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Glycobiology ; 13(11): 749-54, 2003 Nov.
Article in English | MEDLINE | ID: mdl-12851287

ABSTRACT

In this study, we use a novel glycan array to analyze the glycan-binding antibody repertoire in a pool of affinity-purified IgG collected from a healthy human population. The glycan array used is based on mono- and oligosaccharides covalently linked to the surface via a long linker at their reducing ends. They are thus presented to the medium with a well-defined orientation and are accessible for specific binding by glycan-binding proteins, such as antibodies and lectins. A novel anticellulose antibody was detected that binds specifically to beta4-linked saccharides with a preference for glucopyranose over galactopyranose residues. We also found previously known antiglycan antibodies against mono- and oligosaccharides that are constituents of commonly occurring bacterial polysaccharides. We propose that this array can facilitate high-throughput screening of glycan-binding proteins and the search for biomarkers for personalized medicine.


Subject(s)
Cellulose/immunology , Immunoglobulin G/immunology , Molecular Probe Techniques , Polysaccharides/immunology , Antibody Specificity , Binding Sites , Humans , Immunoglobulin G/isolation & purification , Lectins/chemistry , Lectins/metabolism , Molecular Structure , Monosaccharides/metabolism , Oligosaccharides/metabolism , Protein Binding , Reproducibility of Results
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