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lectin/бересклет европейский
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Distribution of carbohydrates recognized by the lectins Euonymus europaeus and concanavalin A in monoxenic and heteroxenic trypanosomatids.
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We observed a wide distribution of the carbohydrate epitopes galactosyl alpha(1-3)galactose (gal alpha1-3 gal), alpha-glucoside and alpha-mannoside in mono- and heteroxenic trypanosomatids by using fluorescein-labelled lectins of Euonymus europaeus (EE) and Concanavalin A (Con A) as well as sera
The carbohydrate-binding promiscuity of Euonymus europaeus lectin is predicted to involve a single binding site.
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Euonymus europaeus lectin (EEL) is a carbohydrate-binding protein derived from the fruit of the European spindle tree. EEL was first identified for its erythrocyte agglutinating properties and specificity for B and H blood groups. However, a detailed molecular picture of the structural basis of
Euonymus europaeus lectin as an endothelial and epithelial marker in canine tissues.
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The Euonymus europaeus agglutinin (EEA) is an endothelial marker in mammalia. In canine tissues, 4 types of endothelial cells (general, nervous, arterial, hepatic) were identified by the presence of the EEA receptor and by its sensitivity to neuraminidase enhancement. In adult dogs, EEA binding
[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
Effect of sequential glycolysis of the lectin of Euonymus europaeus on activation of the classical complement pathway in normal human serum.
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The lectin of Euonymus europaeus at concentrations of 5-21 micrograms/ml causes activation of the classical complement (C) pathway (C1, C4, C2) when added to normal human serum at 37 degrees C. At higher concentrations, C3 is also consumed. The effect is dependent on a 'natural antibody' in serum of
Studies on Galalpha3-binding proteins: comparison of the glycosphingolipid binding specificities of Marasmius oreades lectin and Euonymus europaeus lectin.
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The carbohydrate binding preferences of the Galalpha3Galbeta4 GlcNAc-binding lectins from Marasmius oreades and Euonymus europaeus were examined by binding to glycosphingolipids on thin-layer chromatograms and in microtiter wells. The M. oreades lectin bound to Galalpha3-terminated
Isolation and immunochemical characterization of the Euonymus europaeus lectin receptor from the major sialoglycoprotein of human O erythrocytes.
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Purification of the Euonymus europaeus lectin by affinity chromatography on the desialized MN blood group glycoprotein, and lectin NH2-terminal analysis.
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Ulex europaeus 1 lectin targets microspheres to mouse Peyer's patch M-cells in vivo.
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The interaction of latex microspheres with mouse Peyer's patch membranous M-cells was studied in a mouse gut loop model after the microspheres were coated with a variety of agents. Carboxylated microspheres (diameter 0.5 micron) were covalently coated with lectins Ulex europaeus 1, Concanavalin A,
Lectin-binding properties of Aeromonas caviae strains.
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The cell surface carbohydrates of four strains of Aeromonas caviae were analyzed by agglutination and lectin-binding assays employing twenty highly purified lectins encompassing all sugar specificities. With the exception of L-fucose and sialic acid, the sugar residues were detected in A. caviae
Lectin activity of the nucleocytoplasmic EUL protein from Arabidopsis thaliana.
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The Euonymus lectin (EUL) domain was recognized as the structural motif for a novel class of putative carbohydrate binding proteins. Confocal microscopy demonstrated that the lectin from Euonymus europaeus (EEA) as well as the EUL protein from Arabidopsis thaliana (ArathEULS3) are located in the
Lectin binding defines and differentiates M-cells in mouse small intestine and caecum.
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M-cell surface glycoconjugate expression was investigated by applying a panel of lectins to whole fixed mouse Peyer's and caecal patches. While the majority of lectins failed to identify mouse M-cells, the lectin Euonymus europaeus differentially stained the surface of M-cells in both mouse Peyer's
Capture of cell culture-derived influenza virus by lectins: strain independent, but host cell dependent.
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Strategies to control influenza outbreaks are focused mainly on prophylactic vaccination. Human influenza vaccines are trivalent blends of different virus subtypes. Therefore and due to frequent antigenic drifts, strain independent manufacturing processes are required for vaccine production. This
Selective lectin reactions of two stocks of Leishmania enriettii with differing pathogenicity.
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Five days old promastigote culture forms of two stocks of Leishmania enriettii pathogenic and non-infective for Cavia procellus, were tested with the lectins of Canavalia ensiformis, Ricinus communis-120, Soja hispida (Glycine maxima), Arachis hypogaea, Ulex europaeus, Ulex europaeus I, Ulex
Lectin interactions with alpha-galactosylated xenoantigens.
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alpha-Galactosylated xenoantigens (Galalpha1-3Galbeta1-4GlcNAcbeta1 and Galalpha1-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc) are often detected with the alpha-Gal specific lectin Griffonia simplicifolia 1 isolectin B4 (GS1 B4). However, this lectin exhibits a broad and variable specificity for
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