The supramolecular organization of ovomucin. Biophysical and morphological studies

C. Rabouille, M. A. Aon, G. Muller, J. Cartaud, D. Thomas

Research output: Contribution to journalArticle

Abstract

Ovomucin participates in the ovomucin-gel-forming properties because of its shape and its ability to interact in a specific spatial organization. Purified from chicken egg-white by exclusion chromatography with Sephacryl S-300 and Sepharose CL-2B and analysed by light-scattering, it exhibited an M(r) of about 40 x 106. This large M(r) can be explained by the aggregation of polymers that can be degraded into 3 x 106-M(r) fragments by reduction with dithiothreitol. The values for hydrodynamic parameters such as M(r), radius of gyration, hydrodynamic radius, mass per unit length and combinations of them suggested that ovomucin is a linear and highly flexible molecule conferring upon it a random-coil-like structure in 0.2 M-NaCl solution. Analysis of the ovomucin molecules by electron microscopy revealed its linear character but also indicated a lower M(r) than that obtained in the light-scattering experiments. By temperature-induced non-specific aggregation of an ovomucin solution containing other globular egg proteins, an attempt was made to find out what conditions are required for gel formation and to examine the quality of aggregation that is obtained under these conditions. Results show that the viscosity of the solution did not increase after heat treatment. Apparently, in the ovomucin gel, specific spatial organization of the ovomucin molecules is required for hydrogel formation.

Original languageEnglish (US)
Pages (from-to)697-706
Number of pages10
JournalBiochemical Journal
Volume266
Issue number3
StatePublished - 1990
Externally publishedYes

Fingerprint

Ovomucin
Agglomeration
Gels
Hydrodynamics
Light scattering
Molecules
Egg Proteins
Light
Egg White
Dithiothreitol
Hydrogel
Chromatography
Viscosity
Sepharose
Electron microscopy
Gel Chromatography
Chickens
Electron Microscopy
Polymers
Hot Temperature

ASJC Scopus subject areas

  • Biochemistry

Cite this

Rabouille, C., Aon, M. A., Muller, G., Cartaud, J., & Thomas, D. (1990). The supramolecular organization of ovomucin. Biophysical and morphological studies. Biochemical Journal, 266(3), 697-706.

The supramolecular organization of ovomucin. Biophysical and morphological studies. / Rabouille, C.; Aon, M. A.; Muller, G.; Cartaud, J.; Thomas, D.

In: Biochemical Journal, Vol. 266, No. 3, 1990, p. 697-706.

Research output: Contribution to journalArticle

Rabouille, C, Aon, MA, Muller, G, Cartaud, J & Thomas, D 1990, 'The supramolecular organization of ovomucin. Biophysical and morphological studies', Biochemical Journal, vol. 266, no. 3, pp. 697-706.
Rabouille C, Aon MA, Muller G, Cartaud J, Thomas D. The supramolecular organization of ovomucin. Biophysical and morphological studies. Biochemical Journal. 1990;266(3):697-706.
Rabouille, C. ; Aon, M. A. ; Muller, G. ; Cartaud, J. ; Thomas, D. / The supramolecular organization of ovomucin. Biophysical and morphological studies. In: Biochemical Journal. 1990 ; Vol. 266, No. 3. pp. 697-706.
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