Skip Navigation



Glycobiology Advance Access published online on January 21, 2004

Glycobiology, doi:10.1093/glycob/cwh034
This Article
Right arrow Advance Access manuscript (PDF) Freely available
Right arrow All Versions of this Article:
14/5/431    most recent
cwh034v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Nakano, M.
Right arrow Articles by Lee, Y. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nakano, M.
Right arrow Articles by Lee, Y. C.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Submitted on September 22, 2003
Revised on October 26, 2003
Accepted on November 14, 2003

© 2004 Oxford University Press

ORIGINAL ARTICLES

Detailed structural features of glycan chains derived from {alpha}1-acid glycoproteins of several different animals--The presence of hypersialylated, O-acetylated sialic acids but not disialy residues

Miyako Nakano 1, Kazuaki Kakehi 1*, Men-Hwei Tsai 2, and Yuan C. Lee 3

1 Faculty of Pharmaceutical Sciences, Kinki University, Kowakae 3-4-1, Higashi-Osaka 577-8502, Japan
2 Ambryx Biotechnology Inc., 5603D Foxwood Drive, Oak Park, CA 91377, USA
3 Biology Department, The Johns Hopkins University, North Charles Street, Baltimore, MD 21218, USA

* To whom correspondence should be addressed. E-mail: k_kakehi{at}phar.kindai.ac.jp.

Abstract

We analyzed carbohydrate chains of human, bovine, sheep and rat {alpha}1-acid glycoprotein (AGP), and found that carbohydrate chains of AGP of different animals showed quite distinct variations. Human AGP is a highly negatively-charged acidic glycoprotein (pKa = 2.6; isoelectic point = 2.7) with a molecular weight of approximately 37000 when examined by matrix-assisted laser-desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS), and contains di-, tri- and tetra-antennary carbohydrate chains. Some of the tri- and tetra-antennary carbohydrate chains are substituted with a fucose residue (sialyl Lewis X type structure). In sheep AGP, mono- and disialo-diantennary carbohydrate chains were abundant. Tri- and tetra-sialo triantennary carbohydrate chains were also present as minor oligosaccharides, and some of the sialic acid residues were substituted with N-glycolylneuraminic acid. In rat AGP, very complex mixture of disialo carbohydrate chains were observed. Complexity of the disialooligosaccharides was due to the presence of N, O-acetylneuraminic acids. Triantennary carbohydrate chains carrying N, O-acetylneuraminic acid were also observed as minor component oligosaccharides. We found some novel carbohydrate chains containing both N-acetylneuraminic acid and N-glycolylneuraminic acid in bovine AGP. Interestingly, triantennary carbohydrate chains were hardly detected in bovine AGP but diantennary carbohydrate chains with tri- or tetra-sialyl residues were abundant. Furthermore, the major sialic acid in these carbohydrate chains was N-glycolylneuraminic acid. It should be noted that these sialic acids are attached to multiple sites of the core oligosaccharide, and are not present as disialyl groups.


{alpha}1-acid glycoprotein, N-acetylneuraminic acid, N-glycolylneuraminic acid, HPLC, MALDI-TOF MS
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
GlycobiologyHome page
M. Nakano, D. Higo, E. Arai, T. Nakagawa, K. Kakehi, N. Taniguchi, and A. Kondo
Capillary electrophoresis-electrospray ionization mass spectrometry for rapid and sensitive N-glycan analysis of glycoproteins as 9-fluorenylmethyl derivatives
Glycobiology, February 1, 2009; 19(2): 135 - 143.
[Abstract] [Full Text] [PDF]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.