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| Registros recuperados: 17 | |
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| 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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| OLIVEIRA,ANTÔNIA S. DE; LÓSSIO,CLÁUDIA F.; RANGEL,ANNE J.; MARTINS,MARIA G.Q.; NASCIMENTO,FERNANDO E.P. DO; ANDRADE,MARIA L.L. DE; CAVADA,BENILDO S.; LACERDA,SÍRLEIS R.; NASCIMENTO,KYRIA S. DO. |
| ABSTRACT Freshwater algae are rich sources of structurally biologically active metabolites, such as fatty acids, steroids, carotenoids and polysaccharides. Among these metabolites, lectins stand out. Lectins are proteins or glycoproteins of non-immune origin which bind to carbohydrates or glycoconjugates, without changing ligand structure. Many studies have reported on the use of Spirogyra spp. as effective bioindicators of heavy metals; however, reports on Spirogyra molecular bioprospecting are quite limited. Therefore, this study aimed to detect, isolate, purify and characterize a lectin present in the freshwater green algae Spirogyra. Presence of the lectin protein in the extract was detected by hemagglutination assays. Subsequently, the protein extract... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Algae; Characterization; Lectin; Purification. |
| Ano: 2017 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652017000502113 |
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| 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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| 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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| 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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| 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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| 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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| 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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| 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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| 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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| 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 |
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| Registros recuperados: 17 | |
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