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Journal article
Dimeric Structure of Single Chloride Channels from Torpedo Electroplax
Proceedings of the National Academy of Sciences - PNAS, v 81(9), pp 2772-2775
01 May 1984
PMID: 6326143
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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 μ M 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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Details
- Title
- Dimeric Structure of Single Chloride Channels from Torpedo Electroplax
- Creators
- Christopher MillerMichael M. White
- Publication Details
- Proceedings of the National Academy of Sciences - PNAS, v 81(9), pp 2772-2775
- Publisher
- National Academy of Sciences of the United States of America
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Pharmacology and Physiology
- Web of Science ID
- WOS:A1984SR73200036
- Scopus ID
- 2-s2.0-0021180163
- Other Identifier
- 991020837743604721
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- Biology