Calmodulin‐binding profiles for nebulin and dystrophin in human skeletal muscle

FEBS Letters

Strong, P.N.¹  Dubowitz, V.¹  Patel, K.¹  Dunn, M.J.¹ 

[1] Jerry Lewis Muscle Research Centre, Department of Paediatrics and Neonatal Medicine, Royal Postgraduate Medical School, London W12 0NN, England

关键词: Muscle protein;    Duchenne muscular dystrophy;    Nebulin;    Dystrophin;    Calmodulin;    SDS-PAGE;    PBS;    phosphate-buffered saline;    TP buffer;    PBS containing 0.05% Tween 20;    TCAP buffer;    TP buffer containing 1 μM Ca2+;    PMSF;    phenylmethylsulphonyl fluoride;   

DOI  :  10.1016/0014-5793(88)80095-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Nebulin and dystrophin are two high-molecular-mass skeletal muscle proteins that have both been associated with the defective gene in Duchenne muscular dystrophy, although the function of neither protein is known. Other high-molecular-mass, calmodulin-binding proteins have recently been implicated in regulating calcium release from skeletal muscle. Western blots of human skeletal muscle biopsy samples were probed with biotinylated calmodulin; nebulin was identified as a prominent high-molecular-mass calmodulin-binding protein but dystrophin did not bind detectable amounts of biotinylated calmodulin. Dystrophin was absent in a Duchenne muscle biopsy.

【 授权许可】

Unknown