pubmed-article:10358011 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10358011 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
pubmed-article:10358011 | lifeskim:mentions | umls-concept:C1253959 | lld:lifeskim |
pubmed-article:10358011 | lifeskim:mentions | umls-concept:C2700384 | lld:lifeskim |
pubmed-article:10358011 | lifeskim:mentions | umls-concept:C1156956 | lld:lifeskim |
pubmed-article:10358011 | lifeskim:mentions | umls-concept:C0332298 | lld:lifeskim |
pubmed-article:10358011 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
pubmed-article:10358011 | pubmed:issue | 24 | lld:pubmed |
pubmed-article:10358011 | pubmed:dateCreated | 1999-7-6 | lld:pubmed |
pubmed-article:10358011 | pubmed:abstractText | Poly-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:10358011 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10358011 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10358011 | pubmed:language | eng | lld:pubmed |
pubmed-article:10358011 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10358011 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10358011 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10358011 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10358011 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10358011 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10358011 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10358011 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10358011 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10358011 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10358011 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10358011 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10358011 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10358011 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10358011 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10358011 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10358011 | pubmed:month | Jun | lld:pubmed |
pubmed-article:10358011 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:10358011 | pubmed:author | pubmed-author:SasakiKK | lld:pubmed |
pubmed-article:10358011 | pubmed:author | pubmed-author:FukudaMM | lld:pubmed |
pubmed-article:10358011 | pubmed:author | pubmed-author:FukudaM NMN | lld:pubmed |
pubmed-article:10358011 | pubmed:author | pubmed-author:HindsgaulOO | lld:pubmed |
pubmed-article:10358011 | pubmed:author | pubmed-author:McAuliffeJJ | lld:pubmed |
pubmed-article:10358011 | pubmed:author | pubmed-author:UjitaMM | lld:pubmed |
pubmed-article:10358011 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10358011 | pubmed:day | 11 | lld:pubmed |
pubmed-article:10358011 | pubmed:volume | 274 | lld:pubmed |
pubmed-article:10358011 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10358011 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10358011 | pubmed:pagination | 16717-26 | lld:pubmed |
pubmed-article:10358011 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:10358011 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10358011 | pubmed:articleTitle | Poly-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:10358011 | pubmed:affiliation | The Glycobiology Program, Cancer Research Center, The Burnham Institute, La Jolla, California 92037, USA. minoru@burnham-inst.org | lld:pubmed |
pubmed-article:10358011 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10358011 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:10358011 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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