Studies on the composition of egg-white ovomucin
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1. Purified ovomucin was isolated as an insoluble glycoprotein complex from thick egg white. 2. A homogeneous glycoprotein, designated α-ovomucin, of molecular weight 210000 and containing N-acetylglucosamine (6.7%, w/w), N-acetylgalactosamine (0.6%, w/w), galactose (1.8%, w/w), mannose (4.6%, w/w), N-acetylneuraminic acid (1.0%, w/w) and sulphate (0.7%, w/w), was isolated from preparations of reduced ovomucin by sedimentation equilibrium in a density gradient of caesium chloride formed in the presence of 4m-guanidine hydrochloride. 3. A carbohydrate-rich fraction, designated β-ovomucin (which is homogeneous by sedimentation-velocity analysis in 5m-guanidine hydrochloride but which is heterogeneous by analytical sedimentation equilibrium in a density gradient of caesium chloride in the presence of 4m-guanidine hydrochloride), containing N-acetylglucosamine (11.0%, w/w), N-acetylgalactosamine (8.7%, w/w), galactose (19.2%, w/w), mannose (4.1%, w/w), N-acetylneuraminic acid (13.8%, w/w) and sulphate (2.7%, w/w), was also obtained from preparations of reduced ovomucin by the density-gradient method. 4. Mild acid hydrolysis of the unfractionated ovomucin complex showed that N-acetylneuraminic acid occupied a terminal position of the oligosaccharide chains. 5. Alkaline β-elimination reactions with the unfractionated ovomucin complex indicated that N-acetylgalactosamine was linked by alkali-labile bonds to hydroxy amino acids.
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Ovomucin is insoluble in neutral pH conditions if denaturing agents such as SDS or β-mercaptoethanol are not present.
“Ovomucin is insoluble in neutral pH conditions if denaturing agents such as SDS or β-mercaptoethanol are not present”
From Egg white proteins and their potential use in food processing or as nutraceutical and pharmaceutical agents—A review (2013) · cites this paper as Robinson and Monsey, 1971
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- Authors
- Robinson, D. S., & Monsey, J. B.
- Affiliations
- Agricultural Research Council Food Research Institute, Colney Lane, Norwich NOR 70F, U.K.
- ORCID
- Robinson, D. S.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1971-02-01
- Volume
- 121
- Issue
- 3
- Pages
- 537-547
- ISSN
- 0306-3283 (ISSN-L)
- PMC
- PMC1176603
- OpenAlex
- W1843733390
- Cited by
- 104
- References
- 36
- Citations by year
- 2025: 4 · 2024: 2 · 2023: 3 · 2022: 4 · 2021: 1 · 2020: 5 · 2019: 6 · 2018: 4 · 2017: 5 · 2016: 5 · 2015: 5 · 2014: 1 · 2013: 2 · 2012: 1
- FWCI
- 1.76
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- 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
- Life Sciences › Agricultural and Biological Sciences › Food Science › Polysaccharides Composition and Applications
- Keywords
- ovomucin, egg white, glycoprotein composition, N-acetylneuraminic acid, sialic acid, N-acetylglucosamine, N-acetylgalactosamine, oligosaccharide structure, glycosylation, sulfate, acid hydrolysis, hydroxy amino acids
- MeSH terms
- Amino Acids, Centrifugation, Density Gradient, Chromatography, Gel, Chromatography, Paper, Egg White, Electrophoresis, Galactosamine, Galactose, Glucosamine, Glycoproteins, Hexosamines, Hexoses, Hydrolysis, Mannose, Models, Structural, Molecular Weight, Neuraminic Acids, Oxidation-Reduction, Sulfates
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