Dimeric Structure of Single Chloride Channels from Torpedo Electroplax
- Creators
- Miller, Christopher
- White, Michael M.
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 µM 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.
Additional Information
© 1984 by the National Academy of Sciences Communicated by Alfred G. Redfield, January 23, 1984 We are grateful to Drs. Ed Moczydlowski and Joan Bell for valuable discussions and suggestions and to Miss Sarah Garber for drawing Fig. 4. This work was supported by National Institutes of Health Research Grants GM-31768 and BRSG S07-RR07044. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.Attached Files
Published - MILpnas84.pdf
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Additional details
- PMCID
- PMC345152
- Eprint ID
- 6442
- Resolver ID
- CaltechAUTHORS:MILpnas84
- GM-31768
- NIH
- S07-RR07044
- NIH
- Created
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2006-12-09Created from EPrint's datestamp field
- Updated
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2021-11-08Created from EPrint's last_modified field