Two types of scorpion neurotoxins characterized by their binding to two separate receptor sites on rat brain synaptosomes

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Summary

The neurotoxin II from the venom of the American scorpion Centruroides suffusus suffusus was iodinated using the lactoperoxydase method. The labeled toxin binds specifically to a single class of non interacting binding sites on rat brain synaptosomes. The dissociation constant is 3–4 nM and the capacity 800–1400 fmoles per mg of protein. No competition between this toxin and neurotoxin II from the African scorpion Androctonus australis Hector has been found. There are 6–10 times more sites for Centruroides than for Androctonus neurotoxin. Moreover, unlike the binding of the Androctonus neurotoxin, the binding of Centruroides neurotoxin II is not potential dependent. Therefore a distinction between scorpion neurotoxins is proposed according to their binding properties to rat brain synaptosomes.

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