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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 ...
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 ...
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 ...
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 ...
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 ...
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, ...
Immunochemical properties of the N-terminal helix of myotoxin II, a lysine-49 phospholipase A2 from Bothrops asper snake venom
(2001)
Myotoxic class II phospholipases A2 from snake venoms can be divided into Asp49 and Lys49 types. The latter, including
Bothrops asper myotoxin II, exert membrane damage despite lacking catalytic activity. A heparin-binding, ...
Immunochemical properties of the N-terminal helix of myotoxin II, a lysine-49 phospholipase A2 from Bothrops asper snake venom
(2001)
Myotoxic class II phospholipases A2 from snake venoms can be divided into Asp49 and Lys49 types. The latter, including
Bothrops asper myotoxin II, exert membrane damage despite lacking catalytic activity. A heparin-binding, ...
Broad cytolytic specificity of myotoxin II, a lysine-49 phospholipase A2 of Bothrops asper snake venom
(1994)
The cytotoxic activity of Bothrops asper myotoxin II, a lysine-49 phospholipase A2 isoform, on different cell types in culture, was investigated. Myotoxin II caused a dose-dependent cytolytic effect on all cell types tested, ...
Broad cytolytic specificity of myotoxin II, a lysine-49 phospholipase A2 of Bothrops asper snake venom
(1994)
The cytotoxic activity of Bothrops asper myotoxin II, a lysine-49 phospholipase A2 isoform, on different cell types in culture, was investigated. Myotoxin II caused a dose-dependent cytolytic effect on all cell types tested, ...