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	Provedor de dados J. Venom. Anim. Toxins incl. Trop. Dis. (2) J. Venom. Anim. Toxins (1) Autor Andriao-Escarso,S. (1) Beletti,ME (1) Canabrava,HAN (1) Canabrava,LCMN (1) Cruz-Höfling,M. A. (1) Fonseca,KC (1) França,LV (1) Giglio,J. R. (1) Hyslop,S. (1) Leite,G. B. (1) Mamede,CC (1) Oliveira,F (1) Oshima-Franco,Y. (1) Prado-Franceschi,J. (1) Queiroz,MR (1) Rodrigues-Simioni,L. (1) Santos,Claudia T. (1) Santos-Filho,Norival A. (1) Silva,MC (1) Stanziola,L (1) Mais... Palavra-chave Myotoxin (3) Bothrops jararacussu (1) Bothrops moojeni (1) Bothrops venom (1) Edema (1) Histological analysis (1) Hyperalgesia (1) Myotoxin inhibitor (1) Neuromuscular junction (1) Neutralization (1) Phospholipases A2 (1) Snake blood (1) ΑPLI (1) Mais... Tipo do documento Info:eu-repo/semantics/article (3) Ano 2017 (1) 2011 (1) 2002 (1) País Brazil (3) Idioma Inglês (3)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 3 Primeira ... 1 ... Última Alpha-type phospholipase A2 inhibitors from snake blood J. Venom. Anim. Toxins incl. Trop. Dis. Santos-Filho,Norival A.; Santos,Claudia T.. Abstract It is of popular and scientific knowledge that toxins from snake venom (among them the PLA2 and myotoxins) are neutralized by various compounds, such as antibodies and proteins purified from animal blood. Venomous and nonvenomous snakes have PLA2 inhibitory proteins, called PLIs, in their blood serum. One hypothesis that could explain the presence of these PLIs in the serum of venomous snakes would be self-protection against the enzymes of their own venom, which eventually could reach the circulatory system. However, the presence of PLIs in non-venomous snakes suggests that their physiological role might not be restricted to protection against PLA2 toxins, but could be extended to other functions, as in the innate immune system and local... Tipo: Info:eu-repo/semantics/article Palavras-chave: Phospholipases A2; Myotoxin; Myotoxin inhibitor; ΑPLI; Snake blood. Ano: 2017 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992017000100203 Biological characterization of a myotoxin phosphoplipase A2 homologue purified from the venom of the snake Bothrops moojeni J. Venom. Anim. Toxins incl. Trop. Dis. Queiroz,MR; Mamede,CC; Fonseca,KC; Canabrava,LCMN; França,LV; Silva,MC; Stanziola,L; Beletti,ME; Canabrava,HAN; Oliveira,F. A myotoxin phospholipase A2 homologue, BmooMtx, was isolated from the venom of Bothrops moojeni by a combination of ion-exchange chromatography on DEAE-Sephacel column and gel filtration on Sephadex G-75. SDS-PAGE showed the enzyme to be a monomer with a molecular weight of 16,500. BmooMtx induced release of creatine kinase and morphological analyses indicated that it provoked an intense myonecrosis, with visible leukocyte infiltrate and damaged muscle cells 24 hours after injection. Anti-BmooMTx antibodies partially neutralized the myotoxic activity of BmooMtx and crude B. moojeni venom, as judged by determination of plasma creatine kinase levels and histological evaluation of skeletal muscle in mice. Anti-BmooMTx antibodies were effective in reducing the... Tipo: Info:eu-repo/semantics/article Palavras-chave: Bothrops moojeni; Hyperalgesia; Myotoxin; Edema. Ano: 2011 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992011000100007 Rabbit antivenom efficacy against myotoxic and neurotoxic activities of Bothrops jararacussu venom and bothropstoxin-I J. Venom. Anim. Toxins Oshima-Franco,Y.; Leite,G. B.; Valério,A. A.; Hyslop,S.; Andriao-Escarso,S.; Giglio,J. R.; Prado-Franceschi,J.; Cruz-Höfling,M. A.; Rodrigues-Simioni,L.. Bothrops jararacussu venom and its major toxin bothropstoxin-I (BthTX-I) possess myotoxic and neurotoxic properties. The efficacy of a rabbit antivenom raised against B. jararacussu venom in the neutralization of physiological, biochemical, and morphological changes induced by the venom and its major toxin BthTX-I was studied in mouse isolated phrenic nerve-diaphragm (PND) and extensor digitorum longus (EDL) preparations. The times required for 50% neuromuscular blockade in PND and EDL preparations for venom were 70+11.5 (S.E.M., n=5) min and 58+8 (n=16) (50 mu g/mL), and for BthTX-I 31+6 (n=3) min and 30+3 (n=5) min (20 mu g/mL), respectively. After 120 min incubation, creatine kinase (CK) concentrations in solution containing the EDL preparations were... Tipo: Info:eu-repo/semantics/article Palavras-chave: Bothrops venom; Myotoxin; Neutralization; Neuromuscular junction; Histological analysis; Bothrops jararacussu. Ano: 2002 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0104-79302002000200004 Registros recuperados: 3 Primeira ... 1 ... Última

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