Synthetic C-oligosaccharides mimic their natural, analogous immunodeterminants in binding to three monoclonal immunoglobulins

The binding of three monoclonal antigalactan immunoglobulins, IgAs X24, J539 and X44 to their natural haptens methyl β- d-galactopyranosyl-(1→6)- β- d-galactopyranoside, and the corresponding tri- and tetrasaccharides, was compared to the binding of these immunoglobulins with the comparable C-linked...

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Bibliographic Details
Published in:	Carbohydrate research Vol. 308; no. 1; pp. 191 - 193
Main Authors:	Wang, Jin, Kováč, Pavol, Sinaÿ, Pierre, Glaudemans, Cornelis P.J.
Format:	Journal Article
Language:	English
Published:	Netherlands Elsevier Ltd 01-03-1998
Subjects:	Antibodies, Monoclonal - immunology Antibodies, Monoclonal - metabolism Binding Binding Sites, Antibody Biological Sciences C-oligosaccharides Carbohydrate Sequence Haptens - immunology Hydrogen Bonding Immunoglobulin A - immunology Immunoglobulin A - metabolism Molecular Mimicry Molecular Sequence Data Monoclonal immunoglobulins Oligosaccharides - chemistry Oligosaccharides - immunology Oligosaccharides - metabolism Binding C-oligosaccharides Monoclonal immunoglobulins
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Summary:	The binding of three monoclonal antigalactan immunoglobulins, IgAs X24, J539 and X44 to their natural haptens methyl β- d-galactopyranosyl-(1→6)- β- d-galactopyranoside, and the corresponding tri- and tetrasaccharides, was compared to the binding of these immunoglobulins with the comparable C-linked oligosaccharide analogues 1– 3. The near identity of affinities of the two sets of oligosaccharides indicated the absence of any hydrogen bond involvement by the intersaccharidic oxygen atoms in the natural immunodeterminants.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0008-6215 1873-426X
DOI:	10.1016/S0008-6215(98)00071-8