Possible involvement of aminotelopeptide in self-assembly and thermal stability of collagen I as revealed by its removal with proteases.

@article{Sato2000PossibleIO,
  title={Possible involvement of aminotelopeptide in self-assembly and thermal stability of collagen I as revealed by its removal with proteases.},
  author={Kaori Sato and Takuya Ebihara and Eijiro Adachi and Seiichi Kawashima and Seisuke Hattori and Shinkichi Irie},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 33},
  pages={25870-5}
}
The functions of aminotelopeptide and N-terminal cross-linking of collagen I were examined. Acetic acid-soluble collagen I (ASC) was purified from neonatal bovine skin and treated with three kinds of proteases. The amino acid sequencing analysis of the N terminus showed that ASC contained a full-length aminotelopeptide. Pepsin and papain cleaved the aminotelopeptide of the alpha1 chain at the same site and the aminotelopeptide of the alpha2 chain at different sites. Proctase-treated ASC lost… CONTINUE READING

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