A phosphorylated light-chain component of myosin from skeletal muscle.

@article{Perrie1973APL,
  title={A phosphorylated light-chain component of myosin from skeletal muscle.},
  author={W T Perrie and Lawrence B. Smillie and Stanton B. Perry},
  journal={The Biochemical journal},
  year={1973},
  volume={135 1},
  pages={151-64}
}
1. The low-molecular-weight components of myosin from rabbit skeletal muscle migrated as four bands on polyacrylamide-gel electrophoresis in 8m-urea but only as three in systems containing sodium dodecyl sulphate. The two bands of intermediate mobility in 8m-urea (Ml(2) and Ml(3)) had identical mobilities in sodium dodecyl sulphate. 2. The isolation of pure samples of all four low-molecular-weight components by DEAE-Sephadex chromatography is described. 3. The amino acid compositions of… CONTINUE READING