| pubmed-article:3085652 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3085652 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:3085652 | lifeskim:mentions | umls-concept:C0022646 | lld:lifeskim |
| pubmed-article:3085652 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
| pubmed-article:3085652 | lifeskim:mentions | umls-concept:C0085535 | lld:lifeskim |
| pubmed-article:3085652 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:3085652 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
| pubmed-article:3085652 | lifeskim:mentions | umls-concept:C1707455 | lld:lifeskim |
| pubmed-article:3085652 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:3085652 | lifeskim:mentions | umls-concept:C0332293 | lld:lifeskim |
| pubmed-article:3085652 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:3085652 | lifeskim:mentions | umls-concept:C0380154 | lld:lifeskim |
| pubmed-article:3085652 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:3085652 | pubmed:dateCreated | 1986-5-30 | lld:pubmed |
| pubmed-article:3085652 | pubmed:abstractText | Baby-hamster kidney (BHK) cells were grown continuously in long-term monolayer culture in the presence of Swainsonine, an inhibitor of alpha-mannosidase II, a processing enzyme involved in glycoprotein biosynthesis. The asparagine-linked oligosaccharides (N-glycans) were isolated from Pronase-digested cells by gel filtration, ion-exchange chromatography and affinity chromatography on concanavalin A--Sepharose and lentil lectin--Sepharose. The major N-glycans, analysed by 500 MHz 1H-n.m.r. spectroscopy, were identified as hybrid structures containing five mannose residues and neutral high-mannose N-glycans. The major hybrid species contained a core-substituted fucose alpha(1----6) residue and a NeuNAc alpha(2----3)Gal beta(1----4)GlcNAc terminal sequence; smaller amounts of non-sialylated and non-fucosylated hybrid structures were also detected. Swainsonine-treated cells also produced neutral oligosaccharides containing a single reducing N-acetylglucosamine residue substituted with polymannose sequences. The glycopeptide composition of Swainsonine-treated BHK cells resembles closely that of the ricin-resistant BHK cell mutant, RicR21 [P. A. Gleeson, J. Feeney and R. C. Hughes (1985) Biochemistry 24, 493-503], except the hybrid structures of RicR21 cells contain three, not five, mannose residues. Like RicR21 cells, Swainsonine-treated BHK cells showed a greatly increased resistance to ricin cytotoxicity, but not to modeccin, another galactose-binding lectin. These effects were readily reversed on removal of Swainsonine and growth in normal medium. | lld:pubmed |
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| pubmed-article:3085652 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3085652 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3085652 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3085652 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3085652 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:3085652 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:3085652 | pubmed:author | pubmed-author:FeeneyJJ | lld:pubmed |
| pubmed-article:3085652 | pubmed:author | pubmed-author:HughesR CRC | lld:pubmed |
| pubmed-article:3085652 | pubmed:author | pubmed-author:FoddyLL | lld:pubmed |
| pubmed-article:3085652 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3085652 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:3085652 | pubmed:volume | 233 | lld:pubmed |
| pubmed-article:3085652 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3085652 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3085652 | pubmed:pagination | 697-706 | lld:pubmed |
| pubmed-article:3085652 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:3085652 | pubmed:year | 1986 | lld:pubmed |
| pubmed-article:3085652 | pubmed:articleTitle | Properties of baby-hamster kidney (BHK) cells treated with Swainsonine, an inhibitor of glycoprotein processing. Comparison with ricin-resistant BHK-cell mutants. | lld:pubmed |
| pubmed-article:3085652 | pubmed:publicationType | Journal Article | lld:pubmed |
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