Abstract
A single point mutation of the rat sodium channel II reduces its sensitivity to tetrodotoxin and saxitoxin by more than three orders of magnitude. The mutation replaces glutamic acid 387 with a glutamine and has only slight effects on the macroscopic current properties, as measured under voltage-clamp in Xenopus oocytes injected with the corresponding cDNA-derived mRNA.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Electric Conductivity
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Membrane Potentials
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Mutation
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Rats
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Saxitoxin / pharmacology*
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Sodium Channels / drug effects*
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Sodium Channels / physiology
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Sodium Channels / ultrastructure
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Structure-Activity Relationship
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Tetrodotoxin / pharmacology*
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Xenopus laevis
Substances
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Sodium Channels
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Saxitoxin
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Tetrodotoxin