artículo científico
Characterization of a basic phospholipase A2-homologue myotoxin isolated from the venom of the snake Bothrops neuwiedii (yarará chica) from Argentina
Fecha
1999Registro en:
0041-0101
10.1016/S0041-0101(99)00115-4
10519651
Autor
Geoghegan, Patricia
Angulo Ugalde, Yamileth
Cangelosi, Adriana
Díaz, Mónica
Lomonte, Bruno
Institución
Resumen
A basic protein was isolated by CM-Sephadex C-25 chromatography from the venom of
Bothrops neuwiedii from Argentina, and named B. neuwiedii myotoxin I. This protein
exerted local myotoxic and edema-forming e ects in mice, with potencies comparable to
other myotoxins isolated from Bothrops spp. venoms. When injected by i.v. route at doses
up to 4.7 mg/kg of body weight, the toxin was not lethal. In vitro, the toxin had no
detectable phospholipase A2 activity on egg yolk phospholipids. B. neuwiedii myotoxin I
appeared as a homodimer in sodium dodecylsulphate±polyacrylamide gel electrophoresis,
with a subunit molecular weight of 15 kD. Gel immunodi usion revealed a pattern of
partial antigenic identity between the newly isolated myotoxin and myotoxin II from
Bothrops asper venom. The sequence of B. neuwiedii myotoxin I was determined for the ®rst
40 amino acid residues, showing high homology to several class II phospholipase A2
myotoxins of the Lys-49 family from crotalids. Altogether, results suggest that this toxin is
a new member of the Lys-49 phospholipase A2-homologues with myotoxic, cytolytic, and
edema-inducing activities