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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
20
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pubmed:dateCreated |
1985-10-11
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pubmed:abstractText |
The biosynthesis of the major human red cell sialoglycoprotein, glycophorin A, was studied in the erythroleukemia cell line K562 with emphasis on O-glycosylation. The cells were pulse-chase labeled with [35S] methionine, and either directly immune precipitated with anti-glycophorin A antiserum or detergent-solubilized extracts first passed through columns containing the N-acetylgalactosamine-specific lectin from Helix pomatia or the glucose/mannose specific lectin from lentil beans. From the sugar-eluted fractions anti-glycophorin A antiserum was used to identify precursor molecules. After 5 min of labeling the first glycophorin A precursors were seen. The largest had an apparent molecular weight of 37,000, and bound to lentil lectin-Sepharose, but not to H. pomatia lectin-Sepharose. The lentil lectin-reactive glycophorin A molecules increased to Mr = 39,000 during chase and obtained sialic acids after 9 min of chase reflecting terminal N- and O-glycosylation. After 5-6 min of labeling two H. pomatia-interacting glycophorin A precursors with apparent molecular weights of 24,000 and 30,000 were obtained. These did not bind to lentil lectin-Sepharose. During chase also these molecules increased in size to Mr = 39,000. The immune precipitation of all antiglycophorin A-reactive precursor molecules was inhibited by purified red cell glycophorin A. The carboxylic ionophore, monensin, caused the accumulation of incompletely O-glycosylated glycophorin A molecules, which bound to H. pomatia lectin-Sepharose. These were degraded by treatment with endo-beta-N-acetylglucosaminidase H reflecting incomplete processing of the N-glycosidic oligosaccharide.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Glycophorin,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosides,
http://linkedlifedata.com/resource/pubmed/chemical/Methionine,
http://linkedlifedata.com/resource/pubmed/chemical/Sialoglycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfur Radioisotopes
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
260
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11314-21
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:3861610-Cell Line,
pubmed-meshheading:3861610-Chromatography, Affinity,
pubmed-meshheading:3861610-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:3861610-Erythrocyte Membrane,
pubmed-meshheading:3861610-Glycophorin,
pubmed-meshheading:3861610-Glycoside Hydrolases,
pubmed-meshheading:3861610-Glycosides,
pubmed-meshheading:3861610-Humans,
pubmed-meshheading:3861610-Leukemia, Myeloid,
pubmed-meshheading:3861610-Methionine,
pubmed-meshheading:3861610-Sialoglycoproteins,
pubmed-meshheading:3861610-Sulfur Radioisotopes
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pubmed:year |
1985
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pubmed:articleTitle |
Biosynthesis of the major human red cell sialoglycoprotein, glycophorin A. O-Glycosylation.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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