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Cited by 257

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Dimeric structure of single chloride channels from Torpedo electroplax.

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Miller, C, White, M M·1984·Proceedings of the National Academy of Sciences

Abstract

The inhibition by 4,4'-diisothiocyano-2,2'-stilbenedisulfonate (DIDS) of Cl- channels from Torpedo electroplax incorporated in planar phospholipid bilayer membranes is studied. DIDS irreversibly and rapidly inhibits the macroscopic conductance of membranes containing many channels. At the single-channel level, the effect of DIDS is more complicated. The uninhibited single channel displays three "substates" of conductances 20, 10, and 0 pS. Short exposure (5-30 s) to 10 microM DIDS converts this three-level active channel into a "conventional" channel of 10-pS conductance. Longer exposure eliminates all channel fluctuations. The results are taken as strong evidence that the Cl- channel is constructed as a functional dimer of identical protein subunits.

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Metadata

Authors
Miller, C., & White, M. M.
Venue
Proceedings of the National Academy of Sciences
Published
1984-05
Volume
81
Issue
9
Pages
2772-2775
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2059610950
Cited by
257
References
0
FWCI
2.30
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Dimeric structure of single chloride channels from Torpedo electroplax. https://app.cochat.ai/papers/10.1073/pnas.81.9.2772
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Miller, C., & White, M. M. (1984). Dimeric structure of single chloride channels from Torpedo electroplax. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.81.9.2772

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