Cited by 104Glycosylation and Glycoproteins ResearchProteoglycans and glycosaminoglycans researchPolysaccharides Composition and Applications

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Studies on the composition of egg-white ovomucin

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Robinson, D. S., Monsey, J. B.·1971·Biochemical Journal

DOI 10.1042/bj1210537PMC PMC1176603

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Abstract

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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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)
DOI: 10.1042/bj1210537
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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