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Two phospholipase A2 inhibitors from the plasma of Cerrophidion (Bothrops) godmani which selectively inhibit two different group-II phospholipase A2 myotoxins from its own venom: isolation, molecular cloning and biological properties
(2000-03-15)
Myotoxic phospholipases A2 (PLA2s; group II) account for most of the muscle-tissue damage that results from envenomation by viperid snakes. In the venom of the Godman's viper (Cerrophidion godmani, formerly Bothrops godmani), ...
Structure of myotoxin-II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom
(2006)
Lys49 snake-venom phospholipase A2 (PLA2) homologues are highly myotoxic
proteins which, although lacking catalytic activity, possess the ability to disrupt
biological membranes, inducing significant muscle-tissue loss ...
Snake Venomics of the Lesser Antillean Pit Vipers Bothrops caribbaeus and Bothrops lanceolatus: Correlation with Toxicological Activities and Immunoreactivity of a Heterologous Antivenom
(2008-10)
The venom proteomes of the snakes Bothrops caribbaeus and Bothrops lanceolatus, endemic to the
Lesser Antillean islands of Saint Lucia and Martinique, respectively, were characterized by reversephase
HPLC fractionation, ...
Structural and functional characterization of myotoxin I, a Lys49 phospholipase A(2) homologue from Bothrops moojeni (Caissaca) snake venom
(2000-01-01)
Myotoxin-I (MjTX-I) was purified to homogeneity from the venom of Bothrops moojeni by ion-exchange chromatography on CM-Sepharose. Its molecular weight, estimated by SDS–PAGE, was 13,400 (reduced) or 26,000 (unreduced). ...
Snake venomics of the South and Central American Bushmasters. Comparison of the toxin composition of Lachesis muta gathered from proteomic versus transcriptomic analysis
(2008-04-30)
We report the proteomic characterization of the venoms of two closely related pit vipers of the genus Lachesis, L. muta (South American Bushmaster) and L. stenophrys (Central American Bushmaster), and compare the toxin ...
Differential susceptibility of C2C12 myoblasts and myotubes to group II phospholipase A2 myotoxins from crotalid snake venoms
(2005)
Group II phospholipase A2 (PLA2) myotoxins isolated from Viperidae/Crotalidae snake venoms induce a rapid cytolytic
effect upon diverse cell types in vitro. Previous studies suggested that this effect could be more ...
The Phospholipase A2 Homologues of Snake Venoms: Biological Activities and Their Possible Adaptive Roles
(2009)
A particular subgroup of toxins with phospholipase A2 (PLA2) structure, but devoid of this enzymatic activity, is commonly found in the venoms of snakes of the family Viperidae, and known as the PLA2 homologues. Among ...
Skeletal muscle necrosis and regeneration after injection of Thalassophryne nattereri (niquim) fish venom in mice
(2001-02)
Stings by Thalassophryne nattereri are responsible for envenomation of fishermen in north-eastern Brazil. Its venom induces prominent local tissue damage, characterized by pain, oedema and necrosis. The pathogenesis of ...
Ability of fucoidan to prevent muscle necrosis induced by snake venom myotoxins: comparison of high- and low-molecular weight fractions
(2008)
Fucoidan, a natural polysaccharide extracted from brown seaweed, inhibits the myotoxic phospholipases A2 present in
the venoms of crotalid snakes. This study evaluated the influence of molecular weight on the ability of ...
Hemostatic effects induced by Thalassophryne nattereri fish venom: a model of endothelium-mediated blood flow impairment.
(2002-08)
Accidents by Thalassophryne nattereri fish venom are characterised by severe local symptoms and signs including pain of fast onset, oedema and necrosis with impaired muscle regeneration. These effects have been related to ...