pubmed-article:1823160 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1823160 | lifeskim:mentions | umls-concept:C0025202 | lld:lifeskim |
pubmed-article:1823160 | lifeskim:mentions | umls-concept:C0032143 | lld:lifeskim |
pubmed-article:1823160 | lifeskim:mentions | umls-concept:C0028959 | lld:lifeskim |
pubmed-article:1823160 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:1823160 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
pubmed-article:1823160 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:1823160 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:1823160 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:1823160 | pubmed:dateCreated | 1992-9-21 | lld:pubmed |
pubmed-article:1823160 | pubmed:abstractText | We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA). These studies have confirmed the published structures for rt-PA, but are not in agreement with some of the structures reported for mt-PA. In the latter glycoprotein we have identified a novel structure as the major oligosaccharide attached to Asn-184 and Asn-448. This is a biantennary oligosaccharide consisting of a fucosylated trimannosyl core to which are attached two GalNAc(1----4)GlcNAc antennae, one of which carries a sialic acid linked at the 6-position of the GalNAc. Minor constituents are sialylated on both or neither antennae. The sialylated GalNAc moiety is unique in N-linked glycoproteins. The majority of complex structures in rmt-PA contain N-acetyllactosamine moieties at both the Asn-184 and Asn-448 sites with the novel oligosaccharide occurring as a minor component at the Asn-184 site. This study demonstrates the power of mass spectrometric strategies based on high-field two-sector FAB-MS for structure elucidations of natural and recombinant glycoproteins. | lld:pubmed |
pubmed-article:1823160 | pubmed:language | eng | lld:pubmed |
pubmed-article:1823160 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1823160 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1823160 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1823160 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1823160 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1823160 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1823160 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1823160 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1823160 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1823160 | pubmed:month | Mar | lld:pubmed |
pubmed-article:1823160 | pubmed:issn | 0959-6658 | lld:pubmed |
pubmed-article:1823160 | pubmed:author | pubmed-author:MorrisH RHR | lld:pubmed |
pubmed-article:1823160 | pubmed:author | pubmed-author:RogersM EME | lld:pubmed |
pubmed-article:1823160 | pubmed:author | pubmed-author:DellAA | lld:pubmed |
pubmed-article:1823160 | pubmed:author | pubmed-author:GaffneyPP | lld:pubmed |
pubmed-article:1823160 | pubmed:author | pubmed-author:EtienneA TAT | lld:pubmed |
pubmed-article:1823160 | pubmed:author | pubmed-author:PanicoMM | lld:pubmed |
pubmed-article:1823160 | pubmed:author | pubmed-author:ChanA LAL | lld:pubmed |
pubmed-article:1823160 | pubmed:author | pubmed-author:Creighton-Kem... | lld:pubmed |
pubmed-article:1823160 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1823160 | pubmed:volume | 1 | lld:pubmed |
pubmed-article:1823160 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1823160 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1823160 | pubmed:pagination | 173-85 | lld:pubmed |
pubmed-article:1823160 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:1823160 | pubmed:meshHeading | pubmed-meshheading:1823160-... | lld:pubmed |
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pubmed-article:1823160 | pubmed:year | 1991 | lld:pubmed |
pubmed-article:1823160 | pubmed:articleTitle | A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator. | lld:pubmed |
pubmed-article:1823160 | pubmed:affiliation | Department of Biochemistry, Imperial College of Science Technology and Medicine, London, UK. | lld:pubmed |
pubmed-article:1823160 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1823160 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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