The subsites of monoclonal anti-dextran IgA W3129.
Synthetic deoxyfluoro derivatives of methyl alpha-D-glucopyranoside, as well as methyl alpha-glycosides of isomalto-oligosaccharides, some having fluorine substituted for hydroxyl groups at selected positions, have been evaluated for their binding with a myeloma monoclonal IgA known to bind only to an oligosaccharide sequence at the nonreducing end of alpha-(1----6)-linked D-glucopyranans (dextrans). The results are compatible with the antibody's possessing one subsite of high affinity for its D-glucosyl group, the remaining three subsites having low affinities for their respective D-glucosyl residues. The high-affinity antibody-subsite occurs at the interior end of the sequence of four subsites, appears to be relatively accessible, and binds the (terminal) nonreducing D-glucosyl group of the oligosaccharidic determinant using two, and possibly three, hydroxyl groups in hydrogen bonding.
Glaudemans
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CP
National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
Kovác
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P
Rao
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AS
D000911:Antibodies, Monoclonal / Q000032:analysis*; D001666:Binding Sites, Antibody; D001667:Binding, Competitive; D002240:Carbohydrate Sequence; D004247:DNA; D003911:Dextrans / Q000276:immunology*; D000939:Epitopes / Q000032:analysis; D006860:Hydrogen Bonding; D007070:Immunoglobulin A / Q000032:analysis*; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000276:immunology
D000911:Antibodies, Monoclonal; D003911:Dextrans; D000939:Epitopes; D007070:Immunoglobulin A; D009844:Oligosaccharides; D004247:DNA