Ovine skeletal muscle multicatalytic proteinase complex (proteasome): purification, characterization, and comparison of its effects on myofibrils with mu-calpains.

@article{Koohmaraie1992OvineSM,
  title={Ovine skeletal muscle multicatalytic proteinase complex (proteasome): purification, characterization, and comparison of its effects on myofibrils with mu-calpains.},
  author={Mohammad Koohmaraie},
  journal={Journal of animal science},
  year={1992},
  volume={70 12},
  pages={3697-708}
}
The latent form of multicatalytic proteinase complex (MCP) was purified to homogeneity from ovine skeletal muscle. The MCP ran as a single band (M(r) 600,000) on nondenaturing polyacrylamide gel (PAGE) and dissociated to a number of subunits (M(r) 21,000 to 31,000) under denaturing and reducing conditions (SDS-PAGE). The proteinase complex was activated reversibly by heating at 60 degrees C and in the presence of SDS. Maximum activation (18-fold) was observed after 2 min at 60 degrees C and… CONTINUE READING

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