Abstract
The coacervate phase produced by raising the temperature of solutions of blocked α-elastin has water content and fibrillar structure at electron microscope level similar to fibrous elastin (Cox, B.A., Starcher, B.C., Urry, D.W. (1973) Biochim, Biophys. Acta 317, 209–213). The stability ranges of the coacervates under varying conditions of temperature, pH, salt concentration and concentration of added organic solvent have been investigated with results that suggest a marked sensitivity of elastin conformation to solution conditions.
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References
Partridge, S.M., Davis, H.F. and Adair, G.S. (1955) Biochem. J. 61, 11–21.
Partridge, S.M. and Davis, H.F. (1955) Biochem. J. 61, 21–30.
Cox, B.A., Starcher, B.C., Urry, D.W. (1973) Biochim. Biophys. Acta 317, 209–213.
Urry, D.W., Starcher, B. and Partridge, S.M. (1969) Nature 222, 795–796.
Starcher, B.C. and Urry, D.W. (1973) Biochem. Biophys. Res. Commun. 53, 210–216.
Bendall, J.R. (1955) Biochem. J. 61, 31–32.
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© 1977 Plenum Press, New York
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Partridge, S.M., Whiting, A.H. (1977). The Coacervate-Sol Transition Observed with α-Elastin and its N-Formyl O-Methyl Derivative. In: Sandberg, L.B., Gray, W.R., Franzblau, C. (eds) Elastin and Elastic Tissue. Advances in Experimental Medicine and Biology, vol 79. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-9093-0_60
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DOI: https://doi.org/10.1007/978-1-4684-9093-0_60
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