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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1994-8-24
|
| pubmed:abstractText |
Recombinant rabbit UDP-GlcNAc: alpha-Man-(1-->3R) beta-(1-->2)-N-acetylglucosaminyl-transferase I (EC 2.4.1.101, GlcNAc-T I) produced in the Sf9 insect cell/baculovirus expression system has been used to convert compounds of the form 3-R-alpha-Man(1-->6)(alpha-Man(1-->3)) beta-Man-O-octyl to 3-R-alpha-Man(1-->6)(beta-GlcNAc(1-->2)alpha-Man(1-->3)) beta-Man-O-octyl where R is OH (14), O-methyl (17), O-pentyl (18), O-(4,4-azo)pentyl (19), O-(5-iodoacetamido)pentyl (20) and O-(5-amino)pentyl (21); 2-deoxy-alpha-Man(1-->6)(beta-GlcNAc(1-->2) alpha-Man(1-->3)) beta-Man-O-octyl (16), 4-O-methyl-alpha-Man(1-->6) (beta-GlcNAc(1-->2) alpha-Man(1-->3)) beta-Man-O-octyl (22), 6-O-methyl-alpha-Man(1-->6)(beta-GlcNAc(1-->2) alpha Man(1-->3)) beta-Man-O-octyl (23) and alpha-Man(1-->6)[beta-GlcNAc(1-->2)(4-O-methyl) alpha-Man(1-->3)] beta-Man-O-octyl (15) were also synthesized by this procedure. The yields ranged from 80 to 99%. Products were characterized by high resolution 1H and 13C nuclear magnetic resonance spectroscopy and fast atom bombardment mass spectrometry. Compounds 14, 15, 17, 22, and 23 are excellent substrates for UDP-GlcNAc: alpha-Man(1-->6R) beta-(1-->2)-N-acetylglucosaminyltransferase II and the other compounds are inhibitors of this enzyme.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/N-Acetylglucosaminyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trisaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-1,3-mannosyl-glycoprotein...,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-1,6-mannosyl-glycoprotein...,
http://linkedlifedata.com/resource/pubmed/chemical/beta-1,3-galactosyl-0-glycosyl-glyco...
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0008-6215
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
2
|
| pubmed:volume |
259
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
93-101
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8039192-Animals,
pubmed-meshheading:8039192-Carbohydrate Conformation,
pubmed-meshheading:8039192-Carbohydrate Sequence,
pubmed-meshheading:8039192-Cell Line,
pubmed-meshheading:8039192-Magnetic Resonance Spectroscopy,
pubmed-meshheading:8039192-Molecular Sequence Data,
pubmed-meshheading:8039192-Moths,
pubmed-meshheading:8039192-N-Acetylglucosaminyltransferases,
pubmed-meshheading:8039192-Oligosaccharides,
pubmed-meshheading:8039192-Optical Rotation,
pubmed-meshheading:8039192-Recombinant Proteins,
pubmed-meshheading:8039192-Spectrometry, Mass, Fast Atom Bombardment,
pubmed-meshheading:8039192-Substrate Specificity,
pubmed-meshheading:8039192-Transfection,
pubmed-meshheading:8039192-Trisaccharides
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
Synthesis of tetrasaccharide analogues of the N-glycan substrate of beta-(1-->2)-N-acetylglucosaminyltransferase II using trisaccharide precursors and recombinant beta-(1-->2)-N-acetylglucosaminyltransferase I.
|
| pubmed:affiliation |
Research Institute, Hospital for Sick Children, Toronto, ON, Canada.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|