pubmed-article:1524573 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1524573 | lifeskim:mentions | umls-concept:C0002028 | lld:lifeskim |
pubmed-article:1524573 | lifeskim:mentions | umls-concept:C1197920 | lld:lifeskim |
pubmed-article:1524573 | lifeskim:mentions | umls-concept:C0023206 | lld:lifeskim |
pubmed-article:1524573 | lifeskim:mentions | umls-concept:C0204727 | lld:lifeskim |
pubmed-article:1524573 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
pubmed-article:1524573 | lifeskim:mentions | umls-concept:C1148586 | lld:lifeskim |
pubmed-article:1524573 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:1524573 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
pubmed-article:1524573 | pubmed:issue | 91 | lld:pubmed |
pubmed-article:1524573 | pubmed:dateCreated | 1992-10-13 | lld:pubmed |
pubmed-article:1524573 | pubmed:abstractText | In the present work, we describe a novel lectin which is specific for poly-N-acetyllactosamine sequences on complex N- and O-linked carbohydrate chains. This lectin was extracted and purified from the algae Udotea petiolata. The purified lectin is a monomer with a molecular mass of 65,000 and an isoelectric point of 5.6. It agglutinates normal, neuraminidase and protease-treated erythrocytes from humans irrespectively of the blood group (A, B and O) and animal erythrocytes. The Udotea lectin displays a strong mitogenic effect on human lymphocytes, especially T-cells. This lectin binds to the human serum plasma protein 8S alpha 3-glycoprotein with high affinity (ID50 0.02 microM); other species of human serum glycoproteins exhibiting a similar preponderance of complex type N-glycosylation showed also high binding capacities in the order 9.5 S alpha 1-glycoprotein greater than alpha 2-macroglobulin = beta 2 glycoprotein = immunoglobulin A greater than asialofetuin greater than alpha 1-acid glycoprotein and mucin glycopeptide (from amnion fluid). Monosaccharides and disaccharides tested do not bind to the lectin. This novel lectin will be useful for identification of N- and O-linked glycans rich in poly-N-acetyllactosamine. | lld:pubmed |
pubmed-article:1524573 | pubmed:language | eng | lld:pubmed |
pubmed-article:1524573 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1524573 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1524573 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1524573 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1524573 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1524573 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1524573 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1524573 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1524573 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1524573 | pubmed:month | Apr | lld:pubmed |
pubmed-article:1524573 | pubmed:issn | 0301-0457 | lld:pubmed |
pubmed-article:1524573 | pubmed:author | pubmed-author:MüllerW EWE | lld:pubmed |
pubmed-article:1524573 | pubmed:author | pubmed-author:UhlenbruckGG | lld:pubmed |
pubmed-article:1524573 | pubmed:author | pubmed-author:SchröderH CHC | lld:pubmed |
pubmed-article:1524573 | pubmed:author | pubmed-author:HanischF GFG | lld:pubmed |
pubmed-article:1524573 | pubmed:author | pubmed-author:KljajicZZ | lld:pubmed |
pubmed-article:1524573 | pubmed:author | pubmed-author:PoznanovicSS | lld:pubmed |
pubmed-article:1524573 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1524573 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1524573 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1524573 | pubmed:pagination | 67-77 | lld:pubmed |
pubmed-article:1524573 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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pubmed-article:1524573 | pubmed:year | 1992 | lld:pubmed |
pubmed-article:1524573 | pubmed:articleTitle | The lectin from the algae Udotea petiolata: isolation, characterization and sugar binding properties. | lld:pubmed |
pubmed-article:1524573 | pubmed:affiliation | Institut für Immunobiologie, Universitätsklinik Köln, Germany. | lld:pubmed |
pubmed-article:1524573 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1524573 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |