The stability of collagen cross-links when derived from hydroxylsyl residues.

@article{Miller1973TheSO,
  title={The stability of collagen cross-links when derived from hydroxylsyl residues.},
  author={Edward John Miller and Paul Robertson},
  journal={Biochemical and biophysical research communications},
  year={1973},
  volume={54 1},
  pages={
          432-9
        }
}
Abstract The cross-linked cyanogen bromide peptide, (4×9), previously isolated after reduction of cartilage collagen, has been isolated without prior reduction of the collagen. The unreduced cross-link is cleaved by periodate allowing recovery of the component peptides. When isolated after borotritide reduction of the collagen, (4×9) contains a single residue of radioactive hydroxylysinohydroxynorleucine. Radioactivity in the cross-link remains in the component peptides when the cross-link is… CONTINUE READING

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Diseases of the collagen molecule.

  • Journal of clinical pathology. Supplement
  • 1978