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ricinus/carbohydrate
Ο σύνδεσμος αποθηκεύεται στο πρόχειρο
Σελίδα 1 από 60 Αποτελέσματα
Expression profiles of genes related to carbohydrate metabolism provide new insights into carbohydrate accumulation in seeds and seedlings of Ricinus communis in response to temperature.
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Ricinus communis possesses a specific metabolic signature to adjust growth and developmental processes in response to temperature: carbohydrates are accumulated at low temperatures, whereas amino acids are accumulated at elevated temperatures. Our objective was to assess tissue-specific changes in
The histochemistry of galactose residues of complex carbohydrates as studied by peroxidase-labeled Ricinus communis agglutinin.
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A peroxidase-labeled Ricinus communis agglutinin diaminobenzidine (PO-RCA-DAB) procedure has been utilized to determine the light microscopic localization of galactose residues of complex carbohydrates in a variety of tissues from different vertebrate species. In the same tissues, the localization
Synthesis and carbohydrate-binding activity of poly(ethyleneglycol)-Ricinus communis agglutinin I conjugates.
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The synthesis of poly(ethyleneglycol) (PEG)-lectin conjugates was investigated to provide new reagents for evaluation as biological response modifiers. PEG was activated with 1,1'-carbonyldiimidazole (CDI), followed by conjugation with Ricinus communis I (RCAI) lectin. The resulting conjugates were
Root cooling strongly affects diel leaf growth dynamics, water and carbohydrate relations in Ricinus communis.
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In laboratory and greenhouse experiments with potted plants, shoots and roots are exposed to temperature regimes throughout a 24 h (diel) cycle that can differ strongly from the regime under which these plants have evolved. In the field, roots are often exposed to lower temperatures than shoots.
Ricinus communis agglutinin-mediated agglutination and fusion of glycolipid-containing phospholipid vesicles: effect of carbohydrate head group size, calcium ions, and spermine.
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The glycolipids galactosylcerebroside (GalCer), lactosylceramide (LacCer), and trihexosylceramide (Gb3) were inserted into phospholipid vesicles, consisting of phosphatidylethanolamine and phosphatidic acid. The extent to which their carbohydrate head groups protruded beyond the vesicle surface and
Defining carbohydrate specificity of Ricinus communis agglutinin as Gal beta 1-->4GlcNAc (II) > Gal beta 1-->3GlcNAc (I) > Gal alpha 1-->3Gal (B) > Gal beta 1-->3GalNAc (T).
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To define carbohydrate specificity of Ricinus communis agglutinin (RCA1), the combining site of RCA1 was further characterized by quantitative precipitin (QPA) and precipitin-inhibition assays (QPIA). Among the oligosaccharides tested for QPIA, Gal beta 1-->4GlcNAc (II, human blood group type II
[Inhibition by cysteine of the carbohydrate-binding activity of lectins from Ricinus communis, Canavalia ensiformis and Euonymus europaeus].
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Precipitation induced by different lectins has been studied in the presence of some aminoacids. It was shown that precipitates formed by lectins from Ricinus communis (RCA1), Canavalia ensiformis (Con A), Euonymus europaeus (Eel) in the presence of appropriate carbohydrate-containing molecules
Evaluation of the stoichiometry and energetics of carbohydrate binding to Ricinus communis agglutinin: a calorimetric study.
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High-sensitivity isothermal titration calorimetry has been used to investigate the thermodynamics of binding of Ricinus communis agglutinin to galactose, lactose and their derivatives in the temperature range 280.5-298 K. The present study unequivocally establishes the carbohydrate-binding
Carbohydrate recognition factors of the lectin domains present in the Ricinus communis toxic protein (ricin).
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Ricin (RCA60) is a potent cytotoxic protein with lectin domains, contained in the seeds of the castor bean Ricinus communis. It is a potential biohazard. To corroborate the biological properties of ricin, it is essential to understand the recognition factors involved in the ricin-glycotope
Novel interactions of complex carbohydrates with peanut (PNA), Ricinus communis (RCA-I), Sambucus nigra (SNA-I) and wheat germ (WGA) agglutinins as revealed by the binding specificities of these lectins towards mucin core-2 O-linked and N-linked glycans and related structures.
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Plant lectins through their multivalent quaternary structures bind intrinsically flexible oligosaccharides. They recognize fine structural differences in carbohydrates and interact with different sequences in mucin core 2 or complex-type N-glycan chain and also in healthy and malignant tissues. They
Colorimetric detection of Ricinus communis Agglutinin 120 using optimally presented carbohydrate-stabilised gold nanoparticles.
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Ricin is a toxic lectin which presents a potential security threat. Its rapid detection is highly desirable. Here we present a colorimetric bioassay based on the aggregation of carbohydrate-stabilised gold nanoparticles which has been used to detect Ricinus communis Agglutinin 120 (RCA(120)) - a
Studies on Ricinus communis lectin--carbohydrate interaction by means of affinity electrophoresis.
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The affinity gel electrophoresis of lectins purified from the seeds of Ricinus communis was studied. The mobilities of lectins on the gel showed various degree of retardation with their affinity toward their macromolecular ligand-agarose. Ricinus agglutinin which possessed the strongest affinity was
The affinity of the lectins Ricinus communis and Glycine maxima to carbohydrates on the cell surface of various forms of Trypanosoma cruzi and Trypanosoma rangeli, and the application of these lectins for the identification of T. cruzi in the feces of Rhodnius prolixus.
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Flagellates of Trypanosoma cruzi (stock Molino 1), obtained from the intestine of experimentally infected Rhodnius prolixus, grown in cellular or acellular culture, as well as from the blood of infected mice, were examined by a direct fluorescence test using the lectins RCA (Ricinus communis-120)
Surface carbohydrates of hamster fibroblasts. II. Interaction of hamster NIL cell surfaces with Ricinus communis lectin and concanavalin A as revealed by surface galactosyl label.
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When hamster fibroblasts (NIL) were treated with galactose oxidase followed by reduction with tritiated borohydride (GAHMBERG, C. G. AND HAKOMORI, S. (1973) J. Biol. Chem. 248, 4311; STECK, T. L., AND DAWSON, G. (1974) J. Biol. Chem. 249, 2135), two major galactoprotein labels were detected on the
On the specificity of carbohydrate-lectin recognition. The interaction of a lectin from Ricinus communis beans with simple saccharides and concanavalin A.
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