Localization and time of synthesis of wheat germ agglutinin in developing wheat (Triticum aestivum, L.)
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The activity of a highly purified plant lectin, wheat germ. agglutinin (WGA), has been detected in wheat embryos as young as days post-anthesis. The amount of hemagglutinating activity present. in young embryos increases to a maximum level at 45 days post-anthesis. The lectin, wheat germ agglutinin (WGA), is synthesized de novo by developing wheat (Triticum aestivum, L.) embryos but is not synthesized or localized in developing endosperm as shown by radioimmunoassay.
Young embryos removed from the grain and cultured on a defined medium germinate precociously and concomitantly cease WGA by: The time course of appearance of wheat-germ agglutinin (WGA) in the various embryonic tissues during embryogenesis in Triticum aestivum L.
was studied by s The radicle, root cap and coleorhiza first accumulated WGA in early Stage II ( d post-anthesis) prior to the main period of embryo growth, while WGA was found in the epiblast and coleoptile in early and late State III, by: Localization and time of synthesis of wheat germ agglutinin in developing wheat (Triticum aestivum, L.)Cited by: 1.
Localization of wheat-germ agglutinin in developing wheat embryos and those cultured in abscisic acid N.V. Raikhel1* and R.S.
Quatrano2 1 Department of Botany, University of Georgia, Athens, G Aand 2 Department of Botany and Plant Patho*logy, Oregon State University, Corvallis, ORUSA Abstract.
The time course of appearance of wheat. Dev Biol. Jun;91(2) Timing, localization, and control of wheat germ agglutinin synthesis in developing wheat embryos. Triplett BA, Quatrano by: The biosynthesis and processing of wheat-germ agglutinin (WGA) were studied in developing wheat (Triticum aestivum L.
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Marshall) embryos using pulse-chase labeling, subcellular fractionation and immunocytochemistry. A substantial amount of newly synthesized WGA was organelle-associated. Isolation of WGA on affinity columns of immobilized N Cited by: Characteristics of two wheat germ agglutinin-resistant variants of B16 mouse melanoma cells with reduced tumorigenicity.
Carbohydrate Research, DOI: /S(00) N. Raikhel, R. Quatrano. Localization of wheat-germ agglutinin in developing wheat embryos and those cultured in abscisic by: Abstract. Wheat germ agglutinin was found to increase glutamine synthetase and nitrogenase activities and excretion of N 2-fixation product (NH 4 +) in Azospirillum brasilense Sp Each effect had a similar pattern and correlated well with each by: Mundy J, Chua NH.
Abscisic acid and water-stress induce the expression of a novel rice gene. EMBO J. Aug; 7 (8)– [PMC free article] Triplett BA, Quatrano RS. Timing, localization, and control of wheat germ agglutinin synthesis in developing wheat embryos. Dev Biol. Jun; 91 (2)–Cited by: Each protomeric unit of wheat germ agglutinin consists of 4 structurally homologous domains with a high degree of amino acid sequence homology among the 4 domains.
Four interlocking disulfide bonds, each within one of the 4 domains, result in a highly compact stable protein . Wheat germ agglutinin (WGA) is the first studied plant lectin shown to bind more strongly to tumour cells than to normal ones. WGA interacts with. Wheat germ agglutinin (WGA) is a lectin that protects wheat from insects, yeast and agglutinin protein, it binds to N-acetyl-D-glucosamine and Sialic acid.
N-acetyl-D-glucosamine in the natural environment of wheat is found in the chitin of insects, and the cell membrane of yeast & bacteria.
WGA is found abundantly—but not exclusively—in the wheat kernel, where it got the 'germ Organism: Triticum aestivum. The inhibition of carbohydrate−protein interactions by tailored multivalent ligands is a powerful strategy for the treatment of many human diseases. Crucial for the success of this approach is an understanding of the molecular mechanisms as to how a binding enhancement of a multivalent ligand is achieved.
Details Localization and time of synthesis of wheat germ agglutinin in developing wheat (Triticum aestivum, L.) PDF
We have synthesized a series of multivalent N-acetylglucosamine (GlcNAc). Production of an Antibody Specific for the Propeptide of Wheat Germ Agglutinin Article (PDF Available) in Plant physiology 91(2) November.
A liquid phase, competition-binding radioimmunoassay for wheat germ agglutinin, with a detection limit of 10 nanograms, was developed in order to determine the distribution of this lectin in young wheat plants. Affinity columns for wheat germ agglutinin removed all antigenically detectable activity from crude extracts of wheat tissue; thus, the Cited by: Inouye (6).
Wheat germ agglutinin gave a single band, and a molecular weight of 23, to 24, was estimated. Earlier data on partially purified wheat germ agglutinin gave a molecular weight of 26, (2).
