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Oligosaccharide Assembly

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...

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Related Experiment Video

Updated: Apr 27, 2026

Improved In-gel Reductive β-Elimination for Comprehensive O-linked and Sulfo-glycomics by Mass Spectrometry

Improved In-gel Reductive β-Elimination for Comprehensive O-linked and Sulfo-glycomics by Mass Spectrometry

Published on: November 20, 2014

Development and Application of Multidimensional HPLC Mapping Method for O-linked Oligosaccharides.

Hirokazu Yagi¹, Erina Ohno², Sachiko Kondo³

¹Graduate School of Pharmaceutical Science, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan. hyagi@phar.nagoya-cu.ac.jp.

|June 28, 2014

Summary

Researchers developed a new HPLC mapping method for detailed O-glycan structure identification. This method enables quantitative analysis of O-glycosylation profiles, advancing glycomic research.

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Sequencing of Plant Wall Heteroxylans Using Enzymic, Chemical Methylation and Physical Mass Spectrometry, Nuclear Magnetic Resonance Techniques

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Published on: March 24, 2016

Area of Science:

Biochemistry
Glycobiology
Analytical Chemistry

Background:

Glycosylation is crucial for protein function, stability, and cell interactions.
N-glycosylation analysis is well-established, but O-glycosylation profiling remains challenging due to a lack of standardized methods.
Detailed characterization of glycan structures is essential for understanding their molecular mechanisms.

Purpose of the Study:

To develop a standardized HPLC mapping method for detailed identification of O-glycans.
To enable quantitative analysis of O-glycosylation profiles, including neutral, sialylated, and sulfated structures.
To apply the method for analyzing O-glycosylation of serum IgA and in vitro enzymatic reactions.

Main Methods:

Development of a novel HPLC mapping technique for O-glycan analysis.
Quantitative identification of isomeric products from N-acetylglucosamine-6O-sulfotransferase reactions.
Application of the method to determine O-glycosylation profiles of serum IgA.

Main Results:

Successfully established an HPLC mapping method for comprehensive O-glycan identification.
Enabled quantitative analysis of neutral, sialylated, and sulfated O-glycans.
Provided detailed O-glycosylation profiles for serum IgA and characterized enzymatic reaction products.

Conclusions:

The developed HPLC method provides a robust platform for detailed O-glycan analysis.
This advancement facilitates quantitative O-glycosylation profiling, crucial for understanding biological roles.
The method is applicable to model glycoproteins and enzymatic studies, paving the way for broader glycomic applications.