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Hydroxyproline and the Shrinkage Temperature of Collagen B. J. RIGBY & J. D. SPIKES Wool Research Laboratories, Commonwealth Scientific and Industrial Research Organization, Ryde, New South Wales. IT is well known that collagens from various sources have characteristic shrinkage temperatures (T s), at which samples will contract abruptly in water or in 0.9 per cent saline solution. The T s values of fish-skin collagens range from about 35° C. to 57° C., according to the mean temperature of the environment1, while mammalian collagen has a T s value of about 62° C., apparently irrespective of source. By an examination of the complete amino-acid analyses, these shrinkage temperatures have been correlated with the hydroxyproline content of the collagen; the lower the amount of hydroxyproline the lower the value of T s (ref. 1). Hydroxyproline is considered to consolidate the collagen structure by forming hydrogen bonds between molecular chains. The data of ref. 1 have been plotted by us in Fig. 1 using the mean values of the shrinkage temperature quoted. These data are represented by circles and include the additional values, hydroxyproline = 12.0 per cent and 13.0 per cent for cattle hide and rat tail tendon respectively. The continuous straight line in Fig. 1 has been fitted by the method of least squares to these data on the assumption that the relation between hydroxyproline and T s is linear.
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