The solubilization of bone and dentin collagens by pepsin. Effect of cross-linkages and non-collagen components.

@article{Carmichael1977TheSO,
  title={The solubilization of bone and dentin collagens by pepsin. Effect of cross-linkages and non-collagen components.},
  author={David J. Carmichael and Carole M. Dodd and Arthur Veis},
  journal={Biochimica et biophysica acta},
  year={1977},
  volume={491 1},
  pages={177-92}
}
Bone and dentin collagen are less susceptible to solubilization by pepsin digestion then is skin collagen. Digestion at 4 degrees C for 72 h solubilized only 35.3% of bovine cortical bone and 5.6% of bovine dentin compared with nearly 100% dissolution of bovine skin. Sodium dodecyl sulfate-acrylamide gel electrophoresis and molecular sieve chromatography showed that, for bone and dentin, intact alpha chains and cross-linked aggregates of beta, gamma and higher weight remained intact after… CONTINUE READING