Interaction of α‐actinin and nebulin in vitro

FEBS Letters

Fürst, Dieter O.¹  Nave, Rüdiger¹  Weber, Klaus¹ 

[1] Max Planck Institute for Biophysical Chemistry, Department of Biochemistry, D-3400 Goettingen, FRG

关键词: α-Actinin;    Cardiac muscle;    Nebulin;    Sarcomere;    Skeletal muscle;    Z-line;    2ME;    2-mereaptoethanol;    SDS-PAGE;    polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate;    BSA;    bovine serum albumin;   

DOI  :  10.1016/0014-5793(90)81144-D

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 ¹²⁵I-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.

【 授权许可】

Unknown