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Antibacterial activity of lactose-binding lectins from Bufo arenarum skin Biocell
Sánchez Riera,Alicia; Daud,Adriana; Gallo,Adriana; Genta,Susana; Aybar,Manuel; Sánchez,Sara.
Amphibians respond to microbial infection through cellular and humoral defense mechanisms such as antimicrobial protein secretion. Most humoral defense proteins are synthetized in the skin. In this study we isolated two b-galactoside-binding lectins with molecular weights of 50 and 56 KDa from the skin of Bufo arenarum. These lectins have significant hemagglutination activity against trypsinized rabbit erythrocytes, which was inhibited by galactose-containing saccharides. They are water-soluble and independent of the presence of calcium. The antimicrobial analysis for each lectin was performed. At mmolar concentration lectins show strong bacteriostatic activity against Gram negative bacteria (Escherichia coli K12 4100 and wild strains of Escherichia coli...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Skin; Lectin; Amphibian; Antibacterial activity.
Ano: 2003 URL: http://www.scielo.org.ar/scielo.php?script=sci_arttext&pid=S0327-95452003000100005
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Antinociceptive properties in mice of a lectin isolated from the marine alga Amansia multifida Lamouroux BJMBR
Neves,S.A.; Freitas,A.L.P.; Souza,B.W.S.; Rocha,M.L.A.; Correia,M.V.O.; Sampaio,D.A.; Viana,G.S.B..
The antinociceptive effects of a lectin (LEC) isolated from the marine alga Amansia multifida were determined in Swiss mice. The LEC (1, 5, and 10 mg/kg) inhibited acetic acid-induced abdominal writhings in a dose-dependent manner after intraperitoneal or oral administration. A partial but significant inhibition of writhings was observed after the combination of LEC (10 mg/kg) with avidin (1 mg/kg), a potent inhibitor of the hemmaglutinant activity of the lectin. However, total writhing inhibition was demonstrable in the group of mice treated with LEC plus mannose (1 mg/kg), as compared to LEC alone or to control groups. Furthermore, avidin and mainly mannose also play a role in antinociception, somehow facilitating the interaction of LEC with its active...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Red algae; Amansia multifida; Lectin; Antinociceptive effects; Mannose-specific lectin.
Ano: 2007 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2007000100016
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Chromatographic and Electrophorotic Separation of Lectin Preparation from Resistant and Susceptible Plants of Tomato to Pseudomonas solanacearum Taiwan Agricultural Research Institute
Chien-Yih Lin.
[[abstract]]Lectin preparations from wilt resistant and susceptible tomato plants to Pseudomonas solanacearum they have similar movement in Sephadex G-200 columns and SDS-polyacrylamide gels. Column fractions with highest protein content have the highest agglutination titers. Protein content, agglutination titers of column fractions, and the staining intensity of gels after electrophoresis are related to the susceptibility or resistance of the plants used for lectin extraction, inoculation of these plants, and the virulence of the Pseudomonas solanacearum isolate used for inoculation.
Palavras-chave: Pseudomonas solanacearum; Lectin; Chromatographic separation; Electrophoretic separation; [[classification]]10.
Ano: 1995
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Differential activity of a lectin from Solieria filiformis against human pathogenic bacteria BJMBR
Holanda,M.L.; Melo,V.M.M.; Silva,L.M.C.M.; Amorim,R.C.N.; Pereira,M.G.; Benevides,N.M.B..
A lectin isolated from the red alga Solieria filiformis was evaluated for its effect on the growth of 8 gram-negative and 3 gram-positive bacteria cultivated in liquid medium (three independent experiments/bacterium). The lectin (500 µg/mL) stimulated the growth of the gram-positive species Bacillus cereus and inhibited the growth of the gram-negative species Serratia marcescens, Salmonella typhi, Klebsiella pneumoniae, Enterobacter aerogenes, Proteus sp, and Pseudomonas aeruginosa at 1000 µg/mL but the lectin (10-1000 µg/mL) had no effect on the growth of the gram-positive bacteria Staphylococcus aureus and B. subtilis, or on the gram-negative bacteria Escherichia coli and Salmonella typhimurium. The purified lectin significantly reduced the cell density...
