Comparison of venoms from two subspecies of the false horned viper (Pseudocerastes persicus).

Gel-isoelectric focusing of Pseudocerastes persicus fieldi venom shows a simple pattern with very few protein bands, while the venom of P. p. persicus reveals close to 30 protein bands. Molecular sieve chromatography of P. p. persicus venom shows a typical elution profile of a viperid snake, with hemorrhagic activity and L-amino acid oxidase activity confined to the high molecular weight peak of proteins. In the venom of P. p. fieldi, which has no hemorrhagin or L-amino acid oxidase, the high molecular weight fraction of proteins is practically missing.