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Phospholipases A2 From Viperidae Snake Venoms: How do They Induce Skeletal Muscle Damage?
(Acta Chim. Slov., 58, 647–659, 2011, 2011)
Phospholipases A2 (PLA2s) are abundant components in snake venoms, which play important toxic roles. This review
focuses on group II PLA2s endowed with myotoxic effects, present in Viperidae venoms. These PLA2s are ...
Pathogenic mechanisms underlying adverse reactions induced by intravenous administration of snake antivenoms
(2013-12-15)
Snake antivenoms are formulations of immunoglobulins, or immunoglobulin fragments, purified from the plasma of animals immunized with snake venoms. Their therapeutic success lies in their ability to mitigate the progress ...
Preclinical efficacy of Australian antivenoms against the venom of the small-eyed snake, Micropechis ikaheka, from Papua New Guinea: An antivenomics and neutralization study
(2014-10-14)
There is no specific antivenom for the treatment of envenoming by the small-eyed snake, Micropechis ikaheka, a dangerous fossorial species endemic to Papua New Guinea, Irian Jaya (West Papua) and neighbouring islands. This ...
Characterization of a novel snake venom component: Kazal-type inhibitor-like protein from the arboreal pitviper Bothriechis schlegelii
(2016-06)
Snake venoms are composed mainly of a mixture of proteins and peptides. Notably, all snake venom toxins have been assigned to a small number of protein families. Proteomic studies on snake venoms have recently identified ...
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), ...
Evaluación de la capacidad de cuatro antivenenos comerciales para neutralizar el veneno de la serpiente Bothrops asper (terciopelo) de Costa Rica
(1995-09)
We studied the ability of four commercially available antivenoms to neutralize several toxic and enzymatic activities of Bothrops asper (terciopelo) venom from Costa Rica. Experiments with preincubation of venom and antivenom ...
Isolation and biochemical, functional and structural characterization of a novel L-amino acid oxidase from Lachesis muta snake venom
(2012-12-01)
The aim of this study was the isolation of the LAAO from Lachesis muta venom (LmLAAO) and its biochemical, functional and structural characterization. Two different purification protocols were developed and both provided ...
Muscle phospholipid hydrolysis by Bothrops asper Asp49 and Lys49 phospholipase A2 myotoxins – distinct mechanisms of action
(2013-07-12)
Bothrops snakes are the major cause of ophidian envenomings in Latin America. Their venom contains myotoxins that cause prominent muscle damage, which may lead to permanent disability. These toxins include myotoxins Mt-I ...
Effects of chemical modifications of crotoxin B, the phospholipase A2 subunit of crotoxin from Crotalus durissus terrificus snake venom, on its enzymatic and pharmacological activities
(2001-09-01)
Crotoxin B, the basic Asp49-PLA2 subunit from crotoxin, the main component of Crotalus durissus terrificus venom, displays myotoxic, edema-inducing, bactericidal (upon Escherichia coli), liposomal-disrupting and anticoagulant ...
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 ...