Abstract
Blocking agents of high selectivity are crucial in defining both physiologically and biochemically the molecular components that control membrane excitability. To obtain such probes for voltage-dependent ion channels, we have examined the venom of several American scorpions for the presence of polypeptide neurotoxins having the required properties. We report here that using voltage-clamped giant axons of the squid Loligo vulgaris we have identified in the venom of the scorpion Centruroides noxius Hoffmann a polypeptide (fraction II-11) that specifically depresses the peak permeability of K+ channels without affecting their voltage-dependent open–close kinetics. The venom also contains a polypeptide toxin (fraction II–10) that specifically depresses Na+ peak permeability with only minor effects on the activation–inactivation kinetics. Furthermore, the physiological effects of the whole venom on the squid giant axon can be assigned quantitatively to the combined action of the two polypeptides.
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Carbone, E., Wanke, E., Prestipino, G. et al. Selective blockage of voltage-dependent K+ channels by a novel scorpion toxin. Nature 296, 90–91 (1982). https://doi.org/10.1038/296090a0
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DOI: https://doi.org/10.1038/296090a0
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