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

Fang Geng, Xi Huang, Kaustav Majumder, Zhihui Zhu, Zhaoxia Cai, Meihu Ma

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9 Scopus citations


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 (N1221) 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.

Original languageEnglish (US)
Pages (from-to)8209-8215
Number of pages7
JournalJournal of Agricultural and Food Chemistry
Issue number37
StatePublished - Sep 23 2015



  • egg white
  • glycosylation
  • mass spectrometry
  • ovomacroglobulin
  • two-dimensional electrophoresis

ASJC Scopus subject areas

  • Chemistry(all)
  • Agricultural and Biological Sciences(all)

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