ulex/carbohydrate

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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,

Purification and characterization of a Cytisus-type Ulex europeus hemagglutinin II by affinity chromatography.

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Ulex europeus hemagglutinin II [Cytisus-type anti-H(O) hemagglutinin] inhibited most by di-N-acetylchitobiose has been purified by affinity chromatography on a column of chitobiose-Sepharose 4B, followed by gel filtration on Sephacryl S-300. The purified hemagglutinin was homogeneous by

Purification and characterization of carbohydrate-binding peptides from Lotus tetragonolobus and Ulex europeus seed lectins using affinity chromatography.

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Carbohydrate-binding peptides of several anti-H(O) leguminous lectins were obtained from endoproteinase Asp-N or Lys-C digests of L-fucose-binding Lotus tetragonolobus lectin (LTA) and Ulex europeus lectin I (UEA-I) and from that of a di-N-acetylchitobiose-binding Ulex europeus lectin II (UEA-II) by

Purification and characterization of a new type lactose-binding Ulex europaeus lectin by affinity chromatography.

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A new type lactose-binding lectin was purified from extracts of Ulex europaeus seeds by affinity chromatography on a column of galactose-Sepharose 4B, followed by gel filtration on Sephacryl S-300. This lectin, designated as Ulex europaeus lectin III (UEA-III), was found to be inhibited by lactose.

[Interaction of carbohydrate-rich glycoprotein from human parotid saliva with concanavalin A and lectin H from Ulex europeus].

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Structural basis of carbohydrate recognition by lectin II from Ulex europaeus, a protein with a promiscuous carbohydrate-binding site.

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Protein-carbohydrate interactions are the language of choice for inter- cellular communication. The legume lectins form a large family of homologous proteins that exhibit a wide variety of carbohydrate specificities. The legume lectin family is therefore highly suitable as a model system to study

Lotus tetragonolobus, Ulex europaeus, Maackia amurensis, and Arachis hypogaea (peanut) lectins influence the binding of Helicobacter pylori to gastric carbohydrates.

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BACKGROUND The carbohydrates of gastric mucins and other sugar structures are involved in interactions with Helicobacter pylori (H. pylori) adhesins. The binding of bacteria to mucins can protect the epithelium from direct contact with the pathogen and from developing infection because of a specific

Isolation and characterization of a mitogenic substance for murine and human B lymphocytes from Ulex europeus seeds.

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A mitogenic substance, which stimulates murine and human B lymphocytes, has been isolated from the seeds of Ulex europeus. The m.w. of this mitogen was estimated to be approximately 100,000 by sodium dodecyl sulfate disc gel electrophoresis. Under physiologic conditions Ulex mitogen was in the form

Surface reaction of Leishmania. III. Ulex europaeus II lectin affinity for excreted factor (EF) serotype A strains.

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Eukaryotic parasites, including species of Leishmania, acquire or synthesize carbohydrate moieties similar to human blood group antigens. Leishmanial strains separate into three serotypes: A, B and AB. All strains containing the A component are agglutinated by Ulex europaeus lectin. Inhibition by

The 2.2 A resolution structure of the O(H) blood-group-specific lectin I from Ulex europaeus.

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The tertiary and quaternary structure of the lectin I from Ulex europaeus (UE-I) has been determined to 2.2 A resolution. UE-I is a dimeric metalloglycoprotein that binds the H-type 2 human blood group determinant [alpha-L-Fucalpha(1-->2)-beta-D-Galbeta(1-->4)-beta-D-Glc NAcalpha-]. Nine changes

Knowledge-based modeling of a legume lectin and docking of the carbohydrate ligand: the Ulex europaeus lectin I and its interaction with fucose.

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Ulex europaeus isolectin I is specific for fucose-containing oligosaccharide such as H type 2 trisaccharide alpha-L-Fuc (1-->2) beta-D-Gal (1-->4) beta-D-GlcNAc. Several legume lectins have been crystallized and modeled, but no structural data are available concerning such fucose-binding lectin. The

Specific carbohydrate expression by small-diameter subclasses of rabbit trigeminal, glossopharyngeal, and vagal afferent fibers studied with the lectin Ulex europaeus agglutinin I.

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Lectin Ulex europaeus agglutinin I (UEAI), which binds to some alpha-L-fucose containing carbohydrates, specifically labeled a subset of trigeminal, glossopharyngeal, and vagal ganglion cells and their axons in the rabbit. The UEAI-positive trigeminal afferent fibers traveled through the spinal

The fucosyl specific lectins of Ulex europaeus and Sarothamnus scoparius. Biochemical characteristics and binding properties to human B-lymphocytes.

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From the seeds of the gorse, Ulex europaeus and of the broom, Sarothamnus scoparius L-fucosyl-specific lectins were isolated by affinity chromatography on L-fucosyl-epoxy-Sepharose. The lectins showed similarities in their molecular weights, amino acid composition, carbohydrate content and in the

Glycoconjugate with Ulex europaeus agglutinin-I-binding sites in normal mucosa, adenoma, and carcinoma of the human large bowel.

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Cancerous lesions and nonneoplastic mucosa of surgically extirpated specimens from 94 patients with colorectal carcinoma (of the right colon, 31 patients; of the left colon, 29 patients; and of the rectum, 34 patients) and endoscopically polypectomized specimens from 18 patients with rectal adenoma

The use of the lectin Ulex europeus to study epithelial cell differentiation in neoplastic and non-neoplastic oral white lesions.

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Ulex europeus (Ulex 1) has been used to study the expression of cell surface alpha-L-fucose on oral epithelial cells of normal human mucosa, white lesions and carcinomas. In normal tissue and in 11 of 12 specimens of non-specific keratoses (leukoplakia), Ulex 1 stained epithelial spinous cells only.

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