Development and Application of Multidimensional HPLC Mapping Method for O-linked Oligosaccharides.
Biomolecules
; 1(1): 48-62, 2011 Dec 14.
Article
en En
| MEDLINE
| ID: mdl-24970123
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.
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Colección:
01-internacional
Base de datos:
MEDLINE
Idioma:
En
Revista:
Biomolecules
Año:
2011
Tipo del documento:
Article
País de afiliación:
Japón