Reconstitution of the Mitochondrial ATP-Dependent Potassium Channel into Bilayer Lipid Membrane1

Electrical properties and regulation of the mitochondrialATP-dependent potassium channel were studied. The channel protein wassolubilized from the mitochondrial membrane using an ethanol/water mixture.Reconstituted into a bilayer lipid membrane BLM), the protein formed aslightly voltage-dependent ch...

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Bibliographic Details
Published in:Journal of bioenergetics and biomembranes 1999-04, Vol.31 (2), p.159
Main Authors: Mironova, Galina D, Skarga, Yuri Yu, Grigoriev, Serguei M, Negoda, Alexander E, Kolomytkin, Oleg V, Marinov, Benjamen S
Format: Article
Language:English
Subjects:
ATP
Cells
Electrical properties
Ethanol
Online Access:Get full text
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Summary:Electrical properties and regulation of the mitochondrialATP-dependent potassium channel were studied. The channel protein wassolubilized from the mitochondrial membrane using an ethanol/water mixture.Reconstituted into a bilayer lipid membrane BLM), the protein formed aslightly voltage-dependent channel with a conductance of 10 pS in 100 mM KCl.Often