| pubmed-article:8101768 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8101768 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
| pubmed-article:8101768 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:8101768 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:8101768 | lifeskim:mentions | umls-concept:C1524063 | lld:lifeskim |
| pubmed-article:8101768 | lifeskim:mentions | umls-concept:C0163923 | lld:lifeskim |
| pubmed-article:8101768 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8101768 | pubmed:dateCreated | 1993-8-31 | lld:pubmed |
| pubmed-article:8101768 | pubmed:abstractText | A simple preparation of the "core-II" N-acetylglucosaminyltransferase (UDP-D-GlcpNAc:beta-D-Galp-(1-->3)-alpha-D-GalpNAc (GlcNAc to GalNAc) beta-(1-->6)-GlcNAc-transferase, GlcNAcT, EC 2.4.1.102) from commercial mouse kidney acetone powder is reported. The enzyme obtained in a single step of affinity chromatography is suitable for use in preparative oligosaccharide synthesis. In conjunction with previously described preparations of beta-(1-->4)-galactosyltransferase (EC 2.4.1.22), alpha-(2-->3)-sialytransferase (EC 2.4.99.6) and alpha-(1-->3/4)-fucosyltransferase (EC 2.4.1.65), the GlcNAcT was used in the first step of a sequence which converted the disaccharide beta-D-Galp-(1-->3)-alpha-D-GalpNAc-OR into the sialyl-LeX-containing structure alpha-D-NeupAc-(2-->3)-beta-D-Galp- (1-->4)-[alpha-L-Fucp-(1-->3)]-beta-D-GlcpNAc-(1-->6)-[beta-D-Galp - (1-->3)]-alpha-D-GalpNAc-OR (5), where R = (CH2)8CO2Me. Hexasaccharide 5, thus assembled in only one week once the enzymes were prepared, was characterized by 1H and 13C NMR spectroscopy and fast-atom bombardment mass spectrometry, as were all intermediate oligosaccharides. The core II GlcNAcT thus joins the expanding repertoire of readily available reagents for the rapid assembly of oligosaccharides. | lld:pubmed |
| pubmed-article:8101768 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8101768 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8101768 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8101768 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8101768 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8101768 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8101768 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8101768 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8101768 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8101768 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8101768 | pubmed:month | May | lld:pubmed |
| pubmed-article:8101768 | pubmed:issn | 0008-6215 | lld:pubmed |
| pubmed-article:8101768 | pubmed:author | pubmed-author:HindsgaulOO | lld:pubmed |
| pubmed-article:8101768 | pubmed:author | pubmed-author:PalcicM MMM | lld:pubmed |
| pubmed-article:8101768 | pubmed:author | pubmed-author:OehrleinRR | lld:pubmed |
| pubmed-article:8101768 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8101768 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:8101768 | pubmed:volume | 244 | lld:pubmed |
| pubmed-article:8101768 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8101768 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8101768 | pubmed:pagination | 149-59 | lld:pubmed |
| pubmed-article:8101768 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:8101768 | pubmed:meshHeading | pubmed-meshheading:8101768-... | lld:pubmed |
| pubmed-article:8101768 | pubmed:meshHeading | pubmed-meshheading:8101768-... | lld:pubmed |
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| pubmed-article:8101768 | pubmed:meshHeading | pubmed-meshheading:8101768-... | lld:pubmed |
| pubmed-article:8101768 | pubmed:meshHeading | pubmed-meshheading:8101768-... | lld:pubmed |
| pubmed-article:8101768 | pubmed:meshHeading | pubmed-meshheading:8101768-... | lld:pubmed |
| pubmed-article:8101768 | pubmed:meshHeading | pubmed-meshheading:8101768-... | lld:pubmed |
| pubmed-article:8101768 | pubmed:meshHeading | pubmed-meshheading:8101768-... | lld:pubmed |
| pubmed-article:8101768 | pubmed:meshHeading | pubmed-meshheading:8101768-... | lld:pubmed |
| pubmed-article:8101768 | pubmed:meshHeading | pubmed-meshheading:8101768-... | lld:pubmed |
| pubmed-article:8101768 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8101768 | pubmed:articleTitle | Use of the "core-2"-N-acetylglucosaminyltransferase in the chemical-enzymatic synthesis of a sialyl-LeX-containing hexasaccharide found on O-linked glycoproteins. | lld:pubmed |
| pubmed-article:8101768 | pubmed:affiliation | Department of Chemistry, University of Alberta, Edmonton, Canada. | lld:pubmed |
| pubmed-article:8101768 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8101768 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
