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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 ...
Neutralization of myotoxic phospholipases A2 from the venom of the snake Bothrops asper by monoclonal antibodies
(1992)
The neutralization of two myotoxic phospholipases A2 from the venom of Bothrops asper, myotoxins I and II, by two murine monoclonal antibodies is reported. The monoclonal antibodies, MAb-3 and Mab-4, recognize different ...
An electrophoretic study on phospholipase A2 isoenzymes in the venoms of Central American crotaline snakes
(1992)
The number and isoelectric points of phospholipase A2 isoenzymes were studied in the venoms of 12 Central American crotaline snakes of the genera Bothrops, Crotalus, Lachesis and Agkistrodon. The study was carried out 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 ...
Cleavage of the NH2-Terminal Octapeptide of Bothrops asper Myotoxic Lysine-49 Phospholipase A2 Reduces Its Membrane-Destabilizing Effect
(1994-08)
Bothrops asper myotoxin II was cleaved with cyanogen bromide to determine the role of NH2-terminal amino acid residues in its ability to destabilize negatively charged liposomes and to induce myonecrosis. After treatment, ...
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 ...
The effect of myotoxins isolated from Bothrops snake venoms on multilamellar liposomes: relationship to phospholipase A2, anticoagulant and myotoxic activities
(1991-12)
The effect of four myotoxins isolated from Bothrops snake venoms on the release of peroxidase trapped in large multilamellar liposomes was studied and correlated to their phospholipase A2, myotoxic and anticoagulant ...
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 ...
Isolation and characterization of basic myotoxic phospholipases A2 from Bothrops godmani (Godman's pit viper) snake venom
(1992)
Two basic myotoxic phospholipases A2 were purified to homogeneity from the venom of Bothrops godmani from Costa Rica by ion-exchange chromatography on CM-Sephadex. They have molecular weights of 14,300 (myotoxin I) and ...
Preclinical evaluation of the efficacy of antivenoms for snakebite envenoming: State-of-the-art and challenges ahead
(2017-05)
Animal-derived antivenoms constitute the mainstay in the therapy of snakebite envenoming. The efficacy of antivenoms to neutralize toxicity of medically-relevant snake venoms has to be demonstrated through meticulous ...