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viscum verrucosum/carbohydrate
Link salvestatakse lõikelauale
Leht 1 alates 100 tulemused
Seasonal and spatial variation of carbohydrates in mistletoes (Viscum album) and the xylem sap of its hosts (Populus x euamericana and Abies alba).
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In the present field study we analysed the seasonal pattern of carbohydrate composition and contents in the xylem sap of Viscum album and the xylem sap of a deciduous (Populusxeuramericana) and a coniferous (Abies alba) host tree species. The results were compared with the soluble carbohydrate
Influence of carbohydrates on the cytotoxicity of an aqueous mistletoe drug and of purified mistletoe lectins tested on human T-leukemia cells.
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Partially and highly purified lectins from Viscum album L. (mistletoe) cause a dose-dependent decrease of viability of human leukemia cell cultures, MOLT-4, after 72 h treatment. The LC50 of the partially purified lectin was 27.8 ng/ml, of the highly purified lectin 1.3 ng/ml. Compared to the highly
Modulation of mistletoe (Viscum album L.) lectins cytotoxicity by carbohydrates and serum glycoproteins.
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Three D-galactose and/or N-acetyl-D-galactosamine specific mistletoe lectins, ML I, ML II and ML III, were purified by affinity chromatography followed by cation exchange chromatography. These lectins were toxic for Molt 4 cells in culture at concentrations in the pg/ml range, ML III being the most
Carbohydrate specificity of the receptor sites of mistletoe toxic lectin-I.
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The carbohydrate specificity of mistletoe toxic lectin-I (ML-I) was studied by haemagglutination-inhibition assay. The results indicated that ML-I has a broad range of affinity for Gal alpha,beta linked sequences. The galabiose (E, Gal alpha 1----4Gal) sequence, a receptor of the uropathogenic E.
Differences in amino acid sequences of mistletoe lectin I and III B-subunits determining carbohydrate binding specificity.
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Toxic lectins of European mistletoe Viscum album L.--MLI (viscumin), MLII and MLIII--are present in water extracts of this plant. Earlier we have cloned the full-length gene of MLIII precursor [A.G. Tonevitsky, I.I. Agapov, I.B. Pevzner, N.V. Maluchenko, M.M. Mojsenovich, U. Pfueller, M.P.
Mistletoe effects on Scots pine decline following drought events: insights from within-tree spatial patterns, growth and carbohydrates.
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Forest decline has been attributed to the interaction of several stressors including biotic factors such as mistletoes and climate-induced drought stress. However, few data exist on how mistletoes are spatially arranged within trees and how this spatial pattern is related to changes in radial
NMR investigations of protein-carbohydrate interactions: insights into the topology of the bound conformation of a lactose isomer and beta-galactosyl xyloses to mistletoe lectin and galectin-1.
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A hallmark of oligosaccharides is their often limited spatial flexibility, allowing them to access a distinct set of conformers in solution. Viewing each individual or even the complete ensemble of conformations as potential binding partner(s) for lectins in protein-carbohydrate interactions, it is
Pneumocystis carinii: surface reactive carbohydrates detected by lectin probes.
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Pneumocystis carinii obtained from rat lungs (RLH) and in vitro culture (RTC) were reacted with a panel of 14 fluorescein isothiocyanate conjugated lectins. Percentage fluorescence and fluorescent intensity were determined for both trophic and cyst forms. All RLH and RTC derived organisms bound
Flow cytometric analyses of lectin binding to Pneumocystis carinii surface carbohydrates.
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Pneumocystis carinii obtained from infected rat lung homogenates was incubated with fluorescein isothiocyanate-conjugated lectins, counterstained with the nuclear stain, propidium iodide (PI), and analyzed by dual parameter histograms for lectin-associated green and PI-associated red fluorescence
Suitability of binary mixtures of water with aprotic solvents to turn hydroxyl protons of carbohydrate ligands into conformational sensors in NOE and transferred NOE experiments.
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The structural analysis of protein-carbohydrate interactions is essential for the long-range aim to sort out entropic/ enthalpic factors in the binding process. Of conspicuous clinical interest, this work can also offer the perspective to devise new classes of therapeuticals which interfere with
Persubstituted cyclodextrin-based glycoclusters as inhibitors of protein-carbohydrate recognition using purified plant and mammalian lectins and wild-type and lectin-gene-transfected tumor cells as targets.
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Multivalent glycoclusters have the potential to become pharmaceuticals by virtue of their target specificity toward clinically relevant sugar receptors. Their application can also provide fundamental insights into the impact of two spatial factors on binding, i.e., topologies of ligand (branching
Carbohydrate-binding proteins (plant/human lectins and autoantibodies from human serum) as mediators of release of lysozyme, elastase, and myeloperoxidase from human neutrophils.
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Analysis of cell surface glycosylation not only provides information about cell properties such as their state of differentiation or histogenetic lineage. The carbohydrate chains also provide potentially functional binding sites to endogenous carbohydrate-binding proteins. This interaction can
Are matrix-immobilized neoglycoproteins, plant and human lectins and carbohydrate--binding antibodies from human serum mediators of adhesion in vitro for carcinoma and lymphosarcoma cells?
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Mediation of cell adhesion by defined molecules can be studied by their immobilization onto a nitrocellulose matrix and incubation with cells. In order to infer the capacity of deliberately selected protein-carbohydrate interactions to establish sugar-inhibitable cell adhesion, a panel of
Structural analysis of the carbohydrate chains isolated from mistletoe (Viscum album) lectin I.
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Two glycopeptide fractions prepared from mistletoe (Viscum album) lectin I by Pronase digestion were fractioned by affinity chromatography on a concanavalin A-Sepharose column. With 400-MHz 1H NMR spectroscopy, in conjunction with sugar analysis, the following oligosaccharide structures could be
Cell-type dependence of stability modulation of lectin-initiated contacts by impairment of multivalent carbohydrate binding and intracellular signaling.
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Initial ligand selection and the intermolecular spatial arrangement of glycan-lectin complexes are assumed to be essential to induce formation of stable cell aggregates by a lectin. To distinguish effects of these two processes, the tetrameric mistletoe lectin and its isolated B-chain were used. A
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