic filament lengths of connection and its fragments.

作者信息

Suzuki J, Kimura S, Maruyama K

机构信息

Department of Biology, Faculty of Science, Chiba University.

出版信息

J Biochem. 1994 Aug;116(2):406-10. doi: 10.1093/oxfordjournals.jbchem.a124539.

Abstract

Connectin (titin) is an extraordinarily long filamentous protein of striated muscle. The particle lengths of alpha-connectin (titin 1) and its proteolytic products, beta-connectin (titin 2) and 1,200 kDa fragment, were measured with rotary-shadowed images of the filaments after orientation by centrifugation. It was observed that the 1,200 kDa fragment was frequently folded into a double strand, beta-connectin was partly folded, and alpha-connectin was easily split into beta-connectin and 1,200 kDa fragment. Taking these features into consideration, the average lengths of alpha- and beta-connectin and 1,200 kDa fragment were estimated to be approximately 1,250, 920, and 360 nm, respectively.

摘要

连接蛋白(肌联蛋白)是横纹肌中一种极其长的丝状蛋白。通过离心定向后,利用细丝的旋转阴影图像测量了α-连接蛋白(肌联蛋白1)及其蛋白水解产物β-连接蛋白(肌联蛋白2)和1200 kDa片段的颗粒长度。观察到1200 kDa片段经常折叠成双链,β-连接蛋白部分折叠,而α-连接蛋白很容易分裂成β-连接蛋白和1200 kDa片段。考虑到这些特征,估计α-连接蛋白、β-连接蛋白和1200 kDa片段的平均长度分别约为1250、920和360 nm。

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