Coacervation of Solubilized Elastin effects a Notable Conformational Change (original) (raw)

Nature volume 222, pages 795–796 (1969) Cite this article

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 52 print issues and online access

$199.00 per year

only $3.83 per issue

Buy this article

USD 39.95

Prices may be subject to local taxes which are calculated during checkout

Additional access options:

Similar content being viewed by others

References

  1. Partridge, S. M., Davis, H. F., and Adair, G. D., Biochem. J., 61, 11 (1955).
    Article CAS Google Scholar
  2. Partridge, S. M., and Davis, H. F., Biochem. J., 61, 21 (1955).
    Article CAS Google Scholar
  3. Urry, D. W., and Ji, T. H., Arch. Biochem. Biophys., 128, 802 (1968).
    Article CAS Google Scholar
  4. Mammi, M., Gotte, L., and Pezzin, G., Nature, 220, 371 (1968).
    Article ADS CAS Google Scholar
  5. Lowry, O. H., Rosenbrough, N. J., Farr, A. L., and Randall, R. J., J. Biol. Chem., 193, 265 (1955).
    Google Scholar
  6. Urry, D. W., Ann. Rev. Phys. Chem., 19, 477 (1968).
    Article ADS CAS Google Scholar
  7. Urry, D. W., Proc. US Nat. Acad. Sci., 60, 1114 (1968).
    Article ADS CAS Google Scholar
  8. 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).
    Article CAS Google Scholar
  9. Holzwarth, G., and Doty, P., J. Amer. Chem. Soc., 87, 218 (1965).
    Article CAS Google Scholar
  10. Quadrifoglio, F., and Urry, D. W., J. Amer. Chem. Soc., 90, 2755 (1968).
    Article CAS Google Scholar

Download references

Author information

Authors and Affiliations

  1. Institute for Biomedical Research, American Medical Association, 535 North Dearborn Street, Chicago, Illinois, 60610
    D. W. URRY & B. STARCHER
  2. Meat Research Institute, Langford, Bristol
    S. M. PARTRIDGE

Authors

  1. D. W. URRY
  2. B. STARCHER
  3. S. M. PARTRIDGE

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

Download citation