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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1989-4-14
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pubmed:abstractText |
The trypsin-sensitive glycopeptides from cell surfaces of a multipotential murine haemopoietic cell line (DE) have been studied using serial lectin affinity chromatography on columns of immobilized lentil lectin (LCA), concanavalin A (Con A), and wheat-germ agglutinin (WGA). WGA-binding material consisted of glycopeptides that failed to bind to LCA and Con A. Step elution from the WGA-column with 0.01-, 0.1-, 0.5- and 1.0 M N-acetyl-D-glucosamine yielded four affinity classes of glycopeptide (WGA-W, WGA-I, WGA-S and WGA-SS respectively). WGA-W, WGA-I and WGA-S contained both alkali-stable (N-linked) and alkali-labile (O-linked) carbohydrate on high molecular weight glycopeptides. The WGA-SS fraction contained only N-linked carbohydrate. N-linked glycopeptides isolated from each WGA-binding class differed in molecular size, relative N-acetylneuraminic acid content and affinity for Ricinus communis 120 agglutinin. endo-beta-Galactosidase digestion showed that these glycopeptides contained polylactosamine-type glycans. Gel filtration profiles of the enzyme treated materials were different for each WGA-binding population suggesting variation in branching patterns and/or substitution with fucose residues. Affinity chromatography has shown that the WGA binding molecules are the major glycopeptide group at DE cell surfaces.
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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/Amino Sugars,
http://linkedlifedata.com/resource/pubmed/chemical/Glycopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Mitogen,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Galactosidase,
http://linkedlifedata.com/resource/pubmed/chemical/keratan-sulfate...,
http://linkedlifedata.com/resource/pubmed/chemical/lactosamine,
http://linkedlifedata.com/resource/pubmed/chemical/wheat germ agglutinin receptor
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0269-3879
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
41-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3147728-Amino Sugars,
pubmed-meshheading:3147728-Animals,
pubmed-meshheading:3147728-Cells, Cultured,
pubmed-meshheading:3147728-Chromatography, Affinity,
pubmed-meshheading:3147728-Glycopeptides,
pubmed-meshheading:3147728-Glycoside Hydrolases,
pubmed-meshheading:3147728-Hematopoietic Stem Cells,
pubmed-meshheading:3147728-Lectins,
pubmed-meshheading:3147728-Mice,
pubmed-meshheading:3147728-Receptors, Mitogen,
pubmed-meshheading:3147728-beta-Galactosidase
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pubmed:year |
1986
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pubmed:articleTitle |
Combined use of lectin affinity chromatography and endo-beta-galactosidase to study polylactosamine sequences isolated from haemopoietic cell surfaces.
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pubmed:affiliation |
Cancer Research Campaign Department of Medical Oncology, Christie Hospital, Withington, Manchester, U.K.
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pubmed:publicationType |
Journal Article
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