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Myotoxin II from Bothrops asper (Terciopelo) venom is a lysine-49 phospholipase A2
(1991)
A basic, dimeric myotoxic protein, myotoxin II, purified from Bothrops asper venom has a similar molecular weight and is immunologically cross-reactive with antibodies raised to previously isolated B. asper phospholipases ...
Calcium ion independent membrane leakage induced by phospholipase-like myotoxins
(1992-12)
The two snake venom myotoxins ammodytin L and myotoxin II, purified respectively from Vipera ammodytes ammodytes and Bothrops asper, have phospholipase-like structures but lack an Asp-49 in the active site and are without ...
A new method for the detection of phospholipase A2 variants: identification of isozymes in the venoms of newborn and adult Bothrops asper (terciopelo) snakes
(1988)
A new method for the identification of phospholipase A2 isozymes in snake venoms is described. The technique is based on the separation of the venom components by isoelectric focusing in agarose gels, transfer of the protein ...
Molecular cloning and structural modelling of gamma-phospholipase A2 inhibitors from Bothrops atrox and Micrurus lemniscatus snakes
(2017-10-01)
Phospholipases A2 inhibitors (PLIs) produced by venomous and non-venomous snakes play essential role in this resistance. These endogenous inhibitors may be classified by their fold in PLIα, PLIβ and PLIγ. Phospholipases ...
Effects of Bothrops asper (terciopelo) myotoxin III, a basic phospholipase A2, on liposomes and mouse gastrocnemius muscle
(1993-02)
The action of Bothrops asper myotoxin III, a basic phospholipase A2 which induces acute muscle damage, was studied in mouse gastrocnemius muscle in vivo and in vitro and in multilamellar liposomes. Myonecrosis occurred ...
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 ...
Autocatalytic acylation of phospholipase-like myotoxins
(1995-04)
Several snake venoms contain a phospholipase A2 in which position 49 in the active site is occupied by a lysine or a serine instead of the aspartate residue normally found. Although these proteins do not bind Ca2+ and are ...
The amino acid sequence of a myotoxic phospholipase from the venom of Bothrops asper
(1990)
A myotoxic, basic phospholipase A2 (pI greater than 9.5) with anticoagulant activity has been purified from the venom of Bothrops asper, and its amino acid sequence determined by automated Edman degradation. It is distinct ...
Snake venom phospholipase A(2) inhibitors: Medicinal chemistry and therapeutic potential
(Bentham Science Publ Ltd, 2007-01-01)
Phospholipases A(2) (PLA(2)s) are commonly found in snake venoms from Viperidae, Hydrophidae and Elaphidae families and have been extensively studied due to their pharmacological and physiopathological effects in living ...
p-Bromophenacyl bromide modification of Bothrops asper myotoxin II, a lysine-49 phospholipase A2, affects its pharmacological activities
(1993-09)
Modification of Bothrops asper myotoxin II, a lysine-49 phospholipase A2 variant, was carried out with p-bromophenacyl bromide. Modified toxin did not show changes in its charge and immunological properties but two of its ...