The formation and thermal stability of in vitro assembled fibrils from acid-soluble and pepsin-treated collagens.

@article{Snowden1979TheFA,
  title={The formation and thermal stability of in vitro assembled fibrils from acid-soluble and pepsin-treated collagens.},
  author={J. M. Snowden and D A Swann},
  journal={Biochimica et biophysica acta},
  year={1979},
  volume={580 2},
  pages={372-81}
}
The role of the non-helical regions of the collagen molecule in fibrillogenesis has been investigated by comparing the kinetics of fibril formation of pepsin-treated acid-soluble collagen, acid-soluble collagen and mixtures of the two and by comparison of the thermal stabilities of the fibrils formed. The acid-soluble collagen was found to aggregate more rapidly than the pepsin-treated collagen under physiological conditions of pH and ionic strength. Variations in ionic strength, at… CONTINUE READING

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