Tryptic digestion of scallop S1: evidence for a complex between the two light-chains and a heavy-chain peptide

@article{Szentkiralyi1984TrypticDO,
  title={Tryptic digestion of scallop S1: evidence for a complex between the two light-chains and a heavy-chain peptide},
  author={Eva M. Szentkiralyi},
  journal={Journal of Muscle Research & Cell Motility},
  year={1984},
  volume={5},
  pages={147-164}
}
When scallop S1(+LC) (formerly called CaMg S1) is digested by trypsin, the heavy chain degrades while the two light chains remain complexed to each other and a peptide fragment of the heavy chain. The three components of the complex comigrate during electrophoresis under nondissociating conditions and can be purified by chromatography and concentrated by precipitation with ammonium sulphate in the presence of millimolar calcium ions. The truncated regulatory light chain remains associated with… CONTINUE READING
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Evidence for the role of the COOH - terminal region of myosin subfragment 1 heavy chain in the binding of the alkali light chain

  • M. BURKE, M. SIVARAMAKRISHNAN, V. KAMALAKANNAN
  • Biophys . J
  • 1983

Scallop regulatory and essential light chains complex with the same heavy chain peptide fragment

  • E. M. SZENTKIRALYI
  • Biophys . J
  • 1982

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