期刊
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 63, 期 37, 页码 8209-8215出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.5b02618
关键词
egg white; ovomacroglobulin; glycosylation; mass spectrometry; two-dimensional electrophoresis
资金
- Special Fund for Agro-scientific Research in the Public Interest [201303084]
- Earmarked Fund for Modern Agro-industry Technology Research System [CARS-41-K23]
- Fundamental Research Funds for the Central Universities [2014PY050]
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.
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