pubmed-article:3122730 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3122730 | lifeskim:mentions | umls-concept:C0025914 | lld:lifeskim |
pubmed-article:3122730 | lifeskim:mentions | umls-concept:C0026809 | lld:lifeskim |
pubmed-article:3122730 | lifeskim:mentions | umls-concept:C0040679 | lld:lifeskim |
pubmed-article:3122730 | lifeskim:mentions | umls-concept:C0026131 | lld:lifeskim |
pubmed-article:3122730 | lifeskim:mentions | umls-concept:C0229671 | lld:lifeskim |
pubmed-article:3122730 | lifeskim:mentions | umls-concept:C0032594 | lld:lifeskim |
pubmed-article:3122730 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:3122730 | lifeskim:mentions | umls-concept:C0205225 | lld:lifeskim |
pubmed-article:3122730 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:3122730 | pubmed:dateCreated | 1988-2-4 | lld:pubmed |
pubmed-article:3122730 | pubmed:abstractText | A 'serotransferrin-like' protein was purified from mouse milk. This serotransferrin cross-reacts immunologically with the serotransferrin isolated from mouse plasma and not with the mouse lactotransferrin (lactoferrin). Sugar analysis of the three transferrins, i.e. serotransferrin, milk 'serotransferrin-like' protein and lactotransferrin, revealed that the major difference between the glycan primary structure of mouse serotransferrin and those of mouse milk 'serotransferrin-like' protein and lactotransferrin concerns essentially the presence of one fucose residue in the last two proteins. For structural determination, the N-glycosidically linked glycans were released from the protein by a reductive cleavage of the oligosaccharide-protein linkage under strong alkaline conditions. The primary structure of the released oligosaccharide alditols was determined by methylation analysis and 400 MHz 1H-n.m.r. spectroscopy. The oligosaccharide alditols released from milk 'serotransferrin-like' protein and lactotransferrin were identical and were identified as disialylated biantennary glycans of the N-acetyl-lactosamine type with a fucose residue alpha-1,6-linked to the N-acetylglucosamine residue conjugated to the peptide chain and having the following primary structure: NeuAc(alpha 2-6)Gal(beta 1-4)GlcNAc(beta 1-2)Man(alpha 1-3)[NeuAc(alpha 2-6)Gal(beta 1-4)GlcNAc(beta 1-2)Man(alpha 1-6)]Man(beta 1-4)GlcNAc(beta 1-4)[Fuc(alpha 1-6)]GlcNAc(beta 1-N)Asn. The serotransferrin glycan has the same primary structure but is only partially fucosylated (10-15%). | lld:pubmed |
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pubmed-article:3122730 | pubmed:language | eng | lld:pubmed |
pubmed-article:3122730 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3122730 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:3122730 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3122730 | pubmed:month | Nov | lld:pubmed |
pubmed-article:3122730 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:3122730 | pubmed:author | pubmed-author:MontreuilJJ | lld:pubmed |
pubmed-article:3122730 | pubmed:author | pubmed-author:SpikGG | lld:pubmed |
pubmed-article:3122730 | pubmed:author | pubmed-author:SawatzkiGG | lld:pubmed |
pubmed-article:3122730 | pubmed:author | pubmed-author:WieruszeskiJ... | lld:pubmed |
pubmed-article:3122730 | pubmed:author | pubmed-author:LeclercqYY | lld:pubmed |
pubmed-article:3122730 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3122730 | pubmed:day | 1 | lld:pubmed |
pubmed-article:3122730 | pubmed:volume | 247 | lld:pubmed |
pubmed-article:3122730 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3122730 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3122730 | pubmed:pagination | 571-8 | lld:pubmed |
pubmed-article:3122730 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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pubmed-article:3122730 | pubmed:year | 1987 | lld:pubmed |
pubmed-article:3122730 | pubmed:articleTitle | Primary structure of the glycans from mouse serum and milk transferrins. | lld:pubmed |
pubmed-article:3122730 | pubmed:affiliation | Laboratoire de Chimie Biologique de l'Université des Sciences et Techniques de Lille Flandres-Artois, Villeneuve d'Ascq, France. | lld:pubmed |
pubmed-article:3122730 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3122730 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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