Controlled proteolysis of the purified Ca2+-ATPase of the erythrocyte membrane. A correlation between the structure and the function of the enzyme.

@article{Zurini1984ControlledPO,
  title={Controlled proteolysis of the purified Ca2+-ATPase of the erythrocyte membrane. A correlation between the structure and the function of the enzyme.},
  author={Mauro G. M. Zurini and Joachim Krebs and John T. Penniston and Ernesto Carafoli},
  journal={The Journal of biological chemistry},
  year={1984},
  volume={259 1},
  pages={618-27}
}
The purified Ca2+-pumping ATPase of the erythrocyte plasma membrane has been subjected to a controlled proteolytic treatment with trypsin. The treatment has been previously shown to shift the enzyme from low to high Ca2+ affinity in the absence of calmodulin. The treatment leads to the fragmentation of the ATPase molecule into a number of products and to the accumulation of major limit polypeptides having Mr of 14,000, 28,000, 33,500, 48,000, and 76,000. The 33,500 Mr fragment reacts with 3… CONTINUE READING

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