Carbohydrates in protein. 6. Studies on the carbohydrate-peptide bond in hen's-egg albumin

Marks, G. S.; Marshall, Ruth; Neuberger, A.

doi:10.1042/bj0870274

Cited by 119 publications

(37 citation statements)

References 23 publications

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“…Apart from an acetyl group at the iV-terminal end of the molecule (Narita & Ishii, 1962), the only known non-amino-acid component of ovalbumin is the carbohydrate moiety. This has been the subject of sustained investigation by Neuberger and his collaborators (Marks et al, 1963;Fletcher et al, 1963) and probably com-prises 5 mannose and 3 JV-acetylglucosamine moieties attached as a unit to one aspartic acid residue in each ovalbumin molecule; however, the latest work of Cunningham (Cunningham et al, 1963) shows that the glycopeptide fraction from a pepsin digest of ovalbumin can be fractionated chromatographically into four fractions which differ in the relative amounts of mannose and glucosamine which they contain. This result may provide the explanation of the electrophoretic heterogeneity of dephosphorylated ovalbumin.…”

Section: Discussionmentioning

confidence: 99%

Egg albumen polymorphisms in the fowl: The ovalbumin locus

Lush

1964

Genet. Res.

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1. Ovalbumin was shown, by starch gel electrophoresis, to exist in two genetically different forms, A and B. It was suggested that these are determined by two alleles at one locus, named Ov.2. Ovalbumin of each genetic type is electrophoretically heterogeneous. Dephos-phorylation of each type with human prostatic phosphatase and calf intestinal phosphatase removed some of the heterogeneity, but some remained.3. The genetic difference was shown not to reside in the fragment released from ovalbumin by the proteolytic enzyme subtilisin.4. The genetic difference was evident in the ovalbumin present in the fluid contained in right oviduct cysts.

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Section: Discussionmentioning

confidence: 99%

Egg albumen polymorphisms in the fowl: The ovalbumin locus

Lush

1964

Genet. Res.

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“…An N-(P-aspartyl)glycosylamine linkage has been demonstrated in egg albumin (Marks, Marshall & Neuberger, 1963;Yamashina & Makino, 1962;Bogdanov, Kaverzneva & Andrejeva, 1962). Glycosidic ester linkage to both glutamic acid and aspartic acid also occurs in preparations of bovine submaxillary-gland mucin (Murphy & Gottschalk, 1961).…”

Section: Resultsmentioning

confidence: 99%

Linkage of carbohydrate to hydroxyamino acids in mucopolysaccharides and mucoproteins

1965

Biochemical Journal

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1. Glycosidic linkage of carbohydrate to the primary hydroxyl groups of threonine and serine has been established in human blood-group A and Lea substances, bovine submaxillary-gland mucin and human pseudomyxomatous mucin. 2. Treatment of these substances in 0 09N-lithium hydroxide at 100°for lhr. led to ,B-elimination at these glycosidic linkages with the resultant formation of a-oxobutyric acid and glycine from threonine linkages, and pyruvic acid from serine linkages. Though most of the threonine was destroyed in every ease, about onethird to one-half of the serine residues resisted alkaline cleavage. Such results, indicative of the presence of unbound serine residues, allow, in submaxillary mucin, for a close correlation between the remaining serine, threonine, glutamic acid and aspartic acid and the available sialyl-(2 -÷6)-N-acetylgalactosamine prosthetic groups. 3. The stoichiometry of the f-eliminations has been demonstrated for pseudomyxomatous mucin. The a-oxo acids were separated and determined as their quinoxalinol derivatives by thin-layer chromatography on silica gel. Reaction at the threonine centres favoured a-oxobutyric acid formation (70%, via the intermediary dehydropeptide) over the alternative pathway to glycine (30%). 4. 100% ofthe hexosamine was destroyed in submaxillary-gland mucin, 85% in pseudomyxomatous mucin and about 60% in the blood-group substances. In the latter cases, the glucosamine/galactosamine ratio was increased from about 4:1 to 8-10:1, suggesting a preferential destruction of galactosamine. Evidence was obtained, however, for a further destruction of hexosamine, in addition to that which could be theoretically attached to peptide at possible known binding sites. 5. The major part of the alkali-resistant hexosamine in the blood-group substances was nondiffusible and was accompanied by the constituent carbohydrates in similar molar proportions to the native materials.

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“…While glycomics is the study of the glycome, the central point of glycoproteomics is the study of the profile of glycosylated proteins ( glycoproteome) in a biological system. Initially identified in 1963 [24], glycosylation was thought of as a solely eukaryotic mechanism, although this view is no longer supported [25]. Glycoproteins are present in all cellular compartments of eukaryotic cells, and the glycosylation is highly specific at each site and generally stable for a given cell type and physiological state.…”

Section: Glycoproteinsmentioning

confidence: 99%