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Medientyp:
E-Artikel
Titel:
Interaction of α‐actinin and nebulin in vitro : Support for the existenceof a fourth filament system in skeletal muscle
:
Support for the existenceof a fourth filament system in skeletal muscle
Beteiligte:
Nave, Rüdiger;
Fürst, Dieter O.;
Weber, Klaus
Erschienen:
Wiley, 1990
Erschienen in:
FEBS Letters, 269 (1990) 1, Seite 163-166
Beschreibung:
<jats:p>Nebulin is a high molecular weight polypeptide (mass 0.6–0.8 million) which accounts for 3% of the myofibrillar mass in skeletal muscle. Due to its resistance to extraction under native conditions, relatively little is known about the biochemistry of the molecule. Here we report in vitro binding of α‐actinin (a major Z‐line protein) to nebulin. After solubilization with sodium dodecylsulfate myofibrillar polypeptides separated by gel electrophoresis were blotted on nitrocellulose and probed with <jats:sup>125</jats:sup>I‐labelled α‐actinin, Nebulin is the only polypeptide decorated by α‐actinin. This result gives biochemical support for the hypothesis, based on recent immunoelectron micrographs, that nebulin could form in skeletal muscle a fourth filament system, possibly extending to the Z‐line.</jats:p>