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

作者信息

Wang J, Kovác P, Sinaÿ P, Glaudemans C P

机构信息

Laboratory of Medicinal Chemistry, National Institutes of Health, Bethesda, MD 20892, USA.

出版信息

Carbohydr Res. 1998 Mar;308(1-2):191-3. doi: 10.1016/s0008-6215(98)00071-8.

DOI:10.1016/s0008-6215(98)00071-8
PMID:9675360
Abstract

The binding of three monoclonal antigalactan immunoglobulins, IgAs X24, J539 and X44 to their natural haptens methyl beta-D-galactopyranosyl-(1-->6)-beta-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.

摘要

相似文献

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Synthetic C-oligosaccharides mimic their natural, analogous immunodeterminants in binding to three monoclonal immunoglobulins.
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Monoclonal IgA J539 binds galactopyranosyl antigens on its surface.单克隆IgA J539在其表面结合吡喃半乳糖基抗原。
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Probing the combining site of monoclonal IgA J539 using deoxyfluoro- and other galactosides as ligands.使用脱氧氟化物和其他半乳糖苷作为配体探究单克隆IgA J539的结合位点。
Mol Immunol. 1985 Jun;22(6):651-3. doi: 10.1016/0161-5890(85)90094-x.

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