Abstract
WHEN fibrous elastin is rendered water soluble by partial hydrolysis the product, α-elastin, undergoes a temperature elicited coacervation which is readily reversible1,2. Below room temperature α-elastin is soluble in dilute aqueous buffers in the region of its isoelectric point. On raising the temperature to 37° C a phase separation or coacervation occurs. In this communication we wish briefly to report that the circular dichroism pattern of soluble elastin most nearly resembles that of disordered proteins and polypeptides whereas the circular dichroism pattern of the coacervate (a mucilaginous precipitate) is characteristic of those obtained for the highly helical proteins and polypeptides. A calculation based on model polypeptides and myoglobin and on corrections for dampening of CD patterns due to absorption flattening and dispersion distortions3 implies an approximate 50 per cent α-helical content for the protein in the coacervate.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Partridge, S. M., Davis, H. F., and Adair, G. D., Biochem. J., 61, 11 (1955).
Partridge, S. M., and Davis, H. F., Biochem. J., 61, 21 (1955).
Urry, D. W., and Ji, T. H., Arch. Biochem. Biophys., 128, 802 (1968).
Mammi, M., Gotte, L., and Pezzin, G., Nature, 220, 371 (1968).
Lowry, O. H., Rosenbrough, N. J., Farr, A. L., and Randall, R. J., J. Biol. Chem., 193, 265 (1955).
Urry, D. W., Ann. Rev. Phys. Chem., 19, 477 (1968).
Urry, D. W., Proc. US Nat. Acad. Sci., 60, 1114 (1968).
Edsall, J. T., Flory, P. J., Kendrew, J. C., Liquori, A. M., Memethy, G., Ramachandran, G. N., and Scheraga, H. A., Biopolymers, 4, 121 (1966); J. Biol. Chem., 241, 1004 (1966); J. Mol. Biol., 15, 399 (1966).
Holzwarth, G., and Doty, P., J. Amer. Chem. Soc., 87, 218 (1965).
Quadrifoglio, F., and Urry, D. W., J. Amer. Chem. Soc., 90, 2755 (1968).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
URRY, D., STARCHER, B. & PARTRIDGE, S. Coacervation of Solubilized Elastin effects a Notable Conformational Change. Nature 222, 795–796 (1969). https://doi.org/10.1038/222795a0
Received:
Issue Date:
DOI: https://doi.org/10.1038/222795a0
This article is cited by
-
Injectable tissue integrating networks from recombinant polypeptides with tunable order
Nature Materials (2018)
-
Calcification of α-elastin coacervates: A bulk property of elastin
Calcified Tissue Research (1976)
-
Scanning electron microscopy and electron probe microanalysis of calcified α-elastin coacervates
Calcified Tissue Research (1975)
-
Additional evidence for the binding of calcium ions to elastin at neutral sites
Calcified Tissue Research (1974)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.