Structure, function and tissue forms of the C-terminal globular domain of collagen XVIII containing the angiogenesis inhibitor endostatin.

@article{Sasaki1998StructureFA,
  title={Structure, function and tissue forms of the C-terminal globular domain of collagen XVIII containing the angiogenesis inhibitor endostatin.},
  author={Takako Sasaki and Naomi Fukai and Karlheinz Mann and Walter Goehring and Bjorn Reino Olsen and Rupert Timpl},
  journal={The EMBO journal},
  year={1998},
  volume={17 15},
  pages={4249-56}
}
The C-terminal domain NC1 of mouse collagen XVIII (38 kDa) and the shorter mouse and human endostatins (22 kDa) were prepared in recombinant form from transfected mammalian cells. The NC1 domain aggregated non-covalently into a globular trimer which was partially cleaved by endogenous proteolysis into several monomers (25-32 kDa) related to endostatin. Endostatins were obtained in a highly soluble, monomeric form and showed a single N-terminal sequence which, together with other data, indicated… CONTINUE READING

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