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Am J Physiol Cell Physiol 264: C1489-C1499, 1993;
0363-6143/93 $5.00
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AJP - Cell Physiology, Vol 264, Issue 6 C1489-C1499, Copyright © 1993 by American Physiological Society

ARTICLES

Single-channel characteristics of a purified bovine renal amiloride-sensitive Na+ channel in planar lipid bilayers

Y. Oh and D. J. Benos
Department of Physiology and Biophysics, University of Alabama, Birmingham 35294.

We have purified an amiloride-inhibitable Na+ channel protein from bovine renal papillae using ion-exchange and immunoaffinity chromatography. In the present study, these purified Na+ channels were reconstituted into planar lipid bilayers, and their single-channel characteristics were studied. We observed both large- and small-conductance Na(+)-selective ion channels in planar lipid bilayers. Single-channel conductance for the large- and small-conductance channels saturated as a function of Na+ concentration. These relations could be fitted by a simple Langmuir isotherm with a Michaelis constant of 55 and 45 mM and a maximum open-state conductance of 56 or 8.4 pS, respectively. Both channels were perfectly cation selective, with a Na(+)-to-K+ permeability ratio of 6.7:1 for the large channel and 7.8:1 for the small channel, and their open single-channel current-voltage relations were linear when bathed with symmetrical Na+ solutions. The percent open time of the reconstituted large or small channels varied between 10 and 50% or 1 and 20%, respectively. After application of amiloride, both the large- and small-conductance Na+ channels were inhibited in a dose-dependent manner.


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