Cited by 22Polysaccharides Composition and ApplicationsGlycosylation and Glycoproteins ResearchProteoglycans and glycosaminoglycans research

The supramolecular organization of ovomucin—Biophysical and morphological studies

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Rabouille, C, Aon, M A, Muller, G, Cartaud, J, Thomas, D·1990·Biochemical Journal

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 Mr of about 40 x 10(6). This large Mr can be explained by the aggregation of polymers that can be degraded into 3 x 10(6)-Mr fragments by reduction with dithiothreitol. The values for hydrodynamic parameters such as Mr, 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 Mr 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.

Integrity signals

Registry

Crossref · 10.1042/bj2660697

Cites

34 of 34 references verified0 citation errors · 0 not checkable

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  • Homogenization and sonication improved the solubility of ovomucin to a certain degree by either cleaving the disulfide bonds or releasing the attached carbohydrate from the main protein chain.

    “Homogenization and sonication improved the solubility of ovomucin (Rabouille et al., 1990) to a certain degree by either cleaving the disulfide bonds or releasing the attached carbohydrate from the main protein chain (Omana et al., 2010).”
  • Rabouille et al. (1990) used a 10× dilution method to separate ovomucin, but a 10-fold increase in volume causes an important practical issue for scaled-up production.

    “Rabouille et al. (1990) used a 10× dilution method to separate ovomucin, but a 10-fold increase in volume causes an important practical issue for scaled-up production.”

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Authors
Rabouille, C., Aon, M. A., Muller, G., Cartaud, J., & Thomas, D.
Affiliations
  • Université de Technologie de Compiègne (FR)
  • Laboratoire des Polyméres, Biopolyméres et Membranes, U.A. 500 du C.N.R.S., Faculté de Sciences de Rouen, B.P. 116, 76130 Mont St. Aignan, France
  • Centre National de la Recherche Scientifique (FR)
Corresponding author
  • Rabouille, C
  • Thomas, D
Venue
Biochemical Journal
Published
1990-03-15
Volume
266
Issue
3
Pages
697-706
ISSN
  • 0264-6021 (ISSN-L)
  • 1470-8728
OpenAlex
W60932085
Cited by
22
References
36
Citations by year
2023: 1 · 2020: 1 · 2019: 1 · 2018: 1 · 2016: 1 · 2015: 3 · 2014: 3 · 2013: 1 · 2012: 1
FWCI
3.08
Type
journal article
Language
en
Open access
Locations
  • Biochemical Journal (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Polysaccharides Composition and Applications
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
Keywords
ovomucin, supramolecular organization, egg white proteins, gelation, hydrogels, molecular weight, radius of gyration, hydrodynamic radius, random coil, protein aggregation, heat-induced aggregation, viscosity, chicken egg white
MeSH terms
Animals, Chickens, Egg Proteins, Electrophoresis, Agar Gel, Molecular Weight, Ovomucin, Viscosity

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