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Immunohistochemical demonstration of the binding of bothrops asper myotoxin to skeletal muscle sarcolemma
(1987)
The binding of Bothrops asper myotoxin to mouse skeletal muscle was studied at both the light and electron microscope levels using the peroxidase anti-peroxidase technique. The toxin binds to muscle cell sarcolemma, and ...
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 ...
Effects of a myotoxic phospholipase A2 isolated from Bothrops asper venom on skeletal muscle sarcoplasmic reticulum
(1987)
The myotoxin from B. asper snake venom inhibited Ca-ATPase activity of rabbit sarcoplasmic reticulum after incubation in vitro. Inhibition was non-competitive and albumin enhanced the effect of the toxin. Furthermore, B. ...
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). ...
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 ...
Isolation and partial characterization of a myotoxin from the venom of the snake Bothrops nummifer
(1986)
A myotoxin from the venom of the snake Bothrops nummifer was purified to homogeneity by ion-exchange chromatography on CM-Sephadex. The toxin is a basic dimer with a subunit molecular weight of 16,000, as estimated by ...
Cellular pathology induced by snake venom phospholipase A2 myotoxins and neurotoxins: common aspects of their mechanisms of action
(2008-06-20)
A large variety of snake toxins evolved from PLA2 digestive enzymes through a process of ‘accelerated evolution’. These toxins have different tissue targets, membrane receptors and mechanisms of alteration of the cell ...
Detection of proteins antigenically-related to Bothrops asper myotoxin in crotaline snake venoms
(1987)
The presence of components antigenically related to Bothrops asper myotoxin was investigated by Western blotting and immunoelectrophoretic techniques. B. asper myotoxin is a non-glycosylated monomeric phospholipase A with ...
An Asp49 Phospholipase A2 from Snake Venom Induces Cyclooxygenase-2 Expression and Prostaglandin E2 Production via Activation of NF-κB, p38MAPK, and PKC in Macrophages
(2014)
Phospholipases A2 (PLA2) are key enzymes for production of lipid mediators. We previously demonstrated that a snake venom sPLA2 named MT-III leads to prostaglandin (PG)E2 biosynthesis in macrophages by inducing the expression ...
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 ...