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Ricinus communis lectin

Lectin toxicity - nausea, diarrhea, headache, confusion, dehydration, death Wisteria, castor bean (Ricinus communis) Lectins bind to cell surfaces Ricin - blocks protein synthesis, very toxic, 5 to 6 beans can kill a child... [Pg.166]

Lectin PNA Arachis hypogaea Lectin RCA 120 Ricinus communis Lectin SNA Sambucus nigra... [Pg.173]

Changes in the capacity of hepatoma cells to the binding of Ricinus communis lectin have been noted after treatment with chondroitin lyase AC. The binding sites for this lectin, but not those for concanavalin A, are masked with chondroitin 4-sulphate. By use of a direct method for studying the binding... [Pg.331]

Relatively stable proteins isolated from human heart and from human and rhesus monkey skeletal muscles, are capable of binding to /3-D-galactosides. Gel precipitation and radioimmunoassay studies with rabbit antiserum to calf heart lectin revealed antigenic cross-reactions between the primate and bovine muscle lectins. The lectin from calf heart shows a greater specificity towards the terminal disaccharide (lactosamine) units of blood-group antigen precursor chains than does the Ricinus communis lectin. [Pg.337]

The hepatic-binding protein, which binds to terminal D-galactosyl residues of asialoglycoproteins, and the receptors for Ricinus communis lectin have been localized simultaneously on the plasma membrane of isolated rat hepatocytes. ... [Pg.374]

A heterogeneous population of serum glycoproteins, which bind to immobilized Ricinus communis lectin, have been isolated and shown to account for the inhibition of the binding of desialylized glycoprotein to the hepatocyte membrane.These glycoproteins are present in small amounts in normal human serum, but in increased levels in serum from patients with cirrhosis. [Pg.388]

Immobilized concanavalin A and immobilized Ricinus communis lectin have been used in the separation of Fc from Fab fragments of a myeloma immunoglobulin The Fc fragment binds to both lectins, but the Fab fragment only interacts with concanavalin A. [Pg.401]

Glycoproteins in the sputum of patients with chronic bronchitis have been solubilized and then fractionated on Sepharose 4B into components of high and low molecular weight The sputum of bronchial patients contains more components of low molecular weight. Mucins from macroscopically healthy areas of the bronchial mucosa of six adults are anionic and contain residues of sialic acid and sulphate. Affinity chromatography on immobilized Ricinus communis lectin has enabled the mucins and other glycoproteins secreted by human bronchia to be characterized. ... [Pg.356]

Purified and reduced human Factor VIII exhibits an eight band sub-unit structure (mol. wt. 3.0 X 10 —2.3 x 10 ) as shown by polyacrylamide gel electrophoresis. Rabbit antibody to Factor VIII reacts with all of the sub-units whereas haemophilic antibody reacts with low-molecular-weight sub-units only. Sub-units derived from the largest Factor VIII multimers have a higher binding affinity for D-galactose-specific lectins than have those obtained after reduction of smaller oligomers. Ristocetin cofactor activity of purified Factor VIII is competitively inhibited by two Ricinus communis lectins and by concanavalin A. [Pg.108]

A number of lectins have been purified by affinity chromatography on 0-glycosyl polyacrylamide gels. The physicochemical properties of well-characterized lectins such as Glycine soja, Dolichos biflorus, Phaseolus lunatus. Helix pomatia, and Ricinus communis lectins compared well with those of preparations obtained by alternative chromatographic systems. [Pg.304]

A protease-resistant, transformation sensitive membrane glycoprotein (subunit mol. wt. 1.7 x 10 ) and an intermediate filament-forming protein (IFF, mol. wt. 5.6 x 10 ) have been isolated from hamster embryo fibroblasts. A possible association of the two molecular species is suggested by the fact that the IFF can be co-purified with the glycoprotein using immobilized Ricinus communis lectin, although the IFF has no receptor for the lectin. [Pg.337]

There is still some discordance about markers for ATI cells [17, 18]. Varieties of glycocalyx appear to be expressed in ATI versus ATII cells, which can be distinguished by the binding of specific lectins. Lycopersicon esculen-tum lectin, for example, appears to adhere specifically to the apical plasma membrane of ATI cells [19, 20], Other lectin markers that have been reported in AEC typing are Ricinus communis agglutinin, Erythrina cristagalli lectin, soybean lectin and Bauhinia purpurea agglutinin (all for the ATI phenotype),... [Pg.261]

Circular dichroism (CD) has been utilized to investigate the effect of saccharides on the conformation of lectins in solution. CD has demonstrated saccharide-induced conformational changes in the lectins from Canavalia ensiformis (7), Dolichos biflorus (8), Ricinus communis (9), and Triticum vulgaris (10). The present study uses circular dichroism to assess the secondary structure of SBA and to measure conformational transitions induced by the saccharides which bind to this lectin. These and previous studies will contribute to a clearer understanding of the unique properties of these sugar-binding proteins. [Pg.67]

Ricinus lectin RCAii0 Ricinus communis GalNAc, (3-Gal, 3-Gal... [Pg.503]

Fig. 15.—Human IgA, Glycopeptide871 Showing the Carbohydrate-binding Loci for Various Lectins, [a. Limulus polyphemus b, Triticum vulgaris c, Ricinus communis d, Sophora japonica e, Abrus precatorius f, Cytisus sessilifolius g, Phaseolus vulgaris-, h, Canavalia ensiformis i, Lens culinaris j, Pisum sativus k, Vicia faba-, 1, Bandeiraea simplicifolia II m, Solanum tuberosum and n, Ulex europeus II.]... Fig. 15.—Human IgA, Glycopeptide871 Showing the Carbohydrate-binding Loci for Various Lectins, [a. Limulus polyphemus b, Triticum vulgaris c, Ricinus communis d, Sophora japonica e, Abrus precatorius f, Cytisus sessilifolius g, Phaseolus vulgaris-, h, Canavalia ensiformis i, Lens culinaris j, Pisum sativus k, Vicia faba-, 1, Bandeiraea simplicifolia II m, Solanum tuberosum and n, Ulex europeus II.]...
Ricin was found by Stillmark in 1889 as the first plant lectin derived from the seeds of the castor plant, Ricinus communis L., a member of the Euphorbiaceae or spurge family. Other members of this family include the popular houseplants poinsettia E. pulcherrima), and the croton species. The term castor bean is used commonly to refer to both the plant and seed of R. communis. Ricinus communis commonly grows along streams and riverbeds in addition to subtropical locations high in nutrients. Ricinus communis is a coarse perennial, 10-13 m tall in the tropics, with a stem 7.5-15 cm... [Pg.339]


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See also in sourсe #XX -- [ Pg.298 ]




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