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Progress in Chemistry 2009, Vol. 21 Issue (09): 1888-1894 Previous Articles   Next Articles

• Review •

Separation and Enrichment of Glycoproteins/Glycopeptides

Cao Jing1,2; |Nie Aiying2; |Chen Yaohan2; |Wang Sheng1; |Lu Haojie1,2; |Yang Pengyuan1,2**   

  1. (1.Department of Chemistry, Fudan University, Shanghai 200433, China|2.Institutes of Biomedical Sciences, Fudan University, Shanghai 200032, China)
  • Received: Revised: Online: Published:
  • Contact: Yang Pengyuan E-mail:pyyang@fudan.edu.cn
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Protein glycosylation as an important post-translational modifications has a significant effect on the structures and functions of proteins.As a section of proteomics, glycoproteomics is in the spotlight currently, and the efficient separation and enrichment of glycoproteins/glycopeptides from complex biological samples is the key and difficult point of glycoproteome research. In this paper, the progress in methods for the separation and enrichment of glycoproteins/glycopeptides and their applications are overviewed. These methodologies not only include most-often-used methods such as lectin-based affinity chromatography, boronic acid method, hydrazide chemistry and hydrophilic chromatography, but also some novel methods, for example, size exclusion chromatography and strong cation exchange enrichment.

Contents
1 Introduction
2 Types and current research status of protein glycosylation
3 Methods for separation and enrichment of glycoproteins/glycopeptides and their applications
3.1 Lectin affinity chromatography
3.2 Boronic acid method
3.3 Hydrazide chemistry
3.4 Hydrophilic chromatography
3.5 Other methods
4 Conclusion

CLC Number: 

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