Abstract
Analysis of commercial samples of chicken ovalbumin by reversed-phase high performance liquid chromatography and matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) showed the presence of several other co-purifying glycoproteins. These were isolated, subjected to tryptic digestion, and two of them were identified as ovomucoid and chicken riboflavin binding-protein following database matching of the peptide masses obtained by MALDI. The N-linked glycans were released from the glycoproteins and their structures were examined by MALDI-MS in combination with exoglycosidase digestion. Ovalbumin was found to be glycosylated mainly with high-mannose and hybrid structures, consistent with profiles obtained on the intact glycoprotein by electrospray. The other glycoproteins contained mainly larger, complex glycans with up to five antennae, many of which had earlier been associated with ovalbumin.
MeSH Terms
Carbohydrates/chemistry,isolation & purification
Chromatography, High Pressure Liquid
Electrophoresis, Polyacrylamide Gel
Glycoproteins/chemistry,isolation & purification
Glycoside Hydrolases/chemistry
Hydrazines/chemistry
Hydrolysis
Mass Spectrometry
Ovalbumin/chemistry,isolation & purification
Peptides/chemistry
Polysaccharides/chemistry,isolation & purification
Trypsin
Chemicals
Carbohydrates
Glycoproteins
Hydrazines
Peptides
Polysaccharides
Ovalbumin
Glycoside Hydrolases
Trypsin
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Harvey D J
Department of Biochemistry, Oxford Glycobiology Institute, United Kingdom.
[email protected]
Wing D R
Küster B
Wilson I B
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