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sophora chrysophylla/carbohydrate

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Rabbit anti-carbohydrate antibody elicited by the lymphocyte mitogenic glycoprotein from Wistaria floribunda seeds.

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Rabbit antibody produced in response to the purified mitogenic glycoprotein lectin from Wistaria floribunda seeds (WFM) contains anti-carbohydrate antibody. This antibody, which represents 25% of the total antibody precipitated by the homologous antigen cross-reacts with the glycoprotein

Direct carbohydrate analysis of glycoproteins electroblotted onto polyvinylidene difluoride membrane from sodium dodecyl sulfate-polyacrylamide gel.

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A procedure for the carbohydrate analysis of glycoproteins electrotransferred to a polyvinylidene difluoride membrane is described. The glycoproteins (plant lectins, transferrin, and vitronectin) were first separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and then

The glycoprotein-bound large carbohydrates from embryonal carcinoma cells carry receptors for several lectins recognizing N-acetylgalactosamine and galactose.

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When various lectins were mixed with radioactively labeled embryoglycan (polylactosamine-type glycoprotein-bound carbohydrates from early embryonic cells) isolated from F9 embryonal carcinoma cells and the resulting complex was precipitated with ammonium sulfate, the glycan was found to react with

Primary structure of an N-glycosidic carbohydrate unit derived from Sophora japonica lectin.

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The lectin isolated from Sophora japonica seeds is a glycoprotein which binds oligosaccharides with non-reducing terminal Gal beta(1----3/4)GlcNac beta 1----units. The carbohydrate moiety of the lectin is composed of fucose, xylose, mannose and N-acetylglucosamine. The major glycopeptide of the

Lectin mapping reveals stage-specific display of surface carbohydrates in in vitro and haemolymph-derived cells of the entomopathogenic fungus Beauveria bassiana.

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The entomopathogenic fungus Beauveria bassiana and its insect host target represent a model system with which to examine host-pathogen interactions. Carbohydrate epitopes on the surfaces of fungal cells play diverse roles in processes that include adhesion, non-self recognition and immune invasion

The role of carbohydrates in the IgG binding and suppressive activities of shed human Fc receptors.

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IgG Fc receptor (Fc gamma R) shed from human peripheral mononuclear cells and purified by IgG affinity chromatography bound to ConA, Pisum sativum, Ulex europeus and peanut lectins. The soluble Fc gamma R was not absorbed by wheat germ, soyabean, lentil, Sophora japonica or Helix pomotia lectins.

[Dissecting aneurysm of the aorta: histochemical study using a set of lectins with different carbohydrate specificity].

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By means of lectin-peroxidase technique histotopography of receptor sites for Ricinus communis agglutinin (RCA), peanut agglutinin (PA), soybean agglutinin (SA), Sophora japonica lectin (SJL), wheat germ agglutinin (WGA), Laburnum anagyroides lectin (LAL), Lotus tetragonolobus lectin (LTL) and

[Inhibition by carbohydrates of 4 lestins sensitive to galactose (Cytisus sessilifolius L., Coronilla varia L., Genista scoparia Lam., Sophora japonica L.). Consequence of the substitution by electron attracting radicals].

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The beta 1----2-D-xylose and alpha 1----3-L-fucose substituted N-linked oligosaccharides from Erythrina cristagalli lectin. Isolation, characterisation and comparison with other legume lectins.

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The carbohydrate moieties of Erythrina cristagalli lectin were released as oligosaccharides by hydrazinolysis, followed by N-acetylation and reduction with NaB3H4. Fractionation of the tritium-labelled oligosaccharide mixture by Bio-Gel P-4 column chromatography and high-voltage borate

Solid-phase assay of lectin activity using HRP-conjugated glycoproteins.

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Various enzyme-conjugated probes have been widely used for detection of specific interactions between biomolecules. In the case of glycan-protein interaction, horseradish peroxidase (HRP)-conjugated glycoproteins (HRP-GPs) are useful for the detection of carbohydrate-binding activity of plant and

A novel mannose-specific and sugar specifically aggregatable lectin from the bark of the Japanese pagoda tree (Sophora japonica).

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A new D-mannose/D-glucose-specific lectin (B-SJA-II) was isolated from the bark of the Japanese pagoda tree, Sophora japonica. B-SJA-II was separated from a well known D-galactose/N-acetyl-D-galactosamine-specific lectin (B-SJA-I) by affinity chromatography on lactamyl-Sepharose, then purified by

Seed chemistry of Sophora chrysophylla (mamane) in relation to diet of specialist avian seed predator Loxioides bailleui (palila) in Hawaii.

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This study describes the chemical ecology of a tritrophic interaction among species endemic to the island of Hawaii, USA: a tree (Sophora chrysophylla: mamane), an endangered bird (Loxioides bailleui; palila), and moth larvae (Cydia spp.). Palila and Cydia both specialize on the seed embryos of

Reactivity of five N-acetylgalactosamine-recognizing lectins with preimplantation embryos, early postimplantation embryos, and teratocarcinoma cells of the mouse.

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The expression of receptors for N-acetylgalactosamine-recognizing lectins, namely Helix pomatia agglutinin (HPA), Sophora japonica agglutinin (SJA), Bauhinia purpurea agglutinin (BPA), Vicia villosa agglutinin (VVA), and Wistaria floribunda agglutinin (WFA) was studied in early mouse embryos and
Alterations in cell surface carbohydrates on human lymphoma cell lines with different spontaneous metastatic potential in the severe combined immunodeficiency (SCID) mouse model were analyzed. A difference in cell surface carbohydrates between high- (HBL-2, HBL-7 and HBL-8) and no- or low-(HBL-4,

Demonstration of sugar residues in the ultimobranchial tubule and thyroid C-cells of the rat using peroxidase labelled lectins.

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The distribution of various sugars, that contribute to the composition of the carbohydrate components of the glycoprotein in the ultimobranchial tubule and the thyroid C-cells has been studied, using eight peroxidase-labelled lectins (Dolichos biblorus, Glycine max, Bauhinia purpurea, Helix pomatia,
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