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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1997-10-2
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pubmed:abstractText |
Beta-D-Xylopyranosides, such as p-nitrophenyl-beta-D-xylopyranoside (Xyl-Np) or 4-methylumbelliferyl-beta-D-xylopyranoside (Xyl-MeUmb), when added to the culture medium of human skin fibroblasts have previously been shown to produce some Np- or MeUmb-oligosaccharides related to the regulation of glycosaminoglycan biosynthesis. Among these oligosaccharide derivatives, we synthesized the trisaccharide derivative NeuAc(alpha2-3)Gal(beta1-4)Xyl-Np(beta1- as a potential inhibitor of human skin fibroblast glycosaminoglycan biosynthesis. This synthesis was achieved by sequential use of transglycosylating activities of Escherichia coli beta-galactosidase and Trypanosoma cruzi trans-sialidase. The structure of the oligosaccharide obtained was determined by HPLC, ion-spray mass spectrometry, and NMR.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
247
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1083-90
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:9288934-Carbohydrate Conformation,
pubmed-meshheading:9288934-Chromatography, Gel,
pubmed-meshheading:9288934-Chromatography, High Pressure Liquid,
pubmed-meshheading:9288934-Glycolysis,
pubmed-meshheading:9288934-Glycosaminoglycans,
pubmed-meshheading:9288934-Humans,
pubmed-meshheading:9288934-Kinetics,
pubmed-meshheading:9288934-Magnetic Resonance Spectroscopy,
pubmed-meshheading:9288934-Mass Spectrometry,
pubmed-meshheading:9288934-Nitrobenzenes,
pubmed-meshheading:9288934-Oligosaccharides
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pubmed:year |
1997
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pubmed:articleTitle |
All-transglycolytic synthesis and characterization of sialyl(alpha2-3)galactosyl(beta1-4)xylosyl-p-nitrophenyl(beta1-), an oligosaccharide derivative related to glycosaminoglycan biosynthesis.
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pubmed:affiliation |
Department of Biochemistry, Biophysics and Macromolecular Chemistry, University of Trieste, Italy. vetere@univ.trieste.it
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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