Mass Spectrometry and Two-Dimensional Electrophoresis To Characterize the Glycosylation of Hen Egg White Ovomacroglobulin

Journal of Agricultural and Food Chemistry
Fang GengMeihu Ma

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.

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Citations

Jul 14, 2016·Journal of Biomedical Materials Research. Part B, Applied Biomaterials·Nathaniel T CarpenaByong-Taek Lee
Oct 21, 2016·Electrophoresis·Alireza BanazadehYehia Mechref
Dec 2, 2020·Foods·Iciar MartinezMónica Carrera
Aug 14, 2019·Journal of Agricultural and Food Chemistry·Yaqi MengRussell Keast
Jun 8, 2017·Journal of Agricultural and Food Chemistry·Fang GengMeihu Ma
Oct 20, 2018·Journal of Agricultural and Food Chemistry·Fang GengMeihu Ma

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