Abstract
WE regret the error in our original publication1, and thank Drs. Bowes and Moss for the correction. As they point out, the T s corresponding to the correct value for the hydroxyproline in the example quoted is about 60° C. However, as was stated in the original article of Bowes, Elliott and Moss2, fibrinoid tissue from patients suffering from rheumatic fever and rheumatoid arthritis contains less hydroxyproline than normal tissue, so that our statement was qualitatively correct. We reiterate our main theme, that since the denaturation and shrinkage of collagen is a time-dependent process3, collagen will denature at temperatures below the instantaneous shrinkage temperature given a sufficiently long time, and that this time will be reduced (at any fixed temperature) if the percentage of hydroxyproline is also reduced. Gustavson4 has presented experimental evidence along these lines showing that calf-skin begins to denature in water at 45° C. after one week. Stress relaxation studies5 also show that rat-tail tendon slightly extended in 0.9 per cent saline begins to denature at about 40° C., although there is no tendency for the tendon to shrink when unloaded. We consider this to be the beginning of the structural breakdown which, however, only takes place on a large enough scale to cause instantaneous shrinkage at the higher temperature known as the shrinkage temperature.
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References
Rigby, B. J., and Spikes, J. D., Nature, 187, 150 (1960).
Bowes, J. H., Elliott, R. G., and Moss, J. A., in “Nature and Structure of Collagen”, edit. by Randall, 199 (Butterworths, London, 1953).
Weir, C. E., J. Amer. Leather Chem. Assoc., 44, 108 (1949).
Gustavson, K. H., Nature, 188, 419 (1960).
Rigby, B. J., Hirai, N., Spikes, J. D., and Eyring, H., J. Gen. Physiol., 43, 265 (1959).
Piez, K. A., and Gross, J., Biochim. Biophys. Acta, 34, 24 (1959).
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RIGBY, B., SPIKES, J. Hydroxyproline and the Shrinkage Temperature of Collagen. Nature 188, 1120 (1960). https://doi.org/10.1038/1881120b0
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DOI: https://doi.org/10.1038/1881120b0
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