Artículos de revistas
Fractionation Of Bothrops Jararacussu Snake Venom: Partial Chemical Characterization And Biological Activity Of Bothropstoxin
Registro en:
Toxicon. , v. 26, n. 7, p. 615 - 627, 1988.
410101
10.1016/0041-0101(88)90244-9
2-s2.0-0023878851
Autor
Homsi-Brandeburgo M.I.
Queiroz L.S.
Santo-Neto H.
Rodrigues-Simioni L.
Giglio J.R.
Institución
Resumen
A myotoxin, bothropstoxin (BthTX), showing no detectable phospholipase A2 activity, was purified to homogeneity from the venom of the Brazilian snake Bothrops jararacussu by a combination of gel filtration on Sephadex G-75 and ion-exchange chromatography on SP-Sephadex C-25. Four phospholipases (SIII-SPI to SIII-SPIV) were also isolated, the latter showing, similarly to BthTX (SIII-SPV) myonecrotic activity. Approximate mol. wts, as determined by SDS-PAGE, and pI of SIII-SPI to SIII-SPIV are: 22,400-4.2; 15,500-4.8; 13,800-6.9; and 13,200-7.7, respectively. BthTX is a single chain protein, approximate mol. wt 13,000, with 16 half-cystine residues, pI = 8.2 and LD50 = 7.5 mg/kg (i.p.) and 4.8 mg/kg (i.v.) for 20 g mice. The ten first N-terminal amino acid residues show a significant homology to other toxins with phospholipase structure. 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