Root Lectin
Mostrando 1-12 de 41 artigos, teses e dissertações.
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1. Análise estrutural do domínio de reconhecimento a carboidratos da lectina Dvirl de Dioclea virgata e sua correlação na indução da produção de óxido nítrico / Structural analysis of the carbohydrate recognition domain the DvirL lectin from Dioclea virgata and its correlation in the induction of nitric oxide production
Lectins are defined as proteins or glycoproteins of nonimmune origin that have at least one site of reversible binding to carbohydrates or glycoconjugates. Lectins of plant origin are the most studied and characterized as three-dimensional structure and biological functions related. Lectins can be found in different parts of the plant from its root to the in
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 22/07/2011
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2. Identification of reference genes for expression analysis by real-time quantitative PCR in drought-stressed soybean.
Abstract ? The objective of this work was to validate, by quantitative PCR in real time (RT-qPCR), genes to be used as reference in studies of gene expression in soybean in drought-stressed trials. Four genes commonly used in soybean were evaluated: GmB-actin, GmGAPDH, GmLectin and GmRNAr18S. Total RNA was extracted from six samples: three from roots in a hy
Pesquisa Agropecuária Brasileira. Publicado em: 2011
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3. PurificaÃÃo parcial de uma lectina da raiz de Guettarda platypoda
Lectins, proteins or glycoproteins that reversible bind carbohydrates with distinct degrees of selectivity, they are found in a variety of organisms being involved in numerous cellular processes. In this work evaluated the presence of lectin(s) from Guettarda platypoda D.C., plant popular know with âangelicaâ. Roots of this plant have been used in folk med
Publicado em: 2003
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4. Lectin Binding to the Root and Root Hair Tips of the Tropical Legume Macroptilium atropurpureum Urb
Ten fluorescein isothiocyanate-labeled lectins were tested on the roots of the tropical legume Macroptilium atropurpureum Urb. Four of these (concanavalin A, peanut agglutinin, Ricinis communis agglutinin I [RCA-I], wheat germ agglutinin) were found to bind to the exterior of root cap cells, the root cap slime, and the channels between epidermal cells in the
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5. Effect of lectin on nodulation by wild-type Bradyrhizobium japonicum and a nodulation-defective mutant.
The nodulation characteristics of wild-type Bradyrhizobium japonicum USDA 110 and mutant strain HS111 were examined. Mutant strain HS111 exhibits a delayed-nodulation phenotype, a result of its inability to initiate successful nodulation promptly following inoculation of the soybean root. Previously, we showed that the defect in initiation of infection leadi
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6. Host Recognition in the Rhizobium-Soybean Symbiosis 1
Polar binding of Rhizobium japonicum to roots and root hairs of Glycine soja (L.) Sieb. and Zucc. is specifically inhibited by d-galactose and N-acetyl-d-galactosamine, haptens of Glycine max seed lectin. A protein, immunologically cross-reactive with the G. max seed lectin, is present in G. soja seed extracts. Peptide mapping of the purified G. max and G. s
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7. Cross-reactive antigens and lectin as determinants of symbiotic specificity in the Rhizobium-clover association.
Cross-reactive antigens of clover roots and Rhizobium trifolii were detected on their cell surfaces by tube agglutination, immunofluorescent, and radioimmunoassay techniques. Anti-clover root antiserum had a higher agglutinating titer with infective strains of R. trifolii than with noninfective strains. The root antiserum previously adsorbed with noninfectiv
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8. A nod factor binding lectin with apyrase activity from legume roots
A lectin isolated from the roots of the legume, Dolichos biflorus, binds to Nod factors produced by rhizobial strains that nodulate this plant and has a deduced amino acid sequence with no significant homology to any lectin reported to date. This lectin also is an enzyme that catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside di- and triphospha
The National Academy of Sciences.
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9. Development and trifoliin A-binding ability of the capsule of Rhizobium trifolii.
The age-dependent lectin-binding ability of Rhizobium trifolii 0403 capsular polysaccharide (CPS) was examined by following the development of the capsule and its ability to interact with the white clover lectin trifoliin A. Bacteria grown on agar plates for 3, 5, 7, 14, and 21 days were examined by electron microscopy and immunofluorescence microscopy with
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10. Stimulation of clover root hair infection by lectin-binding oligosaccharides from the capsular and extracellular polysaccharides of Rhizobium trifolii.
A polysaccharide depolymerase isolated from the phage lysate of Rhizobium trifolii 4S was used to fragment capsular polysaccharides (CPS) and extracellular polysaccharides (EPS) of R. trifolii 0403 into oligosaccharides. These products were analyzed for clover lectin (trifoliin A)-binding ability, effect on infection of white clover root hairs, and changes i
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11. Identification of a new pea gene, PsNlec1, encoding a lectin-like glycoprotein isolated from the symbiosomes of root nodules.
A 27-kD glycoprotein antigen recognized by monoclonal antibody MAC266 was purified from isolated symbiosomes derived from pea (Pisum sativum) root nodules containing Rhizobium. The N-terminal amino acid sequence was obtained, and the corresponding cDNA clone was isolated by a polymerase chain reaction-based strategy. The clone contained a single open reading
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12. Adsorption of bacteria to roots as related to host specificity in the Rhizobium-clover symbiosis.
Quantitative microscope techniques were utilized to examine the adsorption of rhizobial cells to clover root hairs. Adsorption of cells of noninfective strains of Rhizobium trifolii or infective R. meliloti strains to clover root hairs was four to five times less than that of the infective R. trifolii strains. Attachment of the rod-shaped bacteria to clover