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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1982-6-21
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pubmed:abstractText |
The Thy-1 glycoprotein of mouse thymocytes was analysed with regard to the properties of its carbohydrate part. Of the different lectins tested, partial binding of Thy-1 from membrane extracts was found to Lens culinaris agglutinin (approximately 50%) and wheat germ agglutinin (approximately 25%). In contrast, concanavalin A bound all Thy-1. The results indicate that there is considerable microheterogeneity in the oligosaccaride chains within the Thy-1 population. Thy-1 was purified from thymocyte membrane extracts by concanavalin A affinity chromatography and gel filtration. The purified preparation revealed, on analysis by isoelectric focusing, at least six charge variants (isoelectric points ranging from approximately 5-9). These variants were isolated, treated with neuraminidase and tested for lectin binding and isoelectric point. It was shown that the charge heterogeneity was due to different amounts of sialic acid; even the most basic form contained at least one sialic acid residue. Furthermore, it was concluded that the degree of sialylation was not correlated to the lectin-binding properties. Analysis of Thy-1 from surface 125I-labelled thymocytes showed that the purified preparation was representative in its complexity of the Thy-1 glycoprotein exposed on the surface membrane. The possible biological implications of the findings are discussed.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Thy-1,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neuraminidase,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Mitogen
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
123
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1-7
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:6121705-Animals,
pubmed-meshheading:6121705-Antigens, Surface,
pubmed-meshheading:6121705-Antigens, Thy-1,
pubmed-meshheading:6121705-Female,
pubmed-meshheading:6121705-Glycoproteins,
pubmed-meshheading:6121705-Isoelectric Focusing,
pubmed-meshheading:6121705-Male,
pubmed-meshheading:6121705-Membrane Proteins,
pubmed-meshheading:6121705-Mice,
pubmed-meshheading:6121705-Mice, Inbred C57BL,
pubmed-meshheading:6121705-Neuraminidase,
pubmed-meshheading:6121705-Oligosaccharides,
pubmed-meshheading:6121705-Receptors, Mitogen,
pubmed-meshheading:6121705-Thymus Gland
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pubmed:year |
1982
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pubmed:articleTitle |
Carbohydrate complexity of the mouse thymocyte Thy-1 glycoprotein as demonstrated by lectin affinity and isoelectric focusing.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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