An essential myosin light chain peptide induces supramaximal stimulation of cardiac myofibrillar ATPase activity.

@article{Rarick1996AnEM,
  title={An essential myosin light chain peptide induces supramaximal stimulation of cardiac myofibrillar ATPase activity.},
  author={Helen M. Rarick and Terry J. Opgenorth and Thomas W. von Geldern and Jinshyun Ruth Wu-Wong and R. John Solaro},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 43},
  pages={27039-43}
}
The N-terminal region of skeletal myosin light chain-1 (MLC-1) binds to the C terminus of actin, yet the functional significance of this interaction is unclear. We studied a fragment (MLC-pep; residues 5-14) of the ventricular MLC-1. When added to rat cardiac myofibrils, 10 nM MLC-pep induced a supramaximal increase in the MgATPase activity at submaximal Ca2+ levels with no effect at low and maximal Ca2+ levels. A nonsense, scrambled sequence peptide had no effect at any pCa value. MLC-pep did… CONTINUE READING

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