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Mass Spectrometry and Two-Dimensional Electrophoresis To Characterize the Glycosylation of Hen Egg White Ovomacroglobulin.
- Source :
-
Journal of agricultural and food chemistry [J Agric Food Chem] 2015 Sep 23; Vol. 63 (37), pp. 8209-15. Date of Electronic Publication: 2015 Sep 15. - Publication Year :
- 2015
-
Abstract
- Glycosylation of proteins plays an important role in their biological functions, such as allergenicity. Ovomacroglobulin (OVMG) is a glycoprotein from hen egg white, but few studies have been done so far to delineate the glycosylated sites of OVMG. The present study characterized the glycosylation of OVMG using mass spectrometry and two-dimensional electrophoresis. MALDI-TOF-MS showed that the OVMG subunit [M + H](+) ion has a peak at m/z 183297; therefore, the carbohydrate moiety is calculated as 11.5% of the whole OVMG molecule. HPLC-ESI-MS/MS confirmed that of 13 potential N-glycosylation sites of OVMG, 11 sites were glycosylated; 1 site (N(1221)) was found in both glycosylated and nonglycosylated forms. On the two-dimensional electrophoresis gel, a series of OVMG spots horizontally distributed at 170 kDa, with an isoelectric point range of 5.03-6.03, indicating the heterogeneity of glycosylation of OVMG. These results provided important information for understanding of structure, function, and potential allergenic sites of OVMG.
- Subjects :
- Amino Acid Sequence
Animals
Carbohydrates analysis
Chickens
Female
Glycosylation
Molecular Sequence Data
Molecular Weight
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Egg White chemistry
Electrophoresis, Gel, Two-Dimensional methods
Mass Spectrometry methods
alpha-Macroglobulins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1520-5118
- Volume :
- 63
- Issue :
- 37
- Database :
- MEDLINE
- Journal :
- Journal of agricultural and food chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 26322443
- Full Text :
- https://doi.org/10.1021/acs.jafc.5b02618