Amino Acid and Carbohydrate Compositions-Crystalline wheat germ agglutinin (1 mg) was hydrolyzed in 6 N HCI at ” for. Search results for wheat germ agglutinin at Sigma-Aldrich.
Now that celiac disease has been allowed official entry into the pantheon of established medical conditions, and gluten intolerance is no longer entirely a fringe medical concept, the time has come to draw attention to the powerful little chemical in wheat known as ‘wheat germ agglutinin’ (WGA) which is largely responsible for many of wheat’s pervasive, and difficult to diagnose, ill.
We generated transgenic mice in which a trans-synaptic tracer, wheat germ agglutinin (WGA), was specifically expressed in the locus coeruleus (LC) neurons under the control of the dopamine-β-hydroxylase (DBH) gene promoter.
WGA protein was produced in more than 95% of the tyrosine hydroxylase (TH)-positive LC neurons sampled. Transynaptic transfer of WGA was Cited by: columns for wheat germ agglutinin removed al antigenicaily detectable activity from crude extracts of wheat tissue; thus, the antigenic cross-reactivitydetected bytheassaypossessessugar-binding specificity similar to the wheat germ-derived lectin.
The amount oflectin per dry grain is approximately 1 microgram, al associated 34daysofCited by: Wheat germ agglutinin (WGA) contains a group of closely related isolectins, with an isoelectric point about pH 9.
This lectin is used for the purification of insulin receptors and for neuronal tracing. Inhibiting/Eluting Sugar: Chitin Hydrolysate or mM N-acetylglucosamine with salt and/or acid elution generally required.
In solution, wheat germ agglutinin exists as a heterodimer with a molecular weight of approximat daltons and is normally cationic under physiological conditions.
Molecular Probes® offers a broad selection of fluorescent wheat germ agglutinin conjugates. Table 1 provides a summary of peak excitation and emission wavelengths. The Wheat File Size: KB. Outsource the entire localization process without having to worry about finding and characterizing target specific antibodies, sourcing and validating difficult-to-find tissues, and having the ability to interpret the resulting immunostaining in relation to complex human pathologies.
WGA / Wheat Germ Agglutinin WGA / Wheat Germ Agglutinin. Wheat germ agglutinin (WGA) is one of the most widely used lectins in cell biology. Our Texas Red-X conjugate of WGA exhibits the bright, red fluorescence of the Texas Red dye (excitation/emission maxima ~/ nm).
Texas Red-X WGA binds to sialic acid and N-acetylglucosaminyl residues. Developing tools for investigating the cellular activity of glycans will help to delineate the molecular basis for aberrant glycosylation in pathological processes such as cancer.
Metabolic oligosaccharide engineering, which inserts sugar-reporting groups into cellular glycoconjugates, represents a powerful method for imaging the localization, trafficking, and Cited by: Crystalline wheat germ agglutinin was prepared from unprocessed wheat germ by a new purification procedure.
Its purity and some of its molecular characteristics were examined by a number of criteria. the agglutinin dimerizes with a molecular weight of aro and a sedimentation coefficient of S.
Amino acid analyses indicate that. Selective wheat germ agglutinin (WGA) uptake in the hippocampus from the locus coeruleus of dopamineβ-hydroxylase-WGA transgenic mice. The central adrenergic system.
An immunoﬂuorescence study of the location of cell bodies and their efferent connections in the rat utilizing dopamine-betahydroxylase as a marker. A series of six mono- di- and trivalent N,N’-diacetylchitobiose derivatives was conveniently prepared by employing a one-pot procedure for Cu(II)-catalyzed diazo transfer and Cu(I)-catalyzed azide–alkyne cycloaddition (CuAAC) starting from commercially available glycoclusters were probed for their binding potencies to the plant lectin wheat germ agglutinin Cited by: Wheat Germ agglutinin from Triticum vulgaris suitable for cell culture, lyophilized powder; find Sigma-Aldrich-L MSDS, related peer-reviewed papers, technical documents, similar products & more at Sigma-Aldrich.
This is how autoimmune conditions begin. It allows gliadin itself, gliadin fragments, wheat germ agglutinin and other lectins, bacterial lipopolysaccharide, and other bacterial components to enter the bloodstream. This is why wheat, rye, barley and corn are associated with type 1 diabetes, Hashimoto’s thyroiditism, and rheumatoid arthritis.
Molecular characterization of the WGA-Fc chimera. We expected the WGA-Fc chimeras to form a dimer of 2 identical aa chains in solution ( aa from WGA + 6 aa from thrombin cleavage site + Cited by: 9.Wheat germ agglutinin (WGA) gene expression and ABA accumulation in the developing embryos of wheat (Triticum aestivum) in response to drought.
Description Localization and time of synthesis of wheat germ agglutinin in developing wheat (Triticum aestivum, L.) FB2
Plant Growth Regulation, 30, – doi: /AAuthor: Л. В. Чеботарьова.
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