Comparison of different electrophoretic separations of hen egg white proteins
Abstract
The hen egg white protein composition has not yet been fully defined. To improve the knowledge of this biological fluid, the most usual and recently developed electrophoretic methods have been used: SDS-PAGE, native-PAGE, isoelectric focusing (IEF), and 2-dimensional electrophoresis (2DE). Seven of the major known proteins were thus identified in at least one electrophoretic system. Isoforms of ovotransferrin, ovalbumin, and ovomucoid were visualized when pI was used for the separation. Two-dimensional electrophoresis allowed separation of a very large number of spots. In each of the four systems, some components were revealed but not identified, and unknown spots were particularly numerous with 2DE. With this technique, many spots corresponding to small acidic proteins were highlighted, among which was the Ch21 protein, whose presence in hen egg white was thus confirmed. This study thus constitutes, to our knowledge, the first proteomic investigation of hen egg white.
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Sodium dodecyl sulfate-PAGE and 2-dimensional electrophoresis denature ovalbumin during separation.
“Sodium dodecyl sulfate-PAGE and 2-dimensional electrophoresis were also used to separate ovalbumin from egg white (Desert et al., 2001).However, the protein is denatured during the separation process.”
From Egg white proteins and their potential use in food processing or as nutraceutical and pharmaceutical agents—A review (2013) · cites this paper as Desert et al., 2001
The major limitation of electrophoresis for separating ovomucin was scaling up and denaturation of the protein during separation.
“The major limitation of this method was scaling up and denaturation of the protein during separation.”
From Egg white proteins and their potential use in food processing or as nutraceutical and pharmaceutical agents—A review (2013) · cites this paper as Desert et al., 2001
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Self-citation
- Authors
- Desert, C., Guérin-Dubiard, C., Nau, F., Jan, G., Val, F., & Mallard, J.
- Affiliations
- Ecole Nationale Supérieure Agronomique de Rennes and Research Laboratory for Dairy Technology (LRTL), Institut National de la Recherche Agronomique, 65 rue de Saint Brieuc, 35042 Rennes Cedex France
- Institut National de la Recherche Agronomique (FR)
- Venue
- Journal of Agricultural and Food Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2001-09-07
- Volume
- 49
- Issue
- 10
- Pages
- 4553-4561
- ISSN
- 0021-8561 (ISSN-L)
- 1520-5118
- OpenAlex
- W2058175369
- Cited by
- 123
- References
- 42
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 2 · 2023: 3 · 2022: 3 · 2021: 4 · 2020: 3 · 2019: 3 · 2018: 6 · 2017: 5 · 2016: 3 · 2015: 5 · 2014: 6 · 2013: 11 · 2012: 10
- FWCI
- 1.51
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Agricultural and Food Chemistry (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Agricultural and Biological Sciences › Food Science › Food and Agricultural Sciences
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Keywords
- proteome, SDS-PAGE, native PAGE, isoelectric focusing, two-dimensional gel electrophoresis, ovomucoid, acidic proteins, protein identification
- MeSH terms
- Animals, Chickens, Conalbumin, Egg Proteins, Electrophoresis, Electrophoresis, Polyacrylamide Gel, Isoelectric Focusing, Isoelectric Point, Ovalbumin, Ovomucin, Blotting, Western
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