| pubmed-article:6487322 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6487322 | lifeskim:mentions | umls-concept:C0036563 | lld:lifeskim |
| pubmed-article:6487322 | lifeskim:mentions | umls-concept:C0330792 | lld:lifeskim |
| pubmed-article:6487322 | lifeskim:mentions | umls-concept:C0005810 | lld:lifeskim |
| pubmed-article:6487322 | lifeskim:mentions | umls-concept:C0014792 | lld:lifeskim |
| pubmed-article:6487322 | lifeskim:mentions | umls-concept:C0600103 | lld:lifeskim |
| pubmed-article:6487322 | lifeskim:mentions | umls-concept:C1428349 | lld:lifeskim |
| pubmed-article:6487322 | lifeskim:mentions | umls-concept:C0001055 | lld:lifeskim |
| pubmed-article:6487322 | lifeskim:mentions | umls-concept:C0023206 | lld:lifeskim |
| pubmed-article:6487322 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:6487322 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
| pubmed-article:6487322 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:6487322 | pubmed:dateCreated | 1984-11-9 | lld:pubmed |
| pubmed-article:6487322 | pubmed:abstractText | We have previously shown that the B4 lectin from Vicia villosa seeds interacts with N-acetylgalactosamine alpha-linked to serine or threonine in cell surface glycoproteins. In the present study, we show that the lectin also binds to Cad erythrocytes (0.44-2.78 X 10(6) sites/cell) with an association constant of 0.61-0.84 X 10(7)M-1. Variability in the number of B4 lectin binding sites in Cad erythrocytes from different individuals parallels reactivity of these erythrocytes with other N-acetylgalactosamine-binding lectins. Agglutination of Cad erythrocytes with B4 lectin is inhibited by urinary Tamm-Horsfall Sda-active glycoprotein. Since the Cad and Sda determinants share the terminal GalNAc beta 1.4----Gal sequence, our results indicate that Vicia villosa B4 lectin can also interact with terminal beta-linked N-acetylgalactosamine in closely-spaced oligosaccharide units of cell surface glycoproteins. | lld:pubmed |
| pubmed-article:6487322 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6487322 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6487322 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6487322 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6487322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6487322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6487322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6487322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6487322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6487322 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6487322 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:6487322 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:6487322 | pubmed:author | pubmed-author:KornfeldRR | lld:pubmed |
| pubmed-article:6487322 | pubmed:author | pubmed-author:TollefsenS... | lld:pubmed |
| pubmed-article:6487322 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6487322 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:6487322 | pubmed:volume | 123 | lld:pubmed |
| pubmed-article:6487322 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6487322 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6487322 | pubmed:pagination | 1099-106 | lld:pubmed |
| pubmed-article:6487322 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:6487322 | pubmed:meshHeading | pubmed-meshheading:6487322-... | lld:pubmed |
| pubmed-article:6487322 | pubmed:meshHeading | pubmed-meshheading:6487322-... | lld:pubmed |
| pubmed-article:6487322 | pubmed:meshHeading | pubmed-meshheading:6487322-... | lld:pubmed |
| pubmed-article:6487322 | pubmed:meshHeading | pubmed-meshheading:6487322-... | lld:pubmed |
| pubmed-article:6487322 | pubmed:meshHeading | pubmed-meshheading:6487322-... | lld:pubmed |
| pubmed-article:6487322 | pubmed:meshHeading | pubmed-meshheading:6487322-... | lld:pubmed |
| pubmed-article:6487322 | pubmed:meshHeading | pubmed-meshheading:6487322-... | lld:pubmed |
| pubmed-article:6487322 | pubmed:meshHeading | pubmed-meshheading:6487322-... | lld:pubmed |
| pubmed-article:6487322 | pubmed:meshHeading | pubmed-meshheading:6487322-... | lld:pubmed |
| pubmed-article:6487322 | pubmed:meshHeading | pubmed-meshheading:6487322-... | lld:pubmed |
| pubmed-article:6487322 | pubmed:meshHeading | pubmed-meshheading:6487322-... | lld:pubmed |
| pubmed-article:6487322 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6487322 | pubmed:articleTitle | The B4 lectin from Vicia villosa seeds interacts with N-acetylgalactosamine residues on erythrocytes with blood group Cad specificity. | lld:pubmed |
| pubmed-article:6487322 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6487322 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
