Mode of degradation of myofibrillar proteins by an endogenous protease, cathepsin L.

@article{Matsukura1981ModeOD,
  title={Mode of degradation of myofibrillar proteins by an endogenous protease, cathepsin L.},
  author={Ushio Matsukura and Akihiro Okitani and Tatsuo Nishimuro and Hideo Kato},
  journal={Biochimica et biophysica acta},
  year={1981},
  volume={662 1},
  pages={
          41-7
        }
}
The mode of degradation of myofibrils and their constituent proteins by cathepsin L (EC 3.4.22.15) of rabbit skeletal muscle was studied. Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis showed that cathepsin L degraded myosin heavy chain, alpha-actinin, actin, troponin T and troponin I assembled in myofibrils and produced mainly fragments of 160 000 and 30 000 daltons in the acidic pH region. This degradation was most intense around pH 4. Degradation of myosin in the isolated… CONTINUE READING

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