pubmed-article:8660631 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8660631 | lifeskim:mentions | umls-concept:C0004492 | lld:lifeskim |
pubmed-article:8660631 | lifeskim:mentions | umls-concept:C0085249 | lld:lifeskim |
pubmed-article:8660631 | lifeskim:mentions | umls-concept:C1539554 | lld:lifeskim |
pubmed-article:8660631 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
pubmed-article:8660631 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
pubmed-article:8660631 | lifeskim:mentions | umls-concept:C0178463 | lld:lifeskim |
pubmed-article:8660631 | lifeskim:mentions | umls-concept:C0243072 | lld:lifeskim |
pubmed-article:8660631 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:8660631 | pubmed:dateCreated | 1996-10-17 | lld:pubmed |
pubmed-article:8660631 | pubmed:abstractText | The chemical synthesis and utilization of two photoaffinity analogs, 125I-labeled 5-[3-(p-azidosalicylamido)-1-propenyl]-UDP-GlcNAc and -UDP-GalNAc, is described. Starting with either UDP-GlcNAc or UDP-GalNAc, the synthesis involved the preparation of the 5-mercuri-UDP-HexNAc and then attachment of an allylamine to the 5 position to give 5-(3-amino)allyl-UDP-HexNAc. This was followed by acylation with N-hydroxysuccinimide p-aminosalicylic acid to form the final product, i.e., 5-[3-(p-azidosalicylamido)-1-propenyl]-UDP-GlcNAc or UDP-GalNAc. These products could then be iodinated with chloramine T to give the 125I-derivatives. Both the UDP-GlcNAc and the UDP-GalNAc derivatives reacted in a concentration-dependent manner with a highly purified UDP-HexNAc pyrophosphorylase, and both specifically labeled the subunit(s) of this protein. The labeling of the protein by the UDP-GlcNAc derivative was inhibited in dose-dependent fashion by either unlabeled UDP-GlcNAc or unlabeled UDP-GalNAc. Likewise, labeling with the UDP-GalNAc probe was blocked by either UDP-GlcNAc or UDP-GalNAc. The UDP-GlcNAc probe also specifically labeled a partially purified preparation of GlcNAc transferase I. | lld:pubmed |
pubmed-article:8660631 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8660631 | pubmed:language | eng | lld:pubmed |
pubmed-article:8660631 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8660631 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8660631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8660631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8660631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8660631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8660631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8660631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8660631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8660631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8660631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8660631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8660631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8660631 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8660631 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8660631 | pubmed:month | Jul | lld:pubmed |
pubmed-article:8660631 | pubmed:issn | 0003-2697 | lld:pubmed |
pubmed-article:8660631 | pubmed:author | pubmed-author:ElbeinA DAD | lld:pubmed |
pubmed-article:8660631 | pubmed:author | pubmed-author:PastuszakII | lld:pubmed |
pubmed-article:8660631 | pubmed:author | pubmed-author:ZenzJJ | lld:pubmed |
pubmed-article:8660631 | pubmed:author | pubmed-author:DrakeR RRR | lld:pubmed |
pubmed-article:8660631 | pubmed:author | pubmed-author:SzumiloTT | lld:pubmed |
pubmed-article:8660631 | pubmed:author | pubmed-author:ShabalinYY | lld:pubmed |
pubmed-article:8660631 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8660631 | pubmed:day | 15 | lld:pubmed |
pubmed-article:8660631 | pubmed:volume | 239 | lld:pubmed |
pubmed-article:8660631 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8660631 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8660631 | pubmed:pagination | 99-106 | lld:pubmed |
pubmed-article:8660631 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:8660631 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8660631 | pubmed:articleTitle | Synthesis of aryl azide derivatives of UDP-GlcNAc and UDP-GalNAc and their use for the affinity labeling of glycosyltransferases and the UDP-HexNAc pyrophosphorylase. | lld:pubmed |
pubmed-article:8660631 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, Arkansas, 72205, USA. | lld:pubmed |
pubmed-article:8660631 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8660631 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |