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	Provedor de dados J. Venom. Anim. Toxins incl. Trop. Dis. (2) Autor Sampaio,Suely V. (2) Sartim,Marco A. (2) Cedro,Rafhaella C. A. (1) Costa,Tássia R. (1) Faccioli,Lúcia H. (1) Menaldo,Danilo L. (1) Santos-Filho,Norival A. (1) Zoccal,Karina F. (1) Mais... Palavra-chave Snake venom (2) Antitumor activity (1) Bactericidal activity (1) Bothrops jararaca (1) C-type lectin (1) Carbohydrate recognition domain (1) Cytotoxicity (1) Galactoside-binding protein (1) Glycoconjugates (1) Inflammation (1) Inflammatory response (1) Mitogenic activity (1) Phospholipase A2 (1) Platelet aggregation (1) Mais... Tipo do documento Info:eu-repo/semantics/article (2) Ano 2018 (1) 2015 (1) País Brazil (2) Idioma Inglês (2)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 2 Primeira ... 1 ... Última Cytotoxic and inflammatory potential of a phospholipase A2 from Bothrops jararaca snake venom J. Venom. Anim. Toxins incl. Trop. Dis. Cedro,Rafhaella C. A.; Menaldo,Danilo L.; Costa,Tássia R.; Zoccal,Karina F.; Sartim,Marco A.; Santos-Filho,Norival A.; Faccioli,Lúcia H.; Sampaio,Suely V.. Abstract Background: Snake venom phospholipases A2 (PLA2s) have been reported to induce myotoxic, neurotoxic, hemolytic, edematogenic, cytotoxic and proinflammatory effects. This work aimed at the isolation and functional characterization of a PLA2 isolated from Bothrops jararaca venom, named BJ-PLA2-I. Methods and Results: For its purification, three consecutive chromatographic steps were used (Sephacryl S-200, Source 15Q and Mono Q 5/50 GL). BJ-PLA2-I showed acidic characteristics, with pI~4.4 and molecular mass of 14. 2 kDa. Sequencing resulted in 60 amino acid residues that showed high similarity to other Bothrops PLA2s, including 100% identity with BJ-PLA2, an Asp49 PLA2 previously isolated from B. jararaca venom. Being an Asp49 PLA2, BJ-PLA2-I... Tipo: Info:eu-repo/semantics/article Palavras-chave: Snake venom; Bothrops jararaca; Phospholipase A2; Inflammation; Cytotoxicity. Ano: 2018 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992018000100324 Snake venom galactoside-binding lectins: a structural and functional overview J. Venom. Anim. Toxins incl. Trop. Dis. Sartim,Marco A.; Sampaio,Suely V.. AbstractSnake venom galactoside-binding lectins (SVgalLs) comprise a class of toxins capable of recognizing and interacting with terminal galactoside residues of glycans. In the past 35 years, since the first report on the purification of thrombolectin from Bothrops atrox snake venom, several SVgalLs from Viperidae and Elapidae snake families have been described, as has progressive improvement in the investigation of structural/functional aspects of these lectins. Moreover, the advances of techniques applied in protein-carbohydrate recognition have provided important approaches in order to screen for possible biological targets. The present review describes the efforts over the past 35 years to elucidate SVgalLs, highlighting their structure and... Tipo: Info:eu-repo/semantics/article Palavras-chave: Snake venom; C-type lectin; Galactoside-binding protein; Carbohydrate recognition domain; Glycoconjugates; Inflammatory response; Antitumor activity; Bactericidal activity; Mitogenic activity; Platelet aggregation. Ano: 2015 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992015000100213 Registros recuperados: 2 Primeira ... 1 ... Última

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