euonymus/carbohydrate

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Promiscuity of the euonymus carbohydrate-binding domain.

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Plants synthesize small amounts of carbohydrate-binding proteins on exposure to stress. For example, on exposure to drought, high salt, wounding and by treatment with some plant hormones or by pathogen attack. In contrast to the 'classical' plant lectins that are mostly located in the vacuolar

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

[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

Inhibitory activity of Euonymus alatus against alpha-glucosidase in vitro and in vivo.

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The major goal in the treatment of diabetes mellitus is to achieve near-normal glycemic control. To optimize both fasting blood glucose and postprandial glucose levels is important in keeping blood glucose levels as close to normal as possible. alpha-Glucosidase is the enzyme that digests dietary

Composition and immunochemical properties of glycoproteins with anti-B agglutinin activity isolated from Euonymus sieboldiana seeds.

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Five major glycoproteins with anti-B agglutinin activity were isolated from seeds of Euonymus Sieboldiana by a procedure based on precipitation with ammonium sulphate, Sepharose 4B gel filtration, CM- and DEAE-Sepharose chromatography and Sephacryl S-200 gel filtration. The purified glycoproteins

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

Proteins with an Euonymus lectin-like domain are ubiquitous in Embryophyta.

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BACKGROUND Cloning of the Euonymus lectin led to the discovery of a novel domain that also occurs in some stress-induced plant proteins. The distribution and the diversity of proteins with an Euonymus lectin (EUL) domain were investigated using detailed analysis of sequences in publicly accessible

The "old" Euonymus europaeus agglutinin represents a novel family of ubiquitous plant proteins.

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Molecular cloning of the "old" but still unclassified Euonymus europaeus agglutinin (EEA) demonstrated that the lectin is a homodimeric protein composed of 152 residue subunits. Analysis of the deduced sequence indicated that EEA is synthesized without a signal peptide and undergoes no

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