| pubmed-article:6325180 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6325180 | lifeskim:mentions | umls-concept:C0019185 | lld:lifeskim |
| pubmed-article:6325180 | lifeskim:mentions | umls-concept:C0007004 | lld:lifeskim |
| pubmed-article:6325180 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
| pubmed-article:6325180 | lifeskim:mentions | umls-concept:C0028959 | lld:lifeskim |
| pubmed-article:6325180 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:6325180 | lifeskim:mentions | umls-concept:C1704666 | lld:lifeskim |
| pubmed-article:6325180 | lifeskim:mentions | umls-concept:C1517892 | lld:lifeskim |
| pubmed-article:6325180 | lifeskim:mentions | umls-concept:C0208973 | lld:lifeskim |
| pubmed-article:6325180 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:6325180 | pubmed:dateCreated | 1984-6-20 | lld:pubmed |
| pubmed-article:6325180 | pubmed:abstractText | Two size classes of O-glycosidically linked oligosaccharides were liberated from glycoprotein E1 of mouse hepatitis virus (MHV) A59 by reductive beta-elimination and separated by h.p.l.c. The structures of the reduced oligosaccharides were determined by successive exoglycosidase digestions and by methylation analyses involving combined capillary gas chromatography-mass spectrometry and mass fragmentography after chemical ionization with ammonia. Oligosaccharide A (Neu5Ac alpha 2----3 Gal beta 1----3 GalNAc) comprised 35% of the total carbohydrate side chains, while the remaining 65% of the oligosaccharides of E1 had the branched structure B: Neu5Ac alpha 2----3 Gal beta 1----3 (Neu5Ac alpha 2----6) GalNAc. Both oligosaccharides were linked to the E1 polypeptide via N-acetylgalactosamine, and 20% of the sialic acids present in E1 glycopeptides were found to consist of N-acetyl-9-mono-O-acetylneuraminic acid. The reported structures of the O-linked glycans are discussed in the context of the amino acid sequence of E1, which exhibits a cluster of four hydroxyamino acids (Ser-Ser-Thr-Thr) as potential O-glycosylation sites at the amino terminus. Oligosaccharides with identical structures and an identical O-glycosylated tetrapeptide sequence are present in the blood group M-active glycophorin A of the human erythrocyte membrane. | lld:pubmed |
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| pubmed-article:6325180 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6325180 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6325180 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6325180 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6325180 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:6325180 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:6325180 | pubmed:author | pubmed-author:StirmSS | lld:pubmed |
| pubmed-article:6325180 | pubmed:author | pubmed-author:LinderDD | lld:pubmed |
| pubmed-article:6325180 | pubmed:author | pubmed-author:KlingD HDH | lld:pubmed |
| pubmed-article:6325180 | pubmed:author | pubmed-author:NiemannHH | lld:pubmed |
| pubmed-article:6325180 | pubmed:author | pubmed-author:WirthMM | lld:pubmed |
| pubmed-article:6325180 | pubmed:author | pubmed-author:GeyerRR | lld:pubmed |
| pubmed-article:6325180 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6325180 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:6325180 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6325180 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6325180 | pubmed:pagination | 665-70 | lld:pubmed |
| pubmed-article:6325180 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:6325180 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6325180 | pubmed:articleTitle | The carbohydrates of mouse hepatitis virus (MHV) A59: structures of the O-glycosidically linked oligosaccharides of glycoprotein E1. | lld:pubmed |
| pubmed-article:6325180 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6325180 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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