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canavalia/carbohydrate
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Structural analysis and anthelmintic activity of Canavalia brasiliensis lectin reveal molecular correlation between the carbohydrate recognition domain and glycans of Haemonchus contortus.
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Haemonchus contortus is one of the most economically important parasites infecting small ruminants worldwide. This nematode has shown a great ability to develop resistance to anthelmintic drugs, calling for the development of alternative control approaches. Because lectins recognize and bind to
Analysis of carbohydrate-protein interactions with synthetic N-linked neoglycoconjugate probes.
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Recently we have describe a simple efficient chemical method of generating an asparagine side-chain linker with beta-stereochemistry at the anomeric position of neutral oligosaccharides. We now report the 1-N-glycyl beta-derivatization of sialylated saccharides. Several neoglycoconjugates formed
Carbohydrate binding specificity of the lectin from the pea (Pisum sativum).
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Hapten inhibition measurements on the precipitin reaction between Pisum sativum lectin and Pichia pinus phosphomannan showed the lectin to bind D-mannose, D-glucose, D-fructose and L-sorbose. Unmodified hydroxyl groups at the C-4 and the C-6 positions of the D-glucopyranose ring were essential for
Surface carbohydrate changes on Onchocerca lienalis larvae as they develop from microfilariae to the infective third-stage in Simulium ornatum.
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Use was made of seven FITC labelled lectins as tools to investigate the surface of Onchocerca lienalis larvae as they develop through to the infective third-stage in a natural vector, Simulium ornatum. The lectins were derived from Canavalia ensiformis (Con A), Lens culinaris (lentil), Triticum
The carbohydrate-binding specificity and molecular modelling of Canavalia maritima and Dioclea grandiflora lectins.
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The carbohydrate-binding specificity of lectins from the seeds of Canavalia maritima and Dioclea grandiflora was studied by hapten-inhibition of haemagglutination using various sugars and sugar derivatives as inhibitors, including N-acetylneuraminic acid and N-acetylmuramic acid. Despite some
[Inhibition by cysteine of the carbohydrate-binding activity of lectins from Ricinus communis, Canavalia ensiformis and Euonymus europaeus].
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Precipitation induced by different lectins has been studied in the presence of some aminoacids. It was shown that precipitates formed by lectins from Ricinus communis (RCA1), Canavalia ensiformis (Con A), Euonymus europaeus (Eel) in the presence of appropriate carbohydrate-containing molecules
Characterizing the glycocalyx of poultry spermatozoa: II. In vitro storage of Turkey semen and mobility phenotype affects the carbohydrate component of sperm membrane glycoconjugates.
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The turkey sperm glycocalyx is known to contain residues of sialic acid, alpha-mannose/alpha-glucose, alpha- and beta-galactose, alpha-fucose, alpha- and beta-N-acetyl-galactosamine, monomers and dimers of N-acetyl-glucosamine, and N-acetyl-lactosamine. Potential changes in these carbohydrates
Ultrastructural localization of carbohydrates in Reichert's membrane of the mouse.
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In the present investigation, we examined the role of trophoblast and parietal endoderm cells in the synthesis of carbohydrate-containing components of Reichert's membrane. To eliminate the function of Reichert's membrane as a filter between maternal and embryonal tissues we carried out our
Analysis of carbohydrate structures in basal laminar deposit in aging human maculae.
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OBJECTIVE
To analyze carbohydrate structures in basal laminar deposit (BLD), an extracellular material that accumulates between the retinal pigment epithelium (RPE) and Bruch's membrane. BLD has been shown to correlate positively with visual loss in age-related macular degeneration.
METHODS
Thirteen
The role of lysosomal sialidase and beta-galactosidase in processing the complex carbohydrate chains on lysosomal enzymes and possibly other glycoproteins.
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Previous studies using the lectin RCA-I from Ricinus communis have indicated that several lysosomal enzymes in the fibroblasts of patients deficient in beta-galactosidase carry excess terminal galactose. Electrophoretic studies have shown that the same enzymes and the non-lysosomal adenosine
Energetics of lectin-carbohydrate binding. A microcalorimetric investigation of concanavalin A-oligomannoside complexation.
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Despite years of study, a comprehensive picture of the binding of the lectin from Canavalia ensiformis, concanavalin A, to carbohydrates remains elusive. We report here studies on the interaction of concanavalin A with methyl 3,6-di-O-(alpha-D-mannopyranosyl)-alpha-D-mannopyranoside, the minimum
Thermodynamic, kinetic, and electron microscopy studies of concanavalin A and Dioclea grandiflora lectin cross-linked with synthetic divalent carbohydrates.
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The jack bean lectin concanavalin A (ConA) and the Dioclea grandiflora lectin (DGL) are highly homologous Man/Glc-specific members of the Diocleinae subtribe. Both lectins bind, cross-link, and precipitate with carbohydrates possessing multiple terminal nonreducing Man residues. The present study
[Fluorescent derivatives of carbohydrates in the analysis of the structure of glycoconjugates. N-(4-methylcoumarin-7-yl) glycamines in the study of asparagine-bound carbohydrate chains of glycoproteins].
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4-(N-Methylcoumarin-7-yl) glycamines were employed in studying asparagine-linked carbohydrate chains of acid desialylated fetuin. The procedure was optimised for the reductive amination of oligosaccharides with 7-amino-4-methylcoumarin in the presence of Na(CN)BH3 to lead to oligosaccharide
Diocleinae lectins are a group of proteins with conserved binding sites for the core trimannoside of asparagine-linked oligosaccharides and differential specificities for complex carbohydrates.
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The seed lectin from Dioclea grandiflora and jack bean lectin concanavalin A (ConA) are both members of the Diocleinae subtribe of Leguminosae lectins. Both lectins have recently been shown to possess enhanced affinities and extended binding sites for the trisaccharide,
Thermodynamics of binding of the core trimannoside of asparagine-linked carbohydrates and deoxy analogs to Dioclea grandiflora lectin.
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The Man/Glc-specific seed lectin from Dioclea grandiflora (DGL) is a member of the Diocleinae subtribe that includes the jack bean lectin concanavalin A (ConA). Both DGL and ConA bind with high affinity to the "core" trimannoside moiety, 3, 6-di-O-(alpha-D-mannopyranosyl)-alpha-D-mannopyranoside,
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