Abstract
SOLUBLE collagen can be extracted from collagenous material with neutral salt solutions and weak acids. These extracts display many similar physical and chemical characteristics, but differ significantly with respect to their solubility. Neutral-salt-soluble collagen has been shown to be the precursor collagen1,2, with acid-soluble collagen being the more mature fibre-forming protein3. The relationship between these soluble collagens which is usually accepted relies on the presence or absence of intramolecular cross links. Apart from hydrogen bonds no intramolecular bonds are considered to occur in neutral-salt-soluble collagen. On the other hand, acid-soluble collagen is formed as intramolecular bonds are introduced into neutral-salt-soluble collagen. Such a relationship alone is insufficient, however, to explain the very different solubility properties of these two forms of collagen. It is therefore proposed that neutral-salt-soluble and acid-soluble collagen are related on an intermolecular basis in their native environment, but that their subsequent extraction in mildly acid and basic conditions results in the degradation of terminally located telopeptides, which play a vital part in the properties of these collagen preparations. The evidence for this theory is now outlined.
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DAVIDSON, R., COOPER, D. Intermolecular Relationship between Neutral-salt-soluble and Acid-soluble Collagen. Nature 217, 168–169 (1968). https://doi.org/10.1038/217168a0
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DOI: https://doi.org/10.1038/217168a0
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