pubmed-article:9368010 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9368010 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:9368010 | lifeskim:mentions | umls-concept:C0751974 | lld:lifeskim |
pubmed-article:9368010 | lifeskim:mentions | umls-concept:C0026682 | lld:lifeskim |
pubmed-article:9368010 | lifeskim:mentions | umls-concept:C0007004 | lld:lifeskim |
pubmed-article:9368010 | lifeskim:mentions | umls-concept:C0205177 | lld:lifeskim |
pubmed-article:9368010 | lifeskim:mentions | umls-concept:C0668363 | lld:lifeskim |
pubmed-article:9368010 | lifeskim:mentions | umls-concept:C1524075 | lld:lifeskim |
pubmed-article:9368010 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:9368010 | pubmed:issue | 47 | lld:pubmed |
pubmed-article:9368010 | pubmed:dateCreated | 1997-12-23 | lld:pubmed |
pubmed-article:9368010 | pubmed:abstractText | A microsomal GlcNAc-6-O-sulfotransferase activity from human bronchial mucosa, able to transfer a sulfate group from adenosine 3'-phosphate 5'-phosphosulfate onto methyl-N-acetylglucosaminides or terminal N-acetylglucosamine residues of carbohydrate chains from human respiratory mucins, has been characterized. The reaction products containing a terminal HO3S-6GlcNAc were identified by high performance anion-exchange chromatography. Using methyl-beta-N-acetylglucosaminide as a substrate, the optimal activity was obtained with 0.1% Triton X-100, 30 mM NaF, 20 mM Mn2+, 5 mM AMP in a 30 mM MOPS (3-(N-morpholino) propanesulfonic acid) buffer at pH 6.7. The apparent Km values for adenosine 3'-phosphate 5'-phosphosulfate and methyl-beta-N-acetylglucosaminide were observed at 9.1 x 10(-6) M and 0.54 x 10(-3) M, respectively. The enzyme had more affinity for carbohydrate chains with a terminal GlcNAc residue than for methyl-beta-N-acetylglucosaminide; it was unable to catalyze the transfer of sulfate to position 6 of the GlcNAc residue contained in a terminal Galbeta1-4GlcNAc sequence. However, oligosaccharides with a nonreducing terminal HO3S-6GlcNAc were substrates for a beta1-4 galactosyltransferase from human bronchial mucosa. These data point out that GlcNAc-6-O-sulfotransferase must act before beta1-4 galactosylation in mucin-type oligosaccharide biosynthesis. | lld:pubmed |
pubmed-article:9368010 | pubmed:language | eng | lld:pubmed |
pubmed-article:9368010 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9368010 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9368010 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9368010 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9368010 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9368010 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9368010 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9368010 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9368010 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9368010 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9368010 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9368010 | pubmed:month | Nov | lld:pubmed |
pubmed-article:9368010 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:9368010 | pubmed:author | pubmed-author:RousselPP | lld:pubmed |
pubmed-article:9368010 | pubmed:author | pubmed-author:StreckerGG | lld:pubmed |
pubmed-article:9368010 | pubmed:author | pubmed-author:LamblinGG | lld:pubmed |
pubmed-article:9368010 | pubmed:author | pubmed-author:Lo-GuidiceJ... | lld:pubmed |
pubmed-article:9368010 | pubmed:author | pubmed-author:DucouroubleM... | lld:pubmed |
pubmed-article:9368010 | pubmed:author | pubmed-author:DegrooteSS | lld:pubmed |
pubmed-article:9368010 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9368010 | pubmed:day | 21 | lld:pubmed |
pubmed-article:9368010 | pubmed:volume | 272 | lld:pubmed |
pubmed-article:9368010 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9368010 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9368010 | pubmed:pagination | 29493-501 | lld:pubmed |
pubmed-article:9368010 | pubmed:dateRevised | 2007-10-30 | lld:pubmed |
pubmed-article:9368010 | pubmed:meshHeading | pubmed-meshheading:9368010-... | lld:pubmed |
pubmed-article:9368010 | pubmed:meshHeading | pubmed-meshheading:9368010-... | lld:pubmed |
pubmed-article:9368010 | pubmed:meshHeading | pubmed-meshheading:9368010-... | lld:pubmed |
pubmed-article:9368010 | pubmed:meshHeading | pubmed-meshheading:9368010-... | lld:pubmed |
pubmed-article:9368010 | pubmed:meshHeading | pubmed-meshheading:9368010-... | lld:pubmed |
pubmed-article:9368010 | pubmed:meshHeading | pubmed-meshheading:9368010-... | lld:pubmed |
pubmed-article:9368010 | pubmed:meshHeading | pubmed-meshheading:9368010-... | lld:pubmed |
pubmed-article:9368010 | pubmed:meshHeading | pubmed-meshheading:9368010-... | lld:pubmed |
pubmed-article:9368010 | pubmed:meshHeading | pubmed-meshheading:9368010-... | lld:pubmed |
pubmed-article:9368010 | pubmed:meshHeading | pubmed-meshheading:9368010-... | lld:pubmed |
pubmed-article:9368010 | pubmed:meshHeading | pubmed-meshheading:9368010-... | lld:pubmed |
pubmed-article:9368010 | pubmed:meshHeading | pubmed-meshheading:9368010-... | lld:pubmed |
pubmed-article:9368010 | pubmed:meshHeading | pubmed-meshheading:9368010-... | lld:pubmed |
pubmed-article:9368010 | pubmed:meshHeading | pubmed-meshheading:9368010-... | lld:pubmed |
pubmed-article:9368010 | pubmed:meshHeading | pubmed-meshheading:9368010-... | lld:pubmed |
pubmed-article:9368010 | pubmed:meshHeading | pubmed-meshheading:9368010-... | lld:pubmed |
pubmed-article:9368010 | pubmed:year | 1997 | lld:pubmed |
pubmed-article:9368010 | pubmed:articleTitle | Characterization of an N-acetylglucosamine-6-O-sulfotransferase from human respiratory mucosa active on mucin carbohydrate chains. | lld:pubmed |
pubmed-article:9368010 | pubmed:affiliation | Unité INSERM 377, place de Verdun, F-59045 Lille, France. | lld:pubmed |
pubmed-article:9368010 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9368010 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9368010 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9368010 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9368010 | lld:pubmed |