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A new muscle damaging toxin, myotoxin II, from the venom of the snake Bothrops asper (terciopelo)
(1989)
A new muscle damaging toxin, myotoxin II, was purified from the venom of Bothrops asper by ion-exchange chromatography on CMSephadex C-25. The toxin is a dimeric, basic protein with a monomer mol.wt of 13,341, according ...
Synergism between basic Asp49 and Lys49 phospholipase A2 myotoxins of viperid snake venom in vitro and in vivo
(PLoS One 9(10):e109846, 2014-10-07)
Two subtypes of phospholipases A2 (PLA2s) with the ability to induce myonecrosis, ‘Asp49’ and ‘Lys49’ myotoxins, often coexist in viperid snake venoms. Since the latter lack catalytic activity, two different mechanisms are ...
Synergism between basic Asp49 and Lys49 phospholipase A2 myotoxins of viperid snake venom in vitro and in vivo
(PLoS One 9(10):e109846, 2014-10-07)
Two subtypes of phospholipases A2 (PLA2s) with the ability to induce myonecrosis, ‘Asp49’ and ‘Lys49’ myotoxins, often coexist in viperid snake venoms. Since the latter lack catalytic activity, two different mechanisms are ...
A new muscle damaging toxin, myotoxin II, from the venom of the snake Bothrops asper (terciopelo)
(1989)
A new muscle damaging toxin, myotoxin II, was purified from the venom of Bothrops asper by ion-exchange chromatography on CMSephadex C-25. The toxin is a dimeric, basic protein with a monomer mol.wt of 13,341, according ...
Characterization of a basic phospholipase A2-homologue myotoxin isolated from the venom of the snake Bothrops neuwiedii (yarará chica) from Argentina
(1999)
A basic protein was isolated by CM-Sephadex C-25 chromatography from the venom of
Bothrops neuwiedii from Argentina, and named B. neuwiedii myotoxin I. This protein
exerted local myotoxic and edema-forming e ects in mice, ...
Localization of Myotoxin I and Myotoxin II from the venom of Bothrops asper in a murine model
(2021)
Phospholipases A2 (PLA2s) and PLA2-like proteins are significant components of snake venoms. Some of these proteins act as potent toxins causing muscle necrosis, which may lead to amputation in severe envenomings. Fundamental ...
Immunoenzymatic quantitation of antibodies to Bothrops asper myotoxins after polyvalent antivenom administration in mice.
(1992)
Two quantitative enzyme-immunoassays (EIA) for Bothrops asper myotoxin and anti-myotoxin antibodies, respectively, were utilized to study their in vivo distribution in mice (Swiss, 18 to 20 g). 2. After polyvalent antivenom ...
Immunoenzymatic quantitation of antibodies to Bothrops asper myotoxins after polyvalent antivenom administration in mice.
(1992)
Two quantitative enzyme-immunoassays (EIA) for Bothrops asper myotoxin and anti-myotoxin antibodies, respectively, were utilized to study their in vivo distribution in mice (Swiss, 18 to 20 g). 2. After polyvalent antivenom ...
Immunohistochemical demonstration of the binding of bothrops asper myotoxin to skeletal muscle sarcolemma
(1987)
The binding of Bothrops asper myotoxin to mouse skeletal muscle was studied at both the light and electron microscope levels using the peroxidase anti-peroxidase technique. The toxin binds to muscle cell sarcolemma, and ...
Immunohistochemical demonstration of the binding of bothrops asper myotoxin to skeletal muscle sarcolemma
(1987)
The binding of Bothrops asper myotoxin to mouse skeletal muscle was studied at both the light and electron microscope levels using the peroxidase anti-peroxidase technique. The toxin binds to muscle cell sarcolemma, and ...