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Interaction of α‐actinin and nebulin in vitro
Author(s) -
Nave Rüdiger,
Fürst Dieter O.,
Weber Klaus
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81144-d
Subject(s) - nebulin , myofibril , biochemistry , skeletal muscle , chemistry , immunoelectron microscopy , actinin , gel electrophoresis , biology , microbiology and biotechnology , sarcomere , myocyte , anatomy , cytoskeleton , antibody , titin , immunology , cell
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 125 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.