Linked Life Data

9837949

Source:http://linkedlifedata.com/resource/pubmed/id/9837949

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
50
pubmed:dateCreated
1999-1-14
pubmed:abstractText
The binding of Bandeiraea simplicifolia lectin-I isolectin B4 on the endogenous glycoproteins of different insect cell lines led us to characterize for the first time a UDP-Gal:Galbeta1-3GalNAc alpha1, 4-galactosyltransferase in a Mamestra brassicae cell line (Mb). The study of the acceptor specificity indicated that the Mb alpha-galactosyltransferase prefers Galbeta1-3-R as acceptor, and among such glycans, the relative substrate activity Vmax/Km was equal to 20 microliters.mg-1.h-1 for Galbetal-3GlcNAcbeta1-O-octyl and to 330 microliters.mg-1.h-1 for Galbeta1-3GalNAcalpha-1-O-benzyl, showing clearly that Galbeta1-3GalNAc disaccharide was the more suitable acceptor substrate for Mb alpha-galactosyltransferase activity. Nuclear magnetic resonance and mass spectrometry data allowed us to establish that the Mb alpha-galactosyltransferase synthesizes one unique product, Galalpha1-4Galbeta1-3GalNAcalpha1-O-benzyl. The Galbeta1-3GalNAc disaccharide is usually present on O-glycosylation sites of numerous asialoglycoproteins and at the nonreducing end of some glycolipids. We observed that Mb alpha1,4-galactosyltransferase catalyzed the transfer of galactose onto both natural acceptors. Finally, we demonstrated that the trisaccharide Galalpha1-4Galbeta1-3GalNAcalpha1-O-benzyl was able to inhibit anti-PK monoclonal antibody-mediated hemagglutination of human blood group PK1 and PK2 erythrocytes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
33644-51
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Characterization of a UDP-Gal:Galbeta1-3GalNAc alpha1, 4-galactosyltransferase activity in a Mamestra brassicae cell line.
pubmed:affiliation
Laboratoire de Chimie Biologique, Unité Mixte de Recherche du CNRS 111, Université des Sciences et Technologies de Lille, F-59655 Villeneuve d'Ascq, France.
pubmed:publicationType
Journal Article