| pubmed-article:2969202 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2969202 | lifeskim:mentions | umls-concept:C0040300 | lld:lifeskim |
| pubmed-article:2969202 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
| pubmed-article:2969202 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:2969202 | lifeskim:mentions | umls-concept:C0025663 | lld:lifeskim |
| pubmed-article:2969202 | lifeskim:mentions | umls-concept:C0680730 | lld:lifeskim |
| pubmed-article:2969202 | lifeskim:mentions | umls-concept:C0008562 | lld:lifeskim |
| pubmed-article:2969202 | lifeskim:mentions | umls-concept:C2256627 | lld:lifeskim |
| pubmed-article:2969202 | lifeskim:mentions | umls-concept:C1148554 | lld:lifeskim |
| pubmed-article:2969202 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:2969202 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2969202 | pubmed:dateCreated | 1988-8-18 | lld:pubmed |
| pubmed-article:2969202 | pubmed:abstractText | A fluorescence assay method for UDP-GlcNAc:glycopeptide beta 1-4 N-acetylglucosaminyltransferase (Gn T-III) has been developed involving a pyridylaminated sugar as a substrate. A fluorescent sugar chain, in which the reducing end of the GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4GlcNAc has been aminated with 2-aminopyridine, is incubated with an enzyme sample, and then the fluorescent product with a bisecting N-acetylglucosamine is separated by reverse-phase high performance liquid chromatography and quantitated with a fluorescence detector. This assay method was found to be sensitive enough for the detection of 0.1 pmol of a reaction product. This assay is a reliable alternative to the use of a radiolabeled substrate and can be used for assaying N-acetylglucosaminyltransferase activity in crude extracts of various rat tissues. The kinetic experiments were carried out using crude enzyme extracts from the rat kidney. The enzyme has a pH optimum of 6.25 and requires Mn2+. The Km values for UDP-GlcNAc and a sugar acceptor substrate were found to be 3.1 mM and 190 microM, respectively. The enzyme activity in the rat kidney was higher than those in the other tissues examined. | lld:pubmed |
| pubmed-article:2969202 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2969202 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2969202 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2969202 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2969202 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2969202 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2969202 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2969202 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2969202 | pubmed:month | May | lld:pubmed |
| pubmed-article:2969202 | pubmed:issn | 0003-2697 | lld:pubmed |
| pubmed-article:2969202 | pubmed:author | pubmed-author:TaniguchiNN | lld:pubmed |
| pubmed-article:2969202 | pubmed:author | pubmed-author:FujiiSS | lld:pubmed |
| pubmed-article:2969202 | pubmed:author | pubmed-author:SugiyamaTT | lld:pubmed |
| pubmed-article:2969202 | pubmed:author | pubmed-author:NishikawaAA | lld:pubmed |
| pubmed-article:2969202 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2969202 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:2969202 | pubmed:volume | 170 | lld:pubmed |
| pubmed-article:2969202 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2969202 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2969202 | pubmed:pagination | 349-54 | lld:pubmed |
| pubmed-article:2969202 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:2969202 | pubmed:meshHeading | pubmed-meshheading:2969202-... | lld:pubmed |
| pubmed-article:2969202 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:2969202 | pubmed:articleTitle | A method for the determination of N-acetylglucosaminyltransferase III activity in rat tissues involving HPLC. | lld:pubmed |
| pubmed-article:2969202 | pubmed:affiliation | Department of Biochemistry, Osaka University Medical School, Japan. | lld:pubmed |
| pubmed-article:2969202 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2969202 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2969202 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2969202 | lld:pubmed |
