Autolysis parallels activation of mu-calpain.

@article{Baki1996AutolysisPA,
  title={Autolysis parallels activation of mu-calpain.},
  author={Andrea Baki and Peter Tompa and Anita Alexa and Orsolya Moln{\'a}r and P{\'e}ter Friedrich},
  journal={The Biochemical journal},
  year={1996},
  volume={318 ( Pt 3)},
  pages={
          897-901
        }
}
The kinetics of autolysis and activation of mu-calpain were measured with microtubule-associated protein 2 (MAP2) as a very sensitive substrate. The initial rate of MAP2 hydrolysis was found to be a linear function of the autolysed 76 kDa form of mu-calpain large subunit at both 10 and 300 microM Ca2+, and both straight lines intersected the origin. This finding supports the view that native mu-calpain is an inactive proenzyme and that activation is accompanied by autolysis. The first-order… CONTINUE READING

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mu-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans.

  • American journal of physiology. Cell physiology
  • 2006
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