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A voltage-gated anion channel from the electric organ of Torpedo californica.
Open accessAbstract
Addition of membrane vesicles prepared from the electric organ of Torpedo californica to the aqueous phase of a planar phospholipid bilayer system results in a large (up to 3 orders of magnitude) stepwise increase in membrane conductance. This increased conductance consists of two components: an ohmic background "leak" and a voltage-dependent, ideally anion-selective conductance. The anion conductance is low at voltages greater than +10 mV, rises sharply as the voltage becomes negative, and then saturates as the voltage becomes highly negative. (The trans side of the bilayer, to which vesicles are not added, is defined as ground.) Under high amplification, the anion conductance shows single channel behavior with a voltage-independent, single channel conductance of 13.9 +/- 0.1 pmho in 0.1 M Cl-. Furthermore, the anion channel, but not the background conductance, is inhibited by submillimolar concentrations of SITS and DIDS, two well known anion transport inhibitors. The inhibition is seen only when SITS or DIDS is added to the cis side. No cholinergic agents tested have any effect on the channel.
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Cited by
X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity
Dutzler, R., Campbell, E. B., Cadene, M., Chait, B. T., & MacKinnon, R. (2002) · Nature · doi:10.1038/415287a · Cited by 1,446
Lysosomal acidification mechanisms
Mindell, J. A. (2012) · Annual Review of Physiology · doi:10.1146/annurev-physiol-012110-142317 · Cited by 1,258
Molecular Structure and Physiological Function of Chloride Channels
Jentsch, T. J., Stein, V., Weinreich, F., & Zdebik, A. A. (2002) · Physiological Reviews · doi:10.1152/physrev.00029.2001 · Cited by 1,256
Open-state substructure of single chloride channels from Torpedo electroplax
Miller, C. (1982) · Philosophical Transactions of the Royal Society of London. B, Biological Sciences · doi:10.1098/rstb.1982.0140 · Cited by 414
Self-citationThe Cl-/H+ antiporter ClC-7 is the primary chloride permeation pathway in lysosomes
Graves, A. R., Curran, P. K., Smith, C. L., & Mindell, J. A. (2008) · Nature · doi:10.1038/nature06907 · Cited by 399
Metadata
- Authors
- White, M. M., & Miller, C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1979-10
- Volume
- 254
- Issue
- 20
- Pages
- 10161-10166
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1600283399
- Cited by
- 194
- References
- 0
- FWCI
- 1.36
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- White, M. M., & Miller, C. (1979). A voltage-gated anion channel from the electric organ of Torpedo californica. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)86687-5
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