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• W2160147414 abstract "Charybdotoxin block of a Shaker K+ channel was studied in Xenopus oocyte macropatches. Toxin on rate increases linearly with toxin concentration in an ionic strength-dependent fashion and is competitively diminished by tetraethylammonium. On rate is insensitive to transmembrane voltage and to K+ on the opposite side of the membrane. Conversely, toxin off rate is insensitive to toxin concentration, ionic strength, and added tetraethylammonium but is enhanced by membrane depolarization or K+ (or Na+) in the trans solution. Charge neutralization of charybdotoxin Lys27, however, renders off rate voltage insensitive. Our results argue that block of voltage-gated K+ channels results from the binding of one toxin molecule, so that Lys27 enters the pore and interacts with K+ (or Na+) in the ion conduction pathway." @default.
• W2160147414 created "2016-06-24" @default.
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• W2160147414 creator A5021498481 @default.
• W2160147414 date "1993-10-01" @default.
• W2160147414 modified "2023-09-26" @default.
• W2160147414 title "Mechanism of charybdotoxin block of a voltage-gated K+ channel" @default.
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• W2160147414 doi "https://doi.org/10.1016/s0006-3495(93)81200-1" @default.
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