Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
91
|
| pubmed:dateCreated |
1992-10-13
|
| 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.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/poly-N-acetyllactosamine
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0301-0457
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
67-77
|
| pubmed:dateRevised |
2010-11-18
|
| pubmed:meshHeading |
pubmed-meshheading:1524573-Amino Acids,
pubmed-meshheading:1524573-B-Lymphocytes,
pubmed-meshheading:1524573-Carbohydrate Sequence,
pubmed-meshheading:1524573-Chromatography, Gel,
pubmed-meshheading:1524573-Chromatography, Ion Exchange,
pubmed-meshheading:1524573-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1524573-Eukaryota,
pubmed-meshheading:1524573-Glycoproteins,
pubmed-meshheading:1524573-Hemadsorption,
pubmed-meshheading:1524573-Hemagglutination,
pubmed-meshheading:1524573-Hemagglutination Inhibition Tests,
pubmed-meshheading:1524573-Humans,
pubmed-meshheading:1524573-Lectins,
pubmed-meshheading:1524573-Lymphocyte Activation,
pubmed-meshheading:1524573-Molecular Sequence Data,
pubmed-meshheading:1524573-Molecular Weight,
pubmed-meshheading:1524573-Oligosaccharides,
pubmed-meshheading:1524573-Polysaccharides,
pubmed-meshheading:1524573-T-Lymphocytes
|
| pubmed:year |
1992
|
| pubmed:articleTitle |
The lectin from the algae Udotea petiolata: isolation, characterization and sugar binding properties.
|
| pubmed:affiliation |
Institut für Immunobiologie, Universitätsklinik Köln, Germany.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|