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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1994-3-28
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pubmed:abstractText |
In the preceding paper [Mandal, D. K., Kishore, N., & Brewer, C. F. (1994) Biochemistry (preceding paper in this issue)] the trisaccharide 3,6-di-O-(alpha-D-mannopyranosyl)-D-mannose, which is present in all asparagine-linked carbohydrates, was shown by titration microcalorimetry to bind to the lectin concanavalin A (Con A) with nearly -6 kcal mol-1 greater enthalpy change (delta H) than methyl alpha-D-mannopyranoside (Me alpha Man). These results indicate that Con A possesses an extended binding site for the trisaccharide. In the present paper, we have investigated the binding of a series of synthetic analogs of the methyl alpha-anomer of the trisaccharide using hemagglutination inhibition, solvent proton magnetic relaxation dispersion (NMRD), near ultraviolet circular dichroism, and titration microcalorimetry measurements. Four of the analogs tested possess an alpha-glucosyl or alpha-galactosyl residue substituted at either the alpha(1-6) or alpha(1-3) position. Analysis of the data indicates that the alpha(1-6) residue of the parent trimannoside binds to the so-called monosaccharide site and the alpha(1-3) residue to a weaker secondary site. Binding at the secondary site involves unfavorable interactions of the 2-equatorial hydroxyl of the alpha(1-3) Glc derivative since this analog binds with 12-fold lower affinity and -3.4 kcal mol-1 lesser delta H than the trimannoside, whereas the alpha(1-3)-2-deoxyGlc analog possesses essentially the same affinity and delta H as the trimannoside.(ABSTRACT TRUNCATED AT 250 WORDS)
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pubmed:grant | |
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 |
Feb
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
33
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1157-62
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8110747-Asparagine,
pubmed-meshheading:8110747-Binding Sites,
pubmed-meshheading:8110747-Calorimetry,
pubmed-meshheading:8110747-Carbohydrate Metabolism,
pubmed-meshheading:8110747-Carbohydrate Sequence,
pubmed-meshheading:8110747-Circular Dichroism,
pubmed-meshheading:8110747-Concanavalin A,
pubmed-meshheading:8110747-Hemagglutination Tests,
pubmed-meshheading:8110747-Magnetic Resonance Spectroscopy,
pubmed-meshheading:8110747-Molecular Sequence Data,
pubmed-meshheading:8110747-Spectrophotometry, Ultraviolet,
pubmed-meshheading:8110747-Thermodynamics
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pubmed:year |
1994
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pubmed:articleTitle |
Studies of the binding specificity of concanavalin A. Nature of the extended binding site for asparagine-linked carbohydrates.
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pubmed:affiliation |
Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, New York 10461.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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