Sea anemone toxin and scorpion toxin share a common receptor site associated with the action potential sodium ionophore.
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منابع مشابه
Sea anemone toxin and scorpion toxin share a common receptor site associated with the action potential sodium ionophore.
Toxin II isolated from the sea anemone Anemonia sulcata enhances activation of the action potential sodium ionophore of electrically excitable neuroblastoma cells by veratridine and batrachotoxin. This heterotropic cooperative effect is identical to that observed previously with scorpion toxin but occurs at a 110-fold higher concentration. Depolarization of the neuroblastoma cells inhibits the ...
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Depolarization of neuroblastoma cells causes a 70-fold increase in the apparent dissociation constant KD for scorpion toxin enhancement of activation of the action potential Na+ ionophore by veratridine and a large increase in the rate of reversal of scorpion toxin action. Depolarization also inhibits binding of 125I-labeled scorpion toxin to a small number of saturable binding sites on electri...
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The action of neurotoxins on tetrodotoxin-insensitive sodium channels in cultured rat muscle cells has been studied by ion flux methods. The alkaloid neurotoxins batrachotoxin, veratridine, and aconitine act at a common receptor site to cause persistent activation of sodium channels. Batrachotoxin is a full agonist, while veratridine and aconitine are partial agonists activating 8% and 1% of so...
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Scorpion toxin enhances activation of the action potential Na+ ionophore by the alkaloid neurotoxins veratridine, batrachotoxin, and aconitine. The pure toxin can be iodinated in a lactoperoxidase-catalyzed reaction. Both the monoiodoand diiodotoxin derivatives retain physiologic activity. Both monoiodoand diiodoscorpion toxin bind to a single class of saturable binding sites in electrically ex...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1978
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)34513-1