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
Biomolecules 2011, 1(1), 48-62; doi:10.3390/biom1010048
Article

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

1
, 1
, 1,4
, 2
 and 1,3,4,5,*
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]   |   Browse Figures

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.
Keywords: O-glycans; HPLC map; glycosylation profiling; sulfated oligosaccharide; IgA O-glycans; HPLC map; glycosylation profiling; sulfated oligosaccharide; IgA
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Share & Cite This Article

Export to BibTeX |
EndNote


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.

View more citation formats

Related Articles

Article Metrics

Comments

Citing Articles

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