The Journal of General Physiology
Axon Instruments microelectrode amplifiers
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
This Article
Right arrow PDF (Full Text)
Right arrow Alert me when this article is cited
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JGP
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Moczydlowski, E.
Right arrow Articles by Miller, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Moczydlowski, E.
Right arrow Articles by Miller, C.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

The Journal of General Physiology, Vol 84, 687-704, Copyright © 1984 by The Rockefeller University Press

ARTICLES

Voltage-dependent blockade of muscle Na+ channels by guanidinium toxins

E Moczydlowski, S Hall, SS Garber, GS Strichartz and C Miller

Na+ channels from rat muscle plasma membrane vesicles were inserted into neutral planar phospholipid bilayers and were activated by batrachotoxin. Single channel blocking events induced by the addition of various guanidinium toxins were analyzed to derive the rates of channel-toxin association and dissociation. Blocking by tetrodotoxin, saxitoxin, and six natural saxitoxin derivatives containing sulfate or hydroxyl groups were studied. Although the binding affinities vary over 2,000-fold, all of the toxins exhibit identical voltage dependence of the blocking reactions, regardless of the toxin's net charge. The results suggest that the voltage dependence of toxin binding is due to a voltage-dependent conformational equilibrium of the toxin receptor, rather than to direct entry of the charged toxin molecule into the applied transmembrane electric field.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Biophys. JHome page
E. Pavlov, T. Britvina, J. R. McArthur, Q. Ma, I. Sierralta, G. W. Zamponi, and R. J. French
Trans-Channel Interactions in Batrachotoxin-Modified Skeletal Muscle Sodium Channels: Voltage-Dependent Block by Cytoplasmic Amines, and the Influence of {micro}-Conotoxin GIIIA Derivatives and Permeant Ions
Biophys. J., November 1, 2008; 95(9): 4277 - 4288.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
D. Boda, W. Nonner, M. Valisko, D. Henderson, B. Eisenberg, and D. Gillespie
Steric Selectivity in Na Channels Arising from Protein Polarization and Mobile Side Chains
Biophys. J., September 15, 2007; 93(6): 1960 - 1980.
[Abstract] [Full Text] [PDF]

Home page
 JGPHome page
K. Hui, D. McIntyre, and R. J. French
Conotoxins as Sensors of Local pH and Electrostatic Potential in the Outer Vestibule of the Sodium Channel
J. Gen. Physiol., June 30, 2003; 122(1): 63 - 79.
[Abstract] [Full Text] [PDF]

Home page
 JGPHome page
B. Tanna, W. Welch, L. Ruest, J. L. Sutko, and A. J. Williams
An Anionic Ryanoid, 10-O-succinoylryanodol, Provides Insights into the Mechanisms Governing the Interaction of Ryanoids and the Subsequent Altered Function of Ryanodine-receptor Channels
J. Gen. Physiol., May 27, 2003; 121(6): 551 - 561.
[Abstract] [Full Text] [PDF]


  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents