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Titolo:
ELECTRON-MICROSCOPIC FILAMENT LENGTHS OF CONNECTIN AND ITS FRAGMENTS
Autore:
SUZUKI J; KIMURA S; MARUYAMA K;
Indirizzi:
CHIBA UNIV,FAC SCI,DEPT BIOL,INAGE KU CHIBA 263 CHIBA JAPAN CHIBA UNIV,FAC SCI,DEPT BIOL,INAGE KU CHIBA 263 CHIBA JAPAN
Titolo Testata:
Journal of Biochemistry
fascicolo: 2, volume: 116, anno: 1994,
pagine: 406 - 410
SICI:
0021-924X(1994)116:2<406:EFLOCA>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
RABBIT SKELETAL-MUSCLE; ALPHA-CONNECTIN; ELASTIC PROTEIN; BETA-CONNECTIN; TITIN; LOCALIZATION; PURIFICATION; MOLECULES; TWITCHIN; NEBULIN;
Keywords:
CONNECTIN; FILAMENT LENGTH; ROTARY SHADOWING; TITIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
21
Recensione:
Indirizzi per estratti:
Citazione:
J. Suzuki et al., "ELECTRON-MICROSCOPIC FILAMENT LENGTHS OF CONNECTIN AND ITS FRAGMENTS", Journal of Biochemistry, 116(2), 1994, pp. 406-410

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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 10:58:11