The structure of avian type XII collagen. Alpha 1 (XII) chains contain 190-kDa non-triple helical amino-terminal domains and form homotrimeric molecules.

@article{Dublet1989TheSO,
  title={The structure of avian type XII collagen. Alpha 1 (XII) chains contain 190-kDa non-triple helical amino-terminal domains and form homotrimeric molecules.},
  author={Bernard Dublet and S Oh and Stephen P. Sugrue and M. K. Gordon and Donald R. Gerecke and Bjorn Reino Olsen and Michel van der Rest},
  journal={The Journal of biological chemistry},
  year={1989},
  volume={264 22},
  pages={13150-6}
}
The monoclonal antibody 75d7, specific for type XII collagen (Sugrue, S.P., Gordon, M.K., Seyer, J., Dublet, B., van der Rest, M., and Olsen, B. R. (1989) J. Cell Biol., in press), was used to characterize the intact form of type XII collagen from chick embryo leg tendons. On an immunoblot of a 6% polyacrylamide gel of tendon extracts, one sharp band is recognized by the antibody at Mr = 220,000, while two fuzzy and poorly resolved bands are seen at Mr = 270,000 and Mr = 290,000. By… CONTINUE READING

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