A Ca2+-activated protease possibly involved in myofibrillar protein turnover. Purification from porcine muscle.

@article{Dayton1976ACP,
  title={A Ca2+-activated protease possibly involved in myofibrillar protein turnover. Purification from porcine muscle.},
  author={William R. Dayton and Darrel E. Goll and Michael G. Zeece and Richard M. Robson and W J Reville},
  journal={Biochemistry},
  year={1976},
  volume={15 10},
  pages={2150-8}
}
Ca2+-activated Z-disk-removing activity in the P0-40 crude muscle extracts described by Busch et al. (Busch, W. A., Stromer, M. H., Goll, D. E., and Suzuki, A. (1972), J. Cell Biol. 52, 367) was purified from porcine skeletal muscle extracts by using five column chromatographic procedures in succession: (1) 6% agarose; (2) DEAE-cellulose; (3) Sephadex G-200; (4) DEAE-cellulose with a very shallow gradient; (5) Sephadex G-150. All Z-disk-removing activity eluted in a single peak off each column… CONTINUE READING

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