Isolation and characterization of the main toxic fraction from the venom of the false horned viper (Pseudocerastes fieldi).
The venom of Pseudocerastes fieldi was subjected to gel filtration on Sephadex G-75. Most of the protein and lethality of the venom were eluted in a major symmetrical peak (C). The lethality of this peak is confined to a basic protein fraction, Cb (pI greater than 9.5) separable by DEAE-cellulose chromatography. Two proteins with molecular sizes close to 16,000 daltons were isolated from this fraction by preparative acidic gel electrophoresis in the presence of Triton X-100. One of the proteins (CbII) is lethal to mice (LD50 = 1 mg/kg) and shows phospholipase A activity as well as direct hemolytic activity. The other protein (CbI) does not reveal any known biological activity. However, upon recombination of the two a synergistic lethal activity is evident (the LD50 of the mixture = 0.25 mg/kg). It is suggested that CbI may be a specifier which potentiates the toxicity of the phospholipase A at the target site.
D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D006168:Guinea Pigs; D006461:Hemolysis / Q000187:drug effects; D014757:Viper Venoms / Q000032:analysis* / Q000633:toxicity
D014757:Viper Venoms