The two-component toxin of Vipera palaestinae: contribution of phospholipase A to its activity.

@article{Simon1980TheTT,
  title={The two-component toxin of Vipera palaestinae: contribution of phospholipase A to its activity.},
  author={Thorsten Simon and Avner Bdolah and Elazar Kochva},
  journal={Toxicon : official journal of the International Society on Toxinology},
  year={1980},
  volume={18 3},
  pages={
          249-59
        }
}
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… CONTINUE READING
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