Linked Life Data

11003557

Source:http://linkedlifedata.com/resource/pubmed/id/11003557

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2000-9-26
pubmed:abstractText
We showed previously that Chinese hamster ovary cells took up and utilized a variety of N-acetylglucosaminides as primers of oligosaccharide biosynthesis (Ding et al., 1999, J. Carbohydr. Chem., 18:471-475). In this study, a library of N-acetylglucosaminides was enzymatically galactosylated in vitro to yield type 2 chain N-acetyllactosaminides bearing a variety of aglycones. Those disaccharides are potential acceptors for fucosyltransferases. As an extension of the previous study, we tested the type 2 chain disaccharyl glycosides (Galbeta1,4-GlcNAcbeta-R) for their aglycone-dependent acceptor specificity for alpha-L-fucosyltransferase III (Fuc-TIII). The enzyme activity significantly depended on the aglycone structures, suggesting that, in addition to the polar groups on the sugar moiety, the hydrophobic aglycone can substantially contribute to recognition in this reaction.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0282-0080
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
725-30
pubmed:dateRevised
2008-8-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Aglycone structure influences alpha-fucosyltransferase III activity using N-acetyllactosamine glycoside acceptors.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't