ELECTRON-MICROSCOPIC FILAMENT LENGTHS OF CONNECTIN AND ITS FRAGMENTS

被引：22

作者：

SUZUKI, J ^{[1
]}

KIMURA, S ^{[1
]}

MARUYAMA, K ^{[1
]}

机构：

[1] CHIBA UNIV,FAC SCI,DEPT BIOL,INAGE KU,CHIBA 263,CHIBA,JAPAN

来源：

JOURNAL OF BIOCHEMISTRY | 1994年 / 116卷 / 02期

关键词：

CONNECTIN; FILAMENT LENGTH; ROTARY SHADOWING; TITIN;

D O I：

10.1093/oxfordjournals.jbchem.a124539

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：406 / 410

页数：5

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