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Mostrando ítems 11-19 de 19
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, ...
Synthetic peptides derived from the C-terminal region of Lys49 phospholipase A2 homologues from Viperidae snake venoms: biomimetic activities and potential applications
(2010)
Lys49-phospholipase A2 homologues constitute a large family of toxins present in the venoms of viperid snake species, which
despite lacking catalytic activity, cause significant skeletal muscle necrosis. The main structural ...
Biochemistry and toxicology of toxins purified from the venom of the snake Bothrops asper
(2009-12-01)
The isolation and study of individual snake venom components paves the way for a deeper
understanding of the pathophysiology of envenomings – thus potentially contributing to
improved therapeutic modalities in the clinical ...
Isolation, characterization and molecular cloning of AnMIP, a new α-type phospholipase A2 myotoxin inhibitor from the plasma of the snake Atropoides nummifer (Viperidae: Crotalinae)
(2007)
A new phospholipase A2 (PLA2)-inhibitory protein was isolated from the plasma of Atropoides nummifer, a crotaline snake from Central
America. This inhibitor was named AnMIP, given its ability to neutralize the activity ...
Stability, distribution and use of antivenoms for snakebite envenomation in Latin America: Report of a workshop
(2009-05)
The issues of antivenom stability and distribution, and the training of health staff in the correct use of antivenoms in Latin America were discussed in a workshop held at Instituto Clodomiro Picado, Costa Rica, in September ...
Crystallization of the Lys49 PLA2 homologue, myotoxin II from the venom of Atropoides nummifer
(2004-12)
Myotoxin II, a Lys49 catalytically inactive phospholipase A2 homologue from Atropoides nummifer venom, was purified, characterized
and crystallized. The crystals belongs to the tetragonal system, space group P43212, with ...
Cytotoxicity induced in myotubes by a Lys49 phospholipase A2 homologue from the venom of the snake Bothrops asper: Evidence of rapid plasma membrane damage and a dual role for extracellular calcium
(2007-12)
Acute muscle tissue damage, myonecrosis, is a typical consequence of envenomations by snakes of the family Viperidae. Catalytically-inactive Lys49 phospholipase A2 homologues are abundant myotoxic components in viperid ...
Antimicrobial activity of myotoxic phospholipases A2 from crotalid snake venoms and synthetic peptide variants derived from their C-terminal region
(2005)
A short peptide derived from the C-terminal region of Bothrops asper myotoxin II, a Lys49 phospholipase A2 (PLA2), was
previously found to reproduce the bactericidal activity of its parent molecule. In this study, a panel ...
Snake venomics and antivenomics: Proteomic tools in the design and control of antivenoms for the treatment of snakebite envenoming
(2009-03-06)
Snakebite envenoming represents a neglected tropical disease that has a heavy public health impact, particularly in Asia, Africa and Latin America. A global initiative, aimed at increasing antivenom production and ...