Identification of glycoproteins containing specific glycans using a lectin-chemical method

Yan Li, Punit Shah, Angelo Michael Demarzo, Jennifer E. Van Eyk, Qianqian Li, Daniel Wan-Yui Chan, Hui Zhang

Research output: Contribution to journalArticle

Abstract

Glycosylation is one of the most common protein modifications. Each glycoprotein can be glycosylated at multiple glycosites, and each glycosites can be modified by different glycans. Due to this heterogeneity of glycosylation, it has proven difficult to study the structure-function relationship of specific glycans and their affected glycoproteins. Here, we report a novel method for rapid and quantitative identification of glycoproteins containing specific glycans. Lectin affinity isolations are followed by chemical immobilization of the captured glycopeptides, allowing the identification of glycoproteins containing specific glycans by subsequent mass spectrometry. The application of the method should be useful to facilitate our understanding of how changes in glycan associate with diseases, and to discover novel glycoproteins with certain glycans that could serve as biomarkers or therapeutic targets.

Original languageEnglish (US)
Pages (from-to)4683-4687
Number of pages5
JournalAnalytical Chemistry
Volume87
Issue number9
DOIs
StatePublished - May 5 2015

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Lectins
Polysaccharides
Glycoproteins
Glycosylation
Glycopeptides
Biomarkers
Mass spectrometry
Proteins

ASJC Scopus subject areas

  • Analytical Chemistry

Cite this

Identification of glycoproteins containing specific glycans using a lectin-chemical method. / Li, Yan; Shah, Punit; Demarzo, Angelo Michael; Van Eyk, Jennifer E.; Li, Qianqian; Chan, Daniel Wan-Yui; Zhang, Hui.

In: Analytical Chemistry, Vol. 87, No. 9, 05.05.2015, p. 4683-4687.

Research output: Contribution to journalArticle

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