Document Detail


An analytical and structural database provides a strategy for sequencing O-glycans from microgram quantities of glycoproteins.
MedLine Citation:
PMID:  11969191     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A sensitive, rapid, quantitative strategy has been developed for O-glycan analysis. A structural database has been constructed that currently contains analytical parameters for more than 50 glycans, enabling identification of O-glycans at the subpicomole level. The database contains the structure, molecular weight, and both normal and reversed-phase HPLC elution positions for each glycan. These observed parameters reflect the mass, three-dimensional shape, and hydrophobicity of the glycans and, therefore, provide information relating to linkage and arm specificity as well as monosaccharide composition. Initially the database was constructed by analyzing glycans released by mild hydrazinolysis from bovine serum fetuin, synthetic glycopeptides, human glycophorin A, and serum IgA1. The structures of the fluorescently labeled sugars were determined from a combination of HPLC data, mass spectrometric composition and mass fragmentation data, and exoglycosidase digestions. This approach was then applied to human neutrophil gelatinase B and secretory IgA, where 18 and 25 O-glycans were identified, respectively, and the parameters of these glycans were added to the database. This approach provides a basis for the analysis of subpicomole quantities of O-glycans from normal levels of natural glycoproteins.
Authors:
Louise Royle; Taj S Mattu; Edmund Hart; James I Langridge; Anthony H Merry; Neil Murphy; David J Harvey; Raymond A Dwek; Pauline M Rudd
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Analytical biochemistry     Volume:  304     ISSN:  0003-2697     ISO Abbreviation:  Anal. Biochem.     Publication Date:  2002 May 
Date Detail:
Created Date:  2002-04-23     Completed Date:  2002-10-02     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0370535     Medline TA:  Anal Biochem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  70-90     Citation Subset:  IM    
Copyright Information:
(c)2002 Elsevier Science (USA).
Affiliation:
Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, United Kingdom.
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MeSH Terms
Descriptor/Qualifier:
Animals
Carbohydrate Sequence
Cattle
Chromatography, High Pressure Liquid / methods,  statistics & numerical data
Databases, Factual
Glycopeptides / chemistry
Glycophorin / chemistry
Glycoproteins / chemistry*
Humans
Immunoglobulin A / chemistry
Immunoglobulin A, Secretory / chemistry
Mass Spectrometry / methods
Matrix Metalloproteinase 9 / chemistry
Microchemistry
Molecular Sequence Data
Polysaccharides / chemistry*
Reproducibility of Results
Sensitivity and Specificity
Sequence Analysis / methods*,  statistics & numerical data
alpha-Fetoproteins / chemistry
Chemical
Reg. No./Substance:
0/Glycopeptides; 0/Glycophorin; 0/Glycoproteins; 0/Immunoglobulin A; 0/Immunoglobulin A, Secretory; 0/Polysaccharides; 0/alpha-Fetoproteins; EC 3.4.24.35/Matrix Metalloproteinase 9

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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