The reconstitution of elastin from a soluble protein derived from ligamentum nuchae

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Abstract
The high-molecular-weight [alpha]-fraction of soluble elastin prepared from ox ligamentum nuchae (Adair et al. 1951) becomes insoluble on prolonged heating of aqueous solutions under certain conditions. Heat-precipitated elastin has many of the physical properties of purified elastin and it is concluded that the protein molecules have essentially the same configuration in the 2 materials. Differences between heat-precipitated (reconstituted) elastin and purified elastin may be attributed to degradation of the latter when it is converted into soluble elastin. The precipitation of elastin appears to consist of two processes, namely a rapid one which may involve configurational changes and results in coacervation and a slow one which is probably due to aggregation of the protein molecules. The bearing of the results of the structure of elastin and its fibrogenesis is discussed.