Results 151 to 160 of about 7,760 (198)
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Immunization with liposome-encapsulated Bothrops jararaca venom
Toxicon, 2000The venom of Bothrops jararaca (BjV) snake was encapsulated into liposomes. The toxicity and ability of the resultant liposomes to protect mice were evaluated. No acute toxicity was found in mice, when liposomes were subcutaneously injected whereas the same dose of venom emulsified in Freund's adjuvant caused the mice to die.
V T, Carvalho +3 more
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Blood-clotting Activity of the Venom of Bothrops jararaca
Nature, 1959THE well-known blood-clotting activity of the venom from snakes of various species of the genus Bothrops has been attributed to its proteolytic activity1, although Michl2 (using paper electrophoresis) and Holz and Raudonat3 (using fractional precipitation with ammonium sulphate) have presented evidence against this point of view.
O B, HENRIQUES +2 more
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The humoral immune responses of patients bitten by the snake Bothrops jararaca (jararaca)
Toxicon, 1990The isotype and specificity of antibodies produced by patients bitten by B. jararaca and submitted to serum therapy were studied. The IgG anti-B. jararaca antibodies have large individual dispersion, starting to appear 10 days after the first bite and increasing to at least 80 days after the bite.
M O, Domingos +3 more
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Angiotensin receptor in the heart of Bothrops jararaca snake
European Journal of Pharmacology, 2001Angiotensin II interacts with specific cell surface angiotensin AT1 and AT2 receptors and, in some vertebrates, with an atypical angiotensin AT receptor. This study was designed to characterize the angiotensin receptor in the heart of Bothrops jararaca snake.
M C, Breno, C S, Porto, Z P, Picarelli
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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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