Abstract：
:The carbohydrate binding specificity of the basic lectin from winged bean (Psophocarpus tetragonolobus) was investigated by quantitative precipitin analysis using blood group A, B, H, Le and I substances and by precipitation inhibition with various mono- and oligosaccharides. The lectin precipitated best with A1 substances and moderately with B and A2 substances, but not with H or Le substances. Inhibition assays of lectin-blood group A1 precipitation demonstration that A substance-derived oligosaccharides having the common structure: D-GalNAc alpha(1----3)D-Gal-(beta 1----3/4) to a D-Glc, were the best inhibitors and about 8 and 4 times more active than D-GalNAc and D-GalNAc alpha(1----3)D-Gal, respectively. A difucosyl A-specific oligosaccharide (A-penta), a monofucosyl (A-tetra) and a non-fucosyl containing (A5II) oligosaccharide, D-GalNAc alpha(1----3)D-Gal beta(1----3)D-GlcNAc, had almost the same reactivity, suggesting that the fucose linked to the sub-terminal D-Gal or to the third sugar. D-GlcNAc, from the non-reducing end made no contribution to the carbohydrate binding. Although a terminal non-reducing D-GalNAc or D-Gal residue was indispensible for binding, the lectin bound not only to these terminal non-reducing galactopyranosyl residues, but also showed increased binding to oligosaccharides in which it was bonded to a sub-terminal D-Gal joined to a D-GlcNAc residue, as in blood group A or B substances. This defines the site, thus far, as complementary to a disaccharide plus the beta linkage to the third sugar (D-Glc or D-GlcNAc) from the non-reducing end. The role of the beta(1----3) or beta(1----4) linkage of the sub-terminal non-reducing D-Gal to the D-GlcNAc requires further study.
journal_name
Mol Immunoljournal_title
Molecular immunologyauthors
Matsuda T,Kabat EA,Surolia Adoi
10.1016/0161-5890(89)90101-6subject
Has Abstractpub_date
1989-02-01 00:00:00pages
189-95issue
2eissn
0161-5890issn
1872-9142journal_volume
26pub_type
杂志文章abstract：BACKGROUND:Allergen epitope characterization provides valuable information useful for the understanding of proteins as food allergens. It is believed that IgE epitopes in general are conformational, nevertheless, for food allergens known to sensitize through the gastrointestinal tract linear epitopes have been suggeste...
journal_title：Molecular immunology
pub_type： 杂志文章
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journal_title：Molecular immunology
pub_type： 杂志文章
doi：10.1016/j.molimm.2008.01.014
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pub_type： 杂志文章
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更新日期：2007-03-01 00:00:00
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pub_type： 杂志文章
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更新日期：1988-04-01 00:00:00
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pub_type： 杂志文章
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更新日期：2011-09-01 00:00:00
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pub_type： 杂志文章
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更新日期：2015-02-01 00:00:00
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pub_type： 杂志文章
doi：10.1016/j.molimm.2005.07.030
更新日期：2006-03-01 00:00:00
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pub_type： 杂志文章
doi：10.1016/j.molimm.2006.09.034
更新日期：2007-03-01 00:00:00
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pub_type： 杂志文章
doi：10.1016/0161-5890(93)90040-i
更新日期：1993-10-01 00:00:00
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journal_title：Molecular immunology
pub_type： 杂志文章,评审
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更新日期：2015-12-01 00:00:00
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pub_type： 杂志文章
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更新日期：1993-05-01 00:00:00
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pub_type： 杂志文章
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更新日期：1995-12-01 00:00:00
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pub_type： 杂志文章
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pub_type： 杂志文章
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更新日期：2016-09-01 00:00:00
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journal_title：Molecular immunology
pub_type： 杂志文章
doi：10.1016/0161-5890(84)90074-9
更新日期：1984-03-01 00:00:00
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更新日期：2003-06-01 00:00:00
