| pubmed-article:2458714 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2458714 | lifeskim:mentions | umls-concept:C0996854 | lld:lifeskim |
| pubmed-article:2458714 | lifeskim:mentions | umls-concept:C0001128 | lld:lifeskim |
| pubmed-article:2458714 | lifeskim:mentions | umls-concept:C0023206 | lld:lifeskim |
| pubmed-article:2458714 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:2458714 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:2458714 | pubmed:dateCreated | 1988-10-19 | lld:pubmed |
| pubmed-article:2458714 | pubmed:abstractText | An acidic lectin (WBA II) was isolated to homogeneity from the crude seed extract of the winged bean (Psophocarpus tetragonolobus) by affinity chromatography on lactosylaminoethyl-Bio-Gel. Binding of WBA II to human erythrocytes of type-A, -B and -O blood groups showed the presence of 10(5) receptors/cell, with high association constants (10(6)-10(8) M-1). Competitive binding studies with blood-group-specific lectins reveal that WBA II binds to H- and T-antigenic determinants on human erythrocytes. Affinity-chromatographic studies using A-, B-, H- and T-antigenic determinants coupled to an insoluble matrix confirm the specificity of WBA II towards H- and T-antigenic determinants. Inhibition of the binding of WBA II by various sugars show that N-acetylgalactosamine and T-antigenic disaccharide (Thomsen-Friedenreich antigen, Gal beta 1-3GalNAc) are the most potent mono- and di-saccharide inhibitors respectively. In addition, inhibition of the binding of WBA II to erythrocytes by dog intestine H-fucolipid prove that the lectin binds to H-antigenic determinant. | lld:pubmed |
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| pubmed-article:2458714 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2458714 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2458714 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2458714 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2458714 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:2458714 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:2458714 | pubmed:author | pubmed-author:SuroliaAA | lld:pubmed |
| pubmed-article:2458714 | pubmed:author | pubmed-author:SajjanS USU | lld:pubmed |
| pubmed-article:2458714 | pubmed:author | pubmed-author:PatanjaliS... | lld:pubmed |
| pubmed-article:2458714 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2458714 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:2458714 | pubmed:volume | 252 | lld:pubmed |
| pubmed-article:2458714 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2458714 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2458714 | pubmed:pagination | 625-31 | lld:pubmed |
| pubmed-article:2458714 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2458714 | pubmed:meshHeading | pubmed-meshheading:2458714-... | lld:pubmed |
| pubmed-article:2458714 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:2458714 | pubmed:articleTitle | Erythrocyte-binding studies on an acidic lectin from winged bean (Psophocarpus tetragonolobus). | lld:pubmed |
| pubmed-article:2458714 | pubmed:affiliation | UGC Centre for Advanced Studies, Indian Institute of Science, Bangalore. | lld:pubmed |
| pubmed-article:2458714 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2458714 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:2458714 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
