Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:10358011rdf:typepubmed:Citationlld:pubmed
pubmed-article:10358011lifeskim:mentionsumls-concept:C0014442lld:lifeskim
pubmed-article:10358011lifeskim:mentionsumls-concept:C1253959lld:lifeskim
pubmed-article:10358011lifeskim:mentionsumls-concept:C2700384lld:lifeskim
pubmed-article:10358011lifeskim:mentionsumls-concept:C1156956lld:lifeskim
pubmed-article:10358011lifeskim:mentionsumls-concept:C0332298lld:lifeskim
pubmed-article:10358011lifeskim:mentionsumls-concept:C0037791lld:lifeskim
pubmed-article:10358011pubmed:issue24lld:pubmed
pubmed-article:10358011pubmed:dateCreated1999-7-6lld:pubmed
pubmed-article:10358011pubmed:abstractTextPoly-N-acetyllactosamine is a unique carbohydrate that can carry various functional oligosaccharides, such as sialyl Lewis X. It has been shown that the amount of poly-N-acetyllactosamine is increased in N-glycans, when they contain Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->4GlcNAcbeta1 -->2)Manalpha1-->6 branched structure. To determine how this increased synthesis of poly-N-acetyllactosamines takes place, the branched acceptor was incubated with a mixture of i-extension enzyme (iGnT) and beta1, 4galactosyltransferase I (beta4Gal-TI). First, N-acetyllactosamine repeats were more readily added to the branched acceptor than the summation of poly-N-acetyllactosamines formed individually on each unbranched acceptor. Surprisingly, poly-N-acetyllactosamine was more efficiently formed on Galbeta1-->4GlcNAcbeta1-->2Manalpha-->R side chain than in Galbeta1-->4GlcNAcbeta1-->6Manalpha-->R, due to preferential action of iGnT on Galbeta1-->4GlcNAcbeta1-->2Manalpha-->R side chain. On the other hand, galactosylation was much more efficient on beta1,6-linked GlcNAc than beta1,2-linked GlcNAc, preferentially forming Galbeta1-->4GlcNAcbeta1-->6(GlcNAcbeta1-->2)Manalph a1-->6Manbeta -->R. Starting with this preformed acceptor, N-acetyllactosamine repeats were added almost equally to Galbeta1-->4GlcNAcbeta1-->6Manalpha-->R and Galbeta1-->4GlcNAcbeta1-->2Manalpha-->R side chains. Taken together, these results indicate that the complemental branch specificity of iGnT and beta4Gal-TI leads to efficient and equal addition of N-acetyllactosamine repeats on both side chains of GlcNAcbeta1-->6(GlcNAcbeta1-->2)Manalpha1-->6Manbet a-->R structure, which is consistent with the structures found in nature. The results also suggest that the addition of Galbeta1-->4GlcNAcbeta1-->6 side chain on Galbeta1-->4GlcNAcbeta1-->2Man-->R side chain converts the acceptor to one that is much more favorable for iGnT and beta4Gal-TI.lld:pubmed
pubmed-article:10358011pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358011pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358011pubmed:languageenglld:pubmed
pubmed-article:10358011pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358011pubmed:citationSubsetIMlld:pubmed
pubmed-article:10358011pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358011pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358011pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358011pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358011pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358011pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358011pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358011pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358011pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358011pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358011pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358011pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358011pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10358011pubmed:statusMEDLINElld:pubmed
pubmed-article:10358011pubmed:monthJunlld:pubmed
pubmed-article:10358011pubmed:issn0021-9258lld:pubmed
pubmed-article:10358011pubmed:authorpubmed-author:SasakiKKlld:pubmed
pubmed-article:10358011pubmed:authorpubmed-author:FukudaMMlld:pubmed
pubmed-article:10358011pubmed:authorpubmed-author:FukudaM NMNlld:pubmed
pubmed-article:10358011pubmed:authorpubmed-author:HindsgaulOOlld:pubmed
pubmed-article:10358011pubmed:authorpubmed-author:McAuliffeJJlld:pubmed
pubmed-article:10358011pubmed:authorpubmed-author:UjitaMMlld:pubmed
pubmed-article:10358011pubmed:issnTypePrintlld:pubmed
pubmed-article:10358011pubmed:day11lld:pubmed
pubmed-article:10358011pubmed:volume274lld:pubmed
pubmed-article:10358011pubmed:ownerNLMlld:pubmed
pubmed-article:10358011pubmed:authorsCompleteYlld:pubmed
pubmed-article:10358011pubmed:pagination16717-26lld:pubmed
pubmed-article:10358011pubmed:dateRevised2007-11-14lld:pubmed
pubmed-article:10358011pubmed:meshHeadingpubmed-meshheading:10358011...lld:pubmed
pubmed-article:10358011pubmed:meshHeadingpubmed-meshheading:10358011...lld:pubmed
pubmed-article:10358011pubmed:meshHeadingpubmed-meshheading:10358011...lld:pubmed
pubmed-article:10358011pubmed:meshHeadingpubmed-meshheading:10358011...lld:pubmed
pubmed-article:10358011pubmed:meshHeadingpubmed-meshheading:10358011...lld:pubmed
pubmed-article:10358011pubmed:meshHeadingpubmed-meshheading:10358011...lld:pubmed
pubmed-article:10358011pubmed:meshHeadingpubmed-meshheading:10358011...lld:pubmed
pubmed-article:10358011pubmed:meshHeadingpubmed-meshheading:10358011...lld:pubmed
pubmed-article:10358011pubmed:meshHeadingpubmed-meshheading:10358011...lld:pubmed
pubmed-article:10358011pubmed:meshHeadingpubmed-meshheading:10358011...lld:pubmed
pubmed-article:10358011pubmed:meshHeadingpubmed-meshheading:10358011...lld:pubmed
pubmed-article:10358011pubmed:meshHeadingpubmed-meshheading:10358011...lld:pubmed
pubmed-article:10358011pubmed:meshHeadingpubmed-meshheading:10358011...lld:pubmed
pubmed-article:10358011pubmed:meshHeadingpubmed-meshheading:10358011...lld:pubmed
pubmed-article:10358011pubmed:meshHeadingpubmed-meshheading:10358011...lld:pubmed
pubmed-article:10358011pubmed:year1999lld:pubmed
pubmed-article:10358011pubmed:articleTitlePoly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of I-extension enzyme and beta1,4-galactosyltransferase I.lld:pubmed
pubmed-article:10358011pubmed:affiliationThe Glycobiology Program, Cancer Research Center, The Burnham Institute, La Jolla, California 92037, USA. minoru@burnham-inst.orglld:pubmed
pubmed-article:10358011pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:10358011pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:10358011pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10358011lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10358011lld:pubmed