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Constitution of the Cross-linkages in Elastin

Abstract

ELASTIN is insoluble in all reagents except those which break peptide bonds, and when wet the protein behaves as a typical rubber-like solid1. These characteristics, together with the swelling properties, are consistent with the view that elastin can be regarded as a cross-linked polymer gel containing long peptide chains randomly crumpled and held laterally at intervals by strong chemical bonds2. In an attempt to isolate small regions of the peptide network containing the cross-links, Thomas and Partridge3 degraded the protein by use of a succession of proteolytic enzymes followed by amino- and carboxy-peptidases. The product consisted of amino-acids and small peptides together with a fraction of higher molecular weight. This fraction was isolated and was found to be bright yellow in colour with the blue-white fluorescence characteristic of elastin fibres.

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References

  1. 1

    Hoeve, C. A. J., and Flory, P. J., J. Amer. Chem. Soc., 80, 6523 (1958).

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  2. 2

    Partridge, S. M., Advances in Protein Chemistry, 17, 227 (Academic Press, New York, 1962).

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  3. 3

    Thomas, J., and Partridge, S. M., First Intern. Cong. Food Sci. and Tech., Proc. (in the press).

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PARTRIDGE, S., ELSDEN, D. & THOMAS, J. Constitution of the Cross-linkages in Elastin. Nature 197, 1297–1298 (1963). https://doi.org/10.1038/1971297a0

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