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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 ...
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 ...
Inhibition of the myotoxic activity of Bothrops aspermyotoxin II in mice by immunization with its synthetic 13-mer peptide 115-129
(1999)
The region comprising amino acid residues 115±129 of myotoxin II, a Lys49
phospholipase A2 from the venom of Bothrops asper, was previously shown to constitute a
heparin binding site, and to be associated with its toxic ...
Individual expression patterns of myotoxin isoforms in the venom of the snake Bothrops Asper.
(1992)
In order to investigate the distribution of myotoxin isoforms in the snake Bothrops asper,
venoms from individual specimens were analyzed by a cathodic electrophoretic system for basic proteins
under native conditions.The ...
Isolation and partial characterization of a myotoxin from the venom of the snake Bothrops nummifer
(1986)
A myotoxin from the venom of the snake Bothrops nummifer was purified to homogeneity by ion-exchange chromatography on CM-Sephadex. The toxin is a basic dimer with a subunit molecular weight of 16,000, as estimated by ...
Purification and characterization of myotoxin IV, a phospholipase A2 variant, from Bothrops asper snake venom
(1995)
A basic myotoxic protein was purified from Bothrops asper venom. Like other basic Bothrops myotoxins, myotoxin IV induces acute muscle damage after intramuscular injection in mice and disrupts negatively charged liposomes ...
Detection of proteins antigenically-related to Bothrops asper myotoxin in crotaline snake venoms
(1987)
The presence of components antigenically related to Bothrops asper myotoxin was investigated by Western blotting and immunoelectrophoretic techniques. B. asper myotoxin is a non-glycosylated monomeric phospholipase A with ...
Comparative biochemical studies of myotoxic phospholipase A(2) from Bothrops venom
(Bentham Science Publ Ltd, 2001-06-01)
Venoms from Bothrops jararacussu, Bothrops asper, Bothrops atrox, Bothrops pirajai, Bothrops moojeni, Bothrops alternatus and Bothrops (Bothriopsis) bilineata were fractionated using a simplified procedure based on ...