Tipo: Info:eu-repo/semantics/other Palavras-chave: Red alga; Solieria filiformis; Human pathogenic bacteria; Lectin; Antibacterial activity; Klebsiella pneumoniae.
Ano: 2005 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005001200005
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Effects of A Recombinant Sarcocystis muris Microneme Protein on Splenocytes of The Natural Intermediate Host OAK
Klein, Harald; Zyto, Nadja; Loeschner, Bettina; Bornhak, Monika; Montag, Thomas.
Palavras-chave: Sarcocystis muris; Micronemes; Recombinant protein; Lectin; Immunosuppression.
Ano: 1998 URL: http://ir.obihiro.ac.jp/dspace/handle/10322/279
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Effects of a Sarcocystis gigantea Extract (SGE) on the Replication of Human Immunodeficiency Virus (HIV) OAK
Drösigk, U.; Tietz, H. J.; Pözsch, F.; Scholz, D.; Hiepe, T. H..
Palavras-chave: Sarcocystis gigantea; Lectin; Immunomodulation; Human Immunodeficiency Virus; HIV.
Ano: 1995 URL: http://ir.obihiro.ac.jp/dspace/handle/10322/235
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Enzyme activity and biochemical changes during production of Lentinula edodes (Berk.) Pegler Ciênc. Tecnol. Aliment.
SOUSA,Maiara Andrade de Carvalho; COSTA,Lívia Martinez Abreu Soares; PEREIRA,Thiago Souza; ZIED,Diego Cunha; RINKER,Danny Lee; DIAS,Eustáquio Souza.
Abstract Shiitake is an important edible and medicinal mushroom cultivated worldwide. Its cultivation involves a complex process of browning that precedes the primordia initiation. The present work through the evaluation of enzymes, lectin and β-glucan during the cultivation cycle of Lentinula edodes, the degradation of cellulose, hemicellulose and lignin, attempted to correlate these with mushroom yield. Strains UFLA-LE1, UFLA-LE2 and UFLA-LE6 consumed significantly more hemicelluloses than the other three strains with strain LE5 consuming significantly the most lignin of all six strains. Strains UFLA-LE4 and UFLA-LE6 were significantly the most productive. The laccase activity increased continuously until the end of the cultivation for all strains....
Tipo: Info:eu-repo/semantics/article Palavras-chave: Shiitake; Lectin; Enzymes; Β-glucan.
Ano: 2019 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612019000300774
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Expressed sequence tags in venomous tissue of Scorpaena plumieri (Scorpaeniformes: Scorpaenidae) Neotropical Ichthyology
Costa,Fábio L. S.; Lima,Maria E. De; Pimenta,Adriano C.; Figueiredo,Suely G.; Kalapothakis,Evanguedes; Salas,Carlos E..
Species of the family Scorpaenidae are responsible for accidents and sporadic casualties by the shore they inhabit. The species Scorpaena plumierifrom this family populate the Northeastern and Eastern coast of Brazil causing human envenomation characterized by local and systemic symptoms. In experimental animals the venom induces cardiotoxic, hypotensive, and airway respiratory effects. As first step to identify the venom components we isolated gland mRNA to produce a cDNA library from the fish gland. This report describes the partial sequencing of 356 gland transcripts from S. plumieri. BLAST analysis of transcripts showed that 30% were unknown sequences, 17% hypothetical proteins, 17% related to metabolic enzymes, 14% belonged to signal transducing...
Tipo: Info:eu-repo/semantics/article Palavras-chave: CDNAs; EST; Glands; Lectin; Scorpionfish; Toxins.
Ano: 2014 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1679-62252014000400871
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Inflammatory and anti-inflammatory effects of soybean agglutinin BJMBR
Soybean agglutinin (SBA) lectin, a protein present in raw soybean meals, can bind to and be extensively endocytosed by intestinal epithelial cells, being nutritionally toxic for most animals. In the present study we show that SBA (5-200 µg/cavity) injected into different cavities of rats induced a typical inflammatory response characterized by dose-dependent exudation and neutrophil migration 4 h after injection. This effect was blocked by pretreatment with glucocorticoid (0.5 mg/kg) or by co-injection of N-acetyl-galactosamine (100 x [M] lectin), but not of other sugars (100 x [M] lectin), suggesting an inflammatory response related to the lectin activity. Neutrophil accumulation was not dependent on a direct effect of SBA on the macrophage population...
