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ulex europaeus/carbohydrate
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Stranica 1 iz 222 rezultatima
A putative carbohydrate-binding domain of the lactose-binding Cytisus sessilifolius anti-H(O) lectin has a similar amino acid sequence to that of the L-fucose-binding Ulex europaeus anti-H(O) lectin.
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The complete amino acid sequence of a lactose-binding Cytisus sessilifolius anti-H(O) lectin II (CSA-II) was determined using a protein sequencer. After digestion of CSA-II with endoproteinase Lys-C or Asp-N, the resulting peptides were purified by reversed-phase high performance liquid
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
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
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
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
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,
Localization of binding sites of Ulex europaeus I, Helix pomatia and Griffonia simplicifolia I-B4 lectins and analysis of their backbone structures by several glycosidases and poly-N-acetyllactosamine-specific lectins in human breast carcinomas.
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Several studies have shown the deletion of blood group A or B antigens and the accumulation of H antigens in human breast carcinomas. Other studies have independently demonstrated that the binding sites of lectins such as Helix pomatia agglutinin (HPA) and Griffonia simplicifolia agglutinin I-B4
Biological activities of carbohydrate-branched chitosan derivatives.
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Two types of biological activities of the carbohydrate-branched chitosan derivatives were investigated. One is the specific interaction with lectins and bacterium. The other is activation of canine polymorphonuclear leukocyte (PMN) cells. The specific bindings of the L-fucose-branched chitosan
Qualitative and quantitative alterations of cell surface carbohydrate residues during epidermal morphogenesis.
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The purpose of this study was to investigate the carbohydrate residue composition of cell surface in the developing epidermis and to define the chronological sequence of its alterations in human fetuses from the 10th to the 20th weeks of gestation and at the 23rd week of gestation, using a panel of
Altered carbohydrate composition in colorectal adenomas and carcinomas: histochemical characterization of N-acetylgalactosamine, L-fucose, and o-acetylated sialic acid.
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Changes of surface sugar residues in the large intestinal mucosa may be associated with malignant transformation and may be of importance in differentiating borderline lesions. To compare these changes in normal mucosa, adenomas, and carcinomas of the large intestine, we investigated modifications
Correlation between carbohydrate-binding specificity and amino acid sequence of carbohydrate-binding regions of Cytisus-type anti-H(O) lectins.
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A carbohydrate-binding peptide of the di-N-acetylchitobiose-binding Cytisus sessilifolius anti-H(O) lectin I (CSA-I) was isolated from the endoproteinase Asp-N digest of CSA-I by affinity chromatography on a column of N-acetyl-D-glucosamine oligomer-Sepharose (GlcNAc oligomer-Sepharose). The amino
Cell surface carbohydrates in psoriasis. Defective cytoplasmic transport by glycoconjugates carrying fucose residues suggested by lectin staining.
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Eleven biopsy specimens of normal skin and twenty-four biopsy specimens of psoriatic lesions were examined histochemically by using several lectins (Ulex europaeus, UEA-1; Dolichos biflorus, DBA; Bandeirea simplicifolia, BS-I; Concanvalia ensiformis, Con A; Triticum vulgaris, WGA; Ricinus communis,
A unique amino acid sequence involved in the putative carbohydrate-binding domain of a legume lectin specific for sialylated carbohydrate chains: primary sequence determination of Maackia amurensis hemagglutinin (MAH).
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The primary sequence of 247 amino acids of Maackia amurensis hemagglutinin (MAH) was determined using a protein sequencer. After digestion with endoproteinase Lys-C, Asp-N, Arg-C, or Glu-C of MAH, the resulting peptides were purified by reversed phase high performance liquid chromatography (HPLC)
Development of gastrointestinal surface. VIII. Lectin identification of carbohydrate differences.
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Binding of microvillus membranes (MVM) from newborn and adult rats by concanavalin A (Con A), Ulex europaeus (UEA I), Dolichos bifluorus (DBA), and Triticum vulgaris (WGA) was examined to determine the availability of carbohydrate-containing sites for these lectins on the intestinal surface during
Cell surface carbohydrates and glomerular targeting of olfactory sensory neuron axons in the mouse.
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Cell surface carbohydrates have been implicated in axon guidance and targeting throughout the nervous system. We have begun to test the hypothesis that, in the olfactory system, a differential distribution of cell surface carbohydrates may influence olfactory sensory neuron (OSN) axon targeting.
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