Next Article in Journal / Special Issue
Exploring the Optimal Strategy to Predict Essential Genes in Microbes
Previous Article in Journal / Special Issue
Ursolic Acid Inhibits Na+/K+-ATPase Activity and Prevents TNF-α-Induced Gene Expression by Blocking Amino Acid Transport and Cellular Protein Synthesis
Article Menu

Export Article

Open AccessArticle
Biomolecules 2011, 1(1), 48-62; https://doi.org/10.3390/biom1010048

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

1
Graduate School of Pharmaceutical Science, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan
2
Graduate School of Medical Sciences and Medical School, Nagoya City University, Kawasumi-1, Mizuho-cho Mizuho-ku, Nagoya 467-8601, Japan
3
Institute for Molecular Science and Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, 5-1 Higashiyama Myodaiji, Okazaki 444-8787, Japan
4
GLYENCE Co., Ltd., 2-22-8 Chikusa, Chikusa-ku, Nagoya 464-0858, Japan
5
The Glycoscience Institute, Ochanomizu University, 2-1-1 Ohtsuka, Bunkyo-ku, Tokyo 112-8610, Japan
*
Author to whom correspondence should be addressed.
Received: 29 August 2011 / Revised: 30 November 2011 / Accepted: 5 December 2011 / Published: 14 December 2011
(This article belongs to the Special Issue Feature Papers)
View Full-Text   |   Download PDF [454 KB, uploaded 14 December 2011]   |  

Abstract

Glycosylation improves the solubility and stability of proteins, contributes to the structural integrity of protein functional sites, and mediates biomolecular recognition events involved in cell-cell communications and viral infections. The first step toward understanding the molecular mechanisms underlying these carbohydrate functionalities is a detailed characterization of glycan structures. Recently developed glycomic approaches have enabled comprehensive analyses of N-glycosylation profiles in a quantitative manner. However, there are only a few reports describing detailed O-glycosylation profiles primarily because of the lack of a widespread standard method to identify O-glycan structures. Here, we developed an HPLC mapping method for detailed identification of O-glycans including neutral, sialylated, and sulfated oligosaccharides. Furthermore, using this method, we were able to quantitatively identify isomeric products from an in vitro reaction catalyzed by N-acetylglucosamine-6O-sulfotransferases and obtain O-glycosylation profiles of serum IgA as a model glycoprotein. View Full-Text
Keywords: O-glycans; HPLC map; glycosylation profiling; sulfated oligosaccharide; IgA O-glycans; HPLC map; glycosylation profiling; sulfated oligosaccharide; IgA
Figures

Graphical abstract

This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

Share & Cite This Article

MDPI and ACS Style

Yagi, H.; Ohno, E.; Kondo, S.; Yoshida, A.; Kato, K. Development and Application of Multidimensional HPLC Mapping Method for O-linked Oligosaccharides. Biomolecules 2011, 1, 48-62.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Biomolecules EISSN 2218-273X Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top