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Registros recuperados: 64
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Neutralizing capacity of a new monovalent anti-Bothrops atrox antivenom: comparison with two commercial antivenoms BJMBR
Three horse-derived antivenoms were tested for their ability to neutralize lethal, hemorrhagic, edema-forming, defibrinating and myotoxic activities induced by the venom of Bothrops atrox from Antioquia and Chocó (Colombia). The following antivenoms were used: a) polyvalent (crotaline) antivenom produced by Instituto Clodomiro Picado (Costa Rica), b) monovalent antibothropic antivenom produced by Instituto Nacional de Salud-INS (Bogotá), and c) a new monovalent anti-B. atrox antivenom produced with the venom of B. atrox from Antioquia and Chocó. The three antivenoms neutralized all toxic activities tested albeit with different potencies. The new monovalent anti-B. atrox antivenom showed the highest neutralizing ability against edema-forming and...
Tipo: Info:eu-repo/semantics/other Palavras-chave: Bothrops atrox; Snake venom; Antivenom; Neutralization; Antioquia; Chocó.
Ano: 1997 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1997000300011
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Behavioral effects of Bj-PRO-7a, a proline-rich oligopeptide from Bothrops jararaca venom BJMBR
Turones,L.C.; Cruz,K.R. da; Camargo-Silva,G.; Reis-Silva,L.L.; Graziani,D.; Ferreira,P.M.; Galdino,P.M.; Pedrino,G.R.; Santos,R.; Costa,E.A.; Ianzer,D.; Xavier,C.H..
The heptapeptide Bj-PRO-7a, isolated and identified from Bothrops jararaca (Bj) venom, produces antihypertensive and other cardiovascular effects that are independent on angiotensin converting enzyme inhibition, possibly relying on cholinergic muscarinic receptors subtype 1 (M1R). However, whether Bj-PRO-7a acts upon the central nervous system and modifies behavior is yet to be determined. Therefore, the aims of this study were: i) to assess the effects of acute administration of Bj-PRO-7a upon behavior; ii) to reveal mechanisms involved in the effects of Bj-PRO-7a upon locomotion/exploration, anxiety, and depression-like behaviors. For this purpose, adult male Wistar (WT, wild type) and spontaneous hypertensive rats (SHR) received intraperitoneal...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Bj-PRO-7a; Snake venom; Neuroactive compounds; Anxiety; Depression; Behavior.
Ano: 2019 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2019001100606
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Isolation and characterization of a serine proteinase with thrombin-like activity from the venom of the snake Bothrops asper BJMBR
Pérez,A.V; Rucavado,A; Sanz,L; Calvete,J.J; Gutiérrez,J.M.
A serine proteinase with thrombin-like activity was isolated from the venom of the Central American pit viper Bothrops asper. Isolation was performed by a combination of affinity chromatography on aminobenzamidine-Sepharose and ion-exchange chromatography on DEAE-Sepharose. The enzyme accounts for approximately 0.13% of the venom dry weight and has a molecular mass of 32 kDa as determined by SDS-PAGE, and of 27 kDa as determined by MALDI-TOF mass spectrometry. Its partial amino acid sequence shows high identity with snake venom serine proteinases and a complete identity with a cDNA clone previously sequenced from this species. The N-terminal sequence of the enzyme is VIGGDECNINEHRSLVVLFXSSGFL CAGTLVQDEWVLTAANCDSKNFQ. The enzyme induces clotting of plasma...
Tipo: Info:eu-repo/semantics/other Palavras-chave: Snake venom; Bothrops asper; Serine proteinase; Thrombin-like serine proteinase; Defibrin(ogen)ation.
Ano: 2008 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2008000100003
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Alternagin-C, a disintegrin-like protein from the venom of Bothrops alternatus, modulates alpha2ß1 integrin-mediated cell adhesion, migration and proliferation BJMBR
Selistre-de-Araujo,H.S.; Cominetti,M.R.; Terruggi,C.H.B.; Mariano-Oliveira,A.; De Freitas,M.S.; Crepin,M.; Figueiredo,C.C.; Morandi,V..
The alpha2ß1 integrin is a major collagen receptor that plays an essential role in the adhesion of normal and tumor cells to the extracellular matrix. Alternagin-C (ALT-C), a disintegrin-like protein purified from the venom of the Brazilian snake Bothrops alternatus, competitively interacts with the alpha2ß1 integrin, thereby inhibiting collagen binding. When immobilized in plate wells, ALT-C supports the adhesion of fibroblasts as well as of human vein endothelial cells (HUVEC) and does not detach cells previously bound to collagen I. ALT-C is a strong inducer of HUVEC proliferation in vitro. Gene expression analysis was done using an Affimetrix HU-95A probe array with probe sets of ~10,000 human genes. In human fibroblasts growing on collagen-coated...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Alpha2ß1 integrin; Disintegrin; Snake venom; Adhesion; Gene expression; Extracellular matrix.
Ano: 2005 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005001000007
Registros recuperados: 64
Primeira ... 1234 ... Última
 

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