Abstract
As one approach to the elucidation of the molecular arrangement in wool keratin, we have been using proteolytic enzymes under mild conditions to try to extract large molecules or aggregates of molecules from wool, which still preserve the configuration they had in the native fibre. In a previous communication1 we described experiments designed to discover the cause of wool's resistance to proteolytic enzymes. An important reason may be the highly cross-linked structure which only allows the fibre to swell a small amount in aqueous solutions, so that the large enzyme molecules cannot easily diffuse into the fibre.
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References
Greenwood, B. D., and Speakman, P. T., Nature, 204, 144 (1964).
Bailey, C. J., Jordan, B. J., and Speakman, P. T., (in preparation).
Szent-Györgyi, A. G., in Structure and Function of Muscle, edit. by Bourne, G. H., 2, 1 (Academic Press, New York and London, 1960).
Harrington, W. F., and von Hippel, P. H., Advances in Protein Chemistry, 16, 1 (1961).
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GREENWOOD, B., SPEAKMAN, P. 3.1-S Protein Fragment released from Reduced Wool by Trypsin. Nature 205, 79–80 (1965). https://doi.org/10.1038/205079a0
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DOI: https://doi.org/10.1038/205079a0
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