Purification and characterization of collagenase activator protein synthesized by articular cartilage.

@article{Treadwell1986PurificationAC,
  title={Purification and characterization of collagenase activator protein synthesized by articular cartilage.},
  author={Benjamin V Treadwell and Jasper Neidel and M Pav{\'i}a and Christine A Towle and M E Trice and Henry J. Mankin},
  journal={Archives of biochemistry and biophysics},
  year={1986},
  volume={251 2},
  pages={715-23}
}
We have isolated an activator of collagenase from medium conditioned with articular cartilage. The activity is contained in an acidic protein appearing as a doublet band of Mr 57,000 and 56,000 on sodium dodecyl sulfate polyacrylamide gels. Both components of the doublet have identical isoelectric points as demonstrated by gel electrophoresis. Purified synovial collagenase has a high dependence on the presence of this factor for activity. Other known activators of latent proteolytic enzymes… CONTINUE READING

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