Tipo: Info:eu-repo/semantics/other Palavras-chave: Lectin; Soybean agglutinin (SBA); Neutrophil migration; Inflammation.
Ano: 1997 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1997000700009
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Isolation and Characterization of Midgut Lectin From Aedes aegypti (L.) (Diptera: Culicidae) BABT
Ayaad,Tahany Hassan; Al-Akeel,Rasha Khalifah; Olayan,Ebtisam.
ABSTRACT The present investigation deals with the isolation and characterization of a lectin from Aedes aegypti (Ae aegypti) female mid gut extract that agglutinates various mammalian red blood cells (RBCs) such as human three groups A, B, and O (RH+), mouse, rat, guinea-pig, sheep and goat erythrocytes. The highest activity of both crude and isolated mid gut lectins were detected against sheep RBCs. Using (NH4)2 SO4 fractionation, ion-exchange and mannose-CNBr-Sepharose 6B affinity chromatography techniques, Ae. aegypti midgut lectin (Aelec) was purified to homogeneity.Isoelectric focusing (IEF) and reducing SDS/PAGE revealed that the isolated mid gut lectin had isoelectric point (PI) of 5.90, and subunits approximate molecular weights of 35.50 and 27.35...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Lectin; Purification; Characterization; Hemagglutination; Aedes aegypti; Mosquitoes.
Ano: 2015 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132015000600905
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Isolation and partial characterization of a D-galactose-binding lectin from the latex of Synadenium carinatum BABT
Souza,Maria Aparecida; Amâncio-Pereira,Francielle; Cardoso,Cristina Ribeiro Barros; Silva,Adriano Gomes da; Silva,Edmar Gomes; Andrade,Lívia Resende; Pena,Janethe Deolina Oliveira; Lanza,Henrique; Afonso-Cardoso,Sandra Regina.
A lectin from the latex of Synadenium carinatum was purified by affinity chromatography on immobilized-D-galactose-agarose and shown to be a potent agglutinin of human erythrocytes. The haemagglutination of human red cells was inhibited by 3.0 mM N-acetyl-D-galactopyranoside, 6.3 mM methyl-beta-D-galactopyranoside, 50 mM methyl-alpha-D-galactopyranoside and 50 mM D-fucose but not by L-fucose, demonstrating an anomeric and a conformational specificity. According to SDS-PAGE analysis, the lectin appeared to be a glycoprotein composed of two polypeptide chains of ca. 28 and 30 kDa, but size exclusion chromatography (Sephadex G-100) and native PAGE revealed a protein of apparent molecular weight 120 - 130 kDa made up of 28 and 30 kDa subunits. The lectin was...
Tipo: Info:eu-repo/semantics/article Palavras-chave: D-Galactose-binding; Lectin; Latex; Synadenium carinatum.
Ano: 2005 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132005000600005
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Isolation of a ß-galactoside-binding lectin from cat liver BJMBR
Franco-Fraguas,L.; Batista-Viera,F.; Carlsson,J..
A lectin from cat liver has been identified and purified by affinity chromatography on asialofetuin-Sepharose. One hundred micrograms of lectin was obtained from one cat liver with a purification factor of 1561. The lectin agglutinates trypsin-treated rabbit and cow erythrocytes. Hemagglutination was inhibited only by saccharides containing ß-galactosyl residues, of which the 1-amine-1-deoxy-ß-D-galactose was the most potent one by inhibiting hemagglutination at a concentration of 12.5 mM, followed by melibiose, trehalose and galactose. The lectin has a subunit molecular mass of 14.4 kDa determined by SDS-PAGE under reducing conditions and a pI of 4.85. Compared with the composition of lectins from calf heart and porcine heart, cat liver lectin contains...
Tipo: Info:eu-repo/semantics/article Palavras-chave: SS-Galactoside-binding lectin; Galectins; Lectin; Cat liver lectin; Affinity chromatography.
Ano: 2003 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2003000400005
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Lectin activity in mycelial extracts of Fusarium species BJM
Bhari,Ranjeeta; Kaur,Bhawanpreet; Singh,Ram S..
ABSTRACT Lectins are non-immunogenic carbohydrate-recognizing proteins that bind to glycoproteins, glycolipids, or polysaccharides with high affinity and exhibit remarkable ability to agglutinate erythrocytes and other cells. In the present study, ten Fusarium species previously not explored for lectins were screened for the presence of lectin activity. Mycelial extracts of F. fujikuroi, F. beomiformii, F. begoniae, F. nisikadoi, F. anthophilum, F. incarnatum, and F. tabacinum manifested agglutination of rabbit erythrocytes. Neuraminidase treatment of rabbit erythrocytes increased lectin titers of F. nisikadoi and F. tabacinum extracts, whereas the protease treatment resulted in a significant decline in agglutination by most of the lectins. Results of...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Fusarium; Lectin; Hemagglutination; Carbohydrate specificity; Culture age.
Ano: 2016 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822016000300775
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Lectin staining patterns in human gastric mucosae with and without exposure to Helicobacter pylori BJM
Melo-Junior,Mario R.; Cavalcanti,Carmelita L.B.; Pontes-Filho,Nicodemos T.; Carvalho Jr.,Luiz B.; Beltrão,Eduardo I. C..
The aim of the present study was to evaluate qualitative changes in the glycoconjugate expression in human gastric tissue of positive and negative patients for Helicobacter pylori, through lectins: Wheat Germ Agglutinin (WGA) and Concanavalin A (Con A). The lectins recognized differently the glycoconjugates in the superficial mucous layer at the gastric tissues. The results suggest a significant change in the carbohydrate moieties present on the surface of the gastric cells during infection.
Tipo: Info:eu-repo/semantics/article Palavras-chave: Lectin; Gastric mucosae; Helicobacter pylori.
Ano: 2008 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822008000200007
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Lectin-binding properties of Aeromonas caviae strains BJM
Rocha-de-Souza,Cláudio M.; Hirata-Jr,Raphael; Mattos-Guaraldi,Ana L.; Freitas-Almeida,Angela C.; Andrade,Arnaldo F. B..
The cell surface carbohydrates of four strains of Aeromonas caviae were analyzed by agglutination and lectin-binding assays employing twenty highly purified lectins encompassing all sugar specificities. With the exception of L-fucose and sialic acid, the sugar residues were detected in A. caviae strains. A marked difference, however, in the pattern of cell surface carbohydrates in different A. caviae isolates was observed. Specific receptors for Tritricum vulgaris (WGA), Lycopersicon esculentum (LEL) and Solanum tuberosum (STA) (D-GlcNAc-binding lectins) were found only in ATCC 15468 strain, whereas Euonymus europaeus (EEL, D-Gal-binding lectin) sites were present exclusively in AeQ32 strain, those for Helix pomatia (HPA, D-GalNAc-binding lectin) in AeC398...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Aeromonas caviae; Lectin; Carbohydrate; Cell surface.
Ano: 2008 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822008000200003
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Lectins from Pisum arvense seeds behave differently from storage proteins during germination in the darkness Rev. Bras. Fisiol. Veg.
SILVA,LUIZA IZABEL M. MOREIRA DA; RAMOS,MÁRCIO VIANA; CAJAZEIRAS,JOÃO BATISTA; FERREIRA,PATRÍCIA RODRIGUES; CARVALHO,CARLOS ALBERTO V.; GRANGEIRO,THALLES BARBOSA; NUNES,EDSON PAULA; SAMPAIO,ALEXANDRE HOLANDA; FREITAS,BEATRIZ TUPINAMBÁ; SILVEIRA,JOAQUIM ALBENÍSIO G. DA; CAVADA,BENILDO SOUSA.
ABSTRACT - The mobilization of seed proteins from Pisum arvense L. during germination in the absence of light was studied. The seeds were found to be completely consumed 22 days after germination and seedlings ceased growth after the 18th day. SDS-PAGE indicated that the main protein bands correspond to high molecular mass storage proteins which undergo proteolysis in the initial stages of germination and are not detected after the 7th day of germination. However, the corresponding lectin profiles were detected during the entire germination process, suggesting that these proteins are strongly resistant to seed proteolytic enzymes and should be important for seedling establishment. Furthermore, haemagglutinating activity in cotyledons was detected until 22...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Lectin; Protein mobilization; Seed germination.
Ano: 2000 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0103-31312000000300008
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Purification and characterisation of a lectin from the red marine alga Pterocladiella capillacea (S.G. Gmel.) Santel. & Hommers. Rev. Bras. Bot.
OLIVEIRA,STÉLIO R.M.; NASCIMENTO,ANTONIA E.; LIMA,MARIA E.P.; LEITE,YÁSKARA F.M.M.; BENEVIDES,NORMA M.B..
A lectin present in the marine red alga Pterocladiella capillacea was purified and characterised by extraction of soluble proteins (crude extract) in 20 mM Tris-HCl buffer, pH 7.5. Among the analysed erythrocytes (human blood group A, B and O and the animals ox, goat, chicken and rabbit) the lectin agglutinated specifically rabbit erythrocytes. The hemagglutinating activity assay showed that the lectin was not dependent on divalent cations and was shown to be inhibited by the glycoproteins avidin and mucin. The purification procedure was conduced by precipitation of the crude extract with 80% saturation ammonium sulfate (F0/80) followed by affinity chromatography on guar-gum column. The lectin of P. capillacea was purified 14.5 fold and had a recovery of...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Agglutinin; Algae; Lectin; Pterocladiella capillacea; Purification.
Ano: 2002 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-84042002012000003
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Purification, partial characterization and antimicrobial activity of Lectin from Chenopodium Quinoa seeds Ciênc. Tecnol. Aliment.
POMPEU,Dávia Guimarães; MATTIOLI,Marcelo Augusto; RIBEIRO,Rosy Iara Maciel de Azambuja; GONÇALVES,Daniel Bonoto; MAGALHÃES,Juliana Teixeira de; MARANGONI,Sérgio; SILVA,José Antônio da; GRANJEIRO,Paulo Afonso.
Abstract A novel lectin was isolated from the seeds of Chenopodium quinoa. To achieve this end, the crude extract from the quinoa was submitted to two purification steps, Sephadex G50 and Mono Q. The hemagglutinating activity showed that this lectin agglutinates human erythrocytes. Its activity is inhibited by glucose and mannose, and remained stable under a wide range of pH levels and temperatures. The quinoa lectin was found to be a heterodimeric lectin of approximately 60 kDa, consisting of two subunits of approximately 25 kDa and 35 kDa. This lectin had its antimicrobial activity tested against several bacteria strains and effectively inhibited three strains. These strains were all Gram-negative, making this lectin a promising antimicrobial tool.
Tipo: Info:eu-repo/semantics/article Palavras-chave: Antimicrobial; Chenopodium quinoa; Glucose/mannose-specific; Lectin; Seeds.
Ano: 2015 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612015000400696
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Subproteome of Lachesis muta rhombeata venom and preliminary studies on LmrSP-4, a novel snake venom serine proteinase J. Venom. Anim. Toxins incl. Trop. Dis.
Wiezel,Gisele A; Bordon,Karla CF; Silva,Ronivaldo R; Gomes,Mário SR; Cabral,Hamilton; Rodrigues,Veridiana M; Ueberheide,Beatrix; Arantes,Eliane C.
Abstract Background: Lachesis muta rhombeata is one of the venomous snakes of medical importance in Brazil whose envenoming is characterized by local and systemic effects which may produce even shock and death. Its venom is mainly comprised of serine and metalloproteinases, phospholipases A2 and bradykinin-potentiating peptides. Based on a previously reported fractionation of L. m. rhombeata venom (LmrV), we decided to perform a subproteome analysis of its major fraction and investigated a novel component present in this venom. Methods: LmrV was fractionated through molecular exclusion chromatography and the main fraction (S5) was submitted to fibrinogenolytic activity assay and fractionated by reversed-phase chromatography. The N-terminal sequences of...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Bushmaster; Snake venom; SVSP; Kallikrein-like; Plasminogen activator; Kininogenase; Lectin; Protease; Envenomation.
Ano: 2019 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992019000100307
Registros recuperados: 19
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