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rdf:type |
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lifeskim:mentions |
umls-concept:C0007589,
umls-concept:C0025914,
umls-concept:C0026809,
umls-concept:C0032594,
umls-concept:C0039194,
umls-concept:C0076570,
umls-concept:C0205307,
umls-concept:C0205384,
umls-concept:C0392747,
umls-concept:C0443172,
umls-concept:C0872366,
umls-concept:C1511938
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pubmed:issue |
2
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pubmed:dateCreated |
1985-5-24
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pubmed:abstractText |
The glycans of the Thy-1 antigen present on thymocytes and lymph-node T-lymphocytes were investigated after external labelling of the cells. Neuraminidase, endoglycosidase H and endoglycosidase F were used in combination with sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and isoelectric focusing in order to characterize the nature of the glycans on 125I-labelled and immunoprecipitated Thy-1. Glycopeptides were prepared from Thy-1 obtained from cells labelled by periodate/boro[3H]hydride treatment. The glycopeptides were separated by affinity chromatography on concanavalin A-Sepharose and analysed by gel filtration. The results show that both types of cells possess Thy-1 molecules with three N-linked carbohydrate chains, of which one is of 'high-mannose' type and the other two of triantennary and biantennary 'complex' type. The ratio of triantennary/biantennary chains was decreased on Thy-1 of mature cells compared with that of immature cells, but instead more sialic acid was present on these chains. Deglycosylated Thy-1 appeared to be of the same size regardless of origin, indicating that only the carbohydrate moiety differs between Thy-1 molecules of the two cell types.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2859851-199169,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2859851-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2859851-6118137,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2859851-6121705,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2859851-6124286,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2859851-6131921,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2859851-6136268,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2859851-6148073,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2859851-6177036,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2859851-62678,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2859851-6812050,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2859851-69628,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2859851-6965519
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
226
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
519-25
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2859851-Animals,
pubmed-meshheading:2859851-Antigens, Surface,
pubmed-meshheading:2859851-Antigens, Thy-1,
pubmed-meshheading:2859851-Cell Differentiation,
pubmed-meshheading:2859851-Chromatography, Gel,
pubmed-meshheading:2859851-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2859851-Glycopeptides,
pubmed-meshheading:2859851-Glycoside Hydrolases,
pubmed-meshheading:2859851-Isoelectric Focusing,
pubmed-meshheading:2859851-Mice,
pubmed-meshheading:2859851-Mice, Inbred C3H,
pubmed-meshheading:2859851-N-Acetylneuraminic Acid,
pubmed-meshheading:2859851-Polysaccharides,
pubmed-meshheading:2859851-Sialic Acids,
pubmed-meshheading:2859851-T-Lymphocytes,
pubmed-meshheading:2859851-Thymus Gland
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pubmed:year |
1985
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pubmed:articleTitle |
Changes in glycan branching and sialylation of the Thy-1 antigen during normal differentiation of mouse T-lymphocytes.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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