Abstract
The heat stable toxic fraction of Vipera palaestinae venom contains a basic (pI 10) non-enzymic component and an acidic (pI 4·5) phospholipase A. The purified phospholipase appears as a single protein band in SDS-gel electrophoresis corresponding to a mol. wt of 15,000. An antitoxic factor previously isolated from the blood serum of Vipera palaestinae inhibits both lethality of the toxic fraction and phospholipase activity of the acidic component. Heterologous phospholipases from the venoms of Pseudocerastes fieldi and Walterinnesia aegyptia, but not from the porcine pancreas could be substituted for the original enzyme in the Vipera two-component toxic system. It is thus evident that phospholipase is an integral part of the V. palaestinae toxin, and it is either species- or organ-specific.
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