Linked Life Data

2912731

Source:http://linkedlifedata.com/resource/pubmed/id/2912731

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1989-3-2
pubmed:abstractText
We have recently demonstrated that certain oligomannose and bisected hybrid-type glycopeptides are bivalent for concanavalin A (ConA) binding and that they can precipitate the lectin [Bhattacharyya, L., Ceccarini, C., Lorenzoni, P & Brewer, C. F. (1987) J. Biol. Chem. 262, 1288-1293]. Two protein-binding sites on each glycopeptide were identified: one on the alpha(1-6) arm of the core beta-mannose residue which binds with high affinity (primary site); the other on the alpha(1-3) arm of the core beta-mannose residue which binds with lower affinity (secondary site). In the present study, we have investigated the relationship between the structures of the primary sites of oligomannose-type glycopeptides and their affinities for ConA. Two mechanisms of binding at the primary sites of oligomannose-type glycopeptides have been identified which account for the 3000-fold increase in affinity of a Man9 glycopeptide relative to that of methyl alpha-D-mannopyranoside. Changes in the structures and affinities of both the primary and secondary sites are observed to influence the precipitation activities of the glycopeptides. These findings have important consequences for the specificity of ConA binding in solutions containing mixtures of the carbohydrates.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
178
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
721-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Interactions of concanavalin A with asparagine-linked glycopeptides. Structure/activity relationships of the binding and precipitation of oligomannose and bisected hybrid-type glycopeptides with concanavalin A.
pubmed:affiliation
Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, New York 10461.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.