The Journal of General Physiology
Track the topics, authors and articles important to you
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

This Article
Right arrow Full Text (PDF, 836K)
Right arrow Alert me when this article is cited
Right arrow Citation Map
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 Stampe, P.
Right arrow Articles by Begenisich, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Stampe, P.
Right arrow Articles by Begenisich, T.
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 107, 449-457, Copyright © 1996 by The Rockefeller University Press


ARTICLES

Unidirectional K+ fluxes through recombinant Shaker potassium channels expressed in single Xenopus oocytes

P Stampe and T Begenisich
Department of Pharmacology and Physiology, University of Rochester Medical Center, NY 14642, USA.

We describe a method to evaluate the ratio of ionic fluxes through recombinant channels expressed in a single Xenopus oocyte. A potassium channel encoded by the Drosophila Shaker gene tested by this method exhibited flux ratios far from those expected for independent ion movement. At a fixed extracellular concentration of 25 mM K+, this channel showed single-file diffusion with an Ussing flux-ratio exponent, n', of 3.4 at a membrane potential of -30 mV. There was an apparent, small voltage dependence of this parameter with n' values of 2.4 at -15 and -5 mV. These results indicate that the pore in these channels can simultaneously accommodate at least four K+ ions. If each of these K+ ions is in contact with two water molecules, the minimum length of the pore is 24 A.
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
Q. Ma, E. Pavlov, T. Britvina, G. W. Zamponi, and R. J. French
Trans-Channel Interactions in Batrachotoxin-Modified Rat Skeletal Muscle Sodium Channels: Kinetic Analysis of Mutual Inhibition between {micro}-Conotoxin GIIIA Derivatives and Amine Blockers
Biophys. J., November 1, 2008; 95(9): 4266 - 4276.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Gastrointest. Liver Physiol.Home page
C. Mahagita, S. M. Grassl, P. Piyachaturawat, and N. Ballatori
Human organic anion transporter 1B1 and 1B3 function as bidirectional carriers and do not mediate GSH-bile acid cotransport
Am J Physiol Gastrointest Liver Physiol, July 1, 2007; 293(1): G271 - G278.
[Abstract] [Full Text] [PDF]


Home page
JGPHome page
M. N. Krishnan, J.-P. Bingham, S. H. Lee, P. Trombley, and E. Moczydlowski
Functional Role and Affinity of Inorganic Cations in Stabilizing the Tetrameric Structure of the KcsA K+ Channel
J. Gen. Physiol., August 29, 2005; 126(3): 271 - 283.
[Abstract] [Full Text] [PDF]


Home page
JGPHome page
H. T. Kurata, L. R. Phillips, T. Rose, G. Loussouarn, S. Herlitze, H. Fritzenschaft, D. Enkvetchakul, C. G. Nichols, and T. Baukrowitz
Molecular Basis of Inward Rectification: Polyamine Interaction Sites Located by Combined Channel and Ligand Mutagenesis
J. Gen. Physiol., October 25, 2004; 124(5): 541 - 554.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
S. Berneche and B. Roux
A microscopic view of ion conduction through the K+ channel
PNAS, July 22, 2003; 100(15): 8644 - 8648.
[Abstract] [Full Text] [PDF]


Home page
JGPHome page
S. Ding and R. Horn
Tail End of the S6 Segment: Role in Permeation in Shaker Potassium Channels
J. Gen. Physiol., June 24, 2002; 120(1): 87 - 97.
[Abstract] [Full Text] [PDF]


Home page
JGPHome page
Z. Varga, M. D. Rayner, and J. G. Starkus
Cations Affect the Rate of Gating Charge Recovery in Wild-type and W434F Shaker Channels through a Variety of Mechanisms
J. Gen. Physiol., April 29, 2002; 119(5): 467 - 486.
[Abstract] [Full Text] [PDF]


Home page
JGPHome page
Z. Varga, M. D. Rayner, and J. G. Starkus
Cations Affect the Rate of Gating Charge Recovery in Wild-type and W434F Shaker Channels through a Variety of Mechanisms
J. Gen. Physiol., April 29, 2002; 119(5): 467 - 486.
[Abstract] [Full Text] [PDF]



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