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A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples
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A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples

Published on: October 1, 2009

Glyco-catch method: A lectin affinity technique for glycoproteomics.

Jun Hirabayashi1, Tomomi Hashidate, Ken-ichi Kasai

  • 1Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Teikyo University, Sagamiko, Kanagawa, Japan. jun-hirabayashi@aist.go.jp

Journal of Biomolecular Techniques : JBT
|June 6, 2009
PubMed
Summary

The glyco-catch method comprehensively analyzes glycoproteins, aiding in understanding the biological roles of glycans in the genome-proteome-glycome era. This technique is valuable for identifying N-glycoproteins in complex biological samples.

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Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
09:54

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases

Published on: December 26, 2011

Area of Science:

  • Glycomics and Post-Translational Modifications
  • Systems Biology and Genomics

Background:

  • Protein glycosylation is a crucial post-translational modification impacting protein function.
  • Glycomics involves studying the entire set of glycans produced by an organism.
  • Understanding glycosylation is vital in the post-genome era for a holistic view of biological systems.

Purpose of the Study:

  • To review protein glycosylation issues and introduce the glyco-catch method.
  • To demonstrate the utility of glyco-catch for identifying glycoproteins.
  • To explore the concept of genome-proteome-glycome by analyzing glycosylation patterns.

Main Methods:

  • Development of the glyco-catch method, a novel affinity technique.
  • Integration of lectin affinity chromatography with in silico database searching.
  • Application of the method to identify N-glycoproteins in mouse liver using galectin-1.

Main Results:

  • The glyco-catch method enables systematic identification of glycoprotein genes and glycosylation sites.
  • Successful application in Caenorhabditis elegans demonstrated the method's practical validity.
  • Identification of complex-type N-glycoproteins in mouse liver captured by galectin-1.

Conclusions:

  • The glyco-catch method is a powerful tool for comprehensive glycoprotein analysis.
  • Accumulating glycosylation data across organisms will elucidate the biological meaning of glycans.
  • Future work includes technical improvements and glycome database construction.