N-glycosylation proteome of endoplasmic reticulum in mouse liver by ConA affinity chromatography coupled with LTQ-FT mass spectrometry

Li Na Song, Jing Lan Wang, Jin Feng Liu, Zhuang Lu, Shao Hui Sui, Wei Jia, Bing Yang, Hao Chi, Le Heng Wang, Si Min He, Wen Feng Yu, Ling Yan Meng, Shuo Chen, Xu Peng, Yi Min Liang, Yun Cai, Xiao Hong Qian

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


Glycosylation is the most versatile and one of the most significant protein post-translational modifications. It is generally classified into three categories according to the amino acid to which the glycan is attached: N-glycosylation, O-glycosylation and C-glycosylation. Synthesis of N-glycoproteins occurs in the rough endoplasmic reticulum (rER), and all N-glycoproteins synthesized in rER have uniform glycan endings with mannose (Man) and glucose (Glc). A systematic strategy was developed to comprehensively profile N-glycoproteins in complex biological samples. The lectin Concanvalin A (ConA), which has a high affinity for glycans ending with Man, was used to extract the N-glycoproteins synthesized or located in the rER, and identified the N-glycoproteins and their glycosylation sites by LTQ-FT MS. The analysis was repeated three times at both the biological sample and mass spectrometry levels. In total, 323 glycosylation sites on 212 N-glycoproteins were identified in the mouse liver. Of these, 131 were known N-glycoproteins in the Swissprot database. The identified N-glycoproteins were classified according to their cell location by the Swissprot database and GO software. The identified N-glycoproteins in this study would serve as a good complement to the N-glycoprotein database for the mouse liver.

Original languageEnglish (US)
Pages (from-to)768-777
Number of pages10
JournalScience China Chemistry
Issue number4
StatePublished - Apr 2010
Externally publishedYes


  • ConA
  • Glycosylation
  • Lectin affinity chromatography
  • rER

ASJC Scopus subject areas

  • Chemistry(all)


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