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

The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.

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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Metadata

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
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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