Results 121 to 130 of about 1,391 (163)
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Separation of the coagulant components of Bothrops jararaca venom
Toxicon, 1970The venom of Bothrops jararaca has been separated into two distinct coagulant components by chromatography on DEAE cellulose, and the presence of an inhibitor in the crude venom detected.
K W, Denson, W E, Rousseau
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Toxicon, 2004
Whereas the presynaptic action of Crotalus durissus terrificus venom is well-established, Bothrops venoms have historically been considered to have only postsynaptic and muscular effects. However, some studies have also suggested a presynaptic action for these venoms. In this work, we used chick biventer cervicis preparations to compare the presynaptic
Léa, Rodrigues-Simioni +6 more
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Whereas the presynaptic action of Crotalus durissus terrificus venom is well-established, Bothrops venoms have historically been considered to have only postsynaptic and muscular effects. However, some studies have also suggested a presynaptic action for these venoms. In this work, we used chick biventer cervicis preparations to compare the presynaptic
Léa, Rodrigues-Simioni +6 more
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Toxicon, 1992
Two fibrinolytic enzymes, jararafibrase I and jararafibrase II, were purified from Bothrops jararaca venom. The purified jararafibrase I and jararafibrase II ran as single protein bands on analytical polyacrylamide gel electrophoresis and had mol. wts of 47,000 +/- 2000 and 21,400 +/- 500, respectively, by SDS-polyacrylamide gel electrophoresis.
M, Maruyama +4 more
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Two fibrinolytic enzymes, jararafibrase I and jararafibrase II, were purified from Bothrops jararaca venom. The purified jararafibrase I and jararafibrase II ran as single protein bands on analytical polyacrylamide gel electrophoresis and had mol. wts of 47,000 +/- 2000 and 21,400 +/- 500, respectively, by SDS-polyacrylamide gel electrophoresis.
M, Maruyama +4 more
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Toxicon, 1989
A metalloprotease from Bothrops jararaca venom (J protease) was purified by DEAE-Sephacel, CM-cellulose, Sephacryl S-200 and Sephadex G-75 chromatograph. The proteolytic activity was inactivated by EDTA, o-phenanthroline and DTNB. Phosphoramidon and cysteine protease inhibitors (leupeptin, E64 and its derivatives) were inactive on this enzyme.
M M, Tanizaki +5 more
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A metalloprotease from Bothrops jararaca venom (J protease) was purified by DEAE-Sephacel, CM-cellulose, Sephacryl S-200 and Sephadex G-75 chromatograph. The proteolytic activity was inactivated by EDTA, o-phenanthroline and DTNB. Phosphoramidon and cysteine protease inhibitors (leupeptin, E64 and its derivatives) were inactive on this enzyme.
M M, Tanizaki +5 more
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Toxicon, 1982
Bothropasin, one of the proteases from the venom of Bothrops jararaca active on casein, was isolated by ammonium sulfate precipitation, DEAE-cellulose and DEAE-Sephadex A-50 chromatographies and Sephadex G-100 column filtration. The preparation possessed no other detectable activities which are present in the crude venom.
F R, Mandelbaum +2 more
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Bothropasin, one of the proteases from the venom of Bothrops jararaca active on casein, was isolated by ammonium sulfate precipitation, DEAE-cellulose and DEAE-Sephadex A-50 chromatographies and Sephadex G-100 column filtration. The preparation possessed no other detectable activities which are present in the crude venom.
F R, Mandelbaum +2 more
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Studies on blood coagulation and fibrinolysis in patients bitten by Bothrops jararaca (jararaca).
Thrombosis and haemostasis, 1990The blood coagulation and the fibrinolytic systems of nine patients envenomed by Bothrops jararaca in São Paulo (Brazil) were studied. Five of the accidents were caused by young snakes (less than 50 cm). On admission, four patients had non-clotting and three partially-clotting blood. Fibrinogen levels were decreased due to the thrombin-like activity of
M, Maruyama +9 more
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Concentrating ability of the Bothrops jararaca gallbladder
Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology, 1999Abstract Total sodium, potassium, magnesium, calcium, chloride and osmolality were measured in plasma and gallbladder bile of the snake Bothrops jararaca under normal hydration conditions or in the presence of chronic challenges of hydromineral balance.
Paulo F. Silveira, Olga M. Mimura
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Sexual dimorphism in venom of Bothrops jararaca(Serpentes: Viperidae)
Toxicon, 2006Bothrops jararaca is an abundant snake in Brazil, and its venom has been studied exhaustively. The species exhibits adult size dimorphism in which female are larger. We registered the growth in Snout-Vent Length and weight of one litter (with 11 females and 12 males). We compared growth curves and venom profile between male and female of B. jararaca in
M F D, Furtado +2 more
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The kininases of Bothrops jararaca plasma.
Acta physiologica latino americana, 1987Evidence is presented to suggest that kininase activity of Bothrops jararaca plasma is due to the presence of at least three distinct enzymes: a carboxypeptidase B type enzyme, similar to that found in human plasma in that its activity is enhanced by Co2+ (1 X 10(-4) M); a carboxypeptidase B type enzyme whose activity is unaffected by Co2+, and an ...
A A, Lavras +4 more
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Effects of catecholamines on the isolated aorta of the snake Bothrops jararaca
Comparative Biochemistry and Physiology Part C: Comparative Pharmacology, 19921. Effects of catecholamines in snakes have been examined using an aorta preparation isolated from Bothrops jararaca. Adrenaline, noradrenaline and isoprenaline produced dose-dependent contractions on this preparation. The relative potency was adrenaline greater than noradrenaline greater than isoprenaline. 2.
N, Yamanouye +2 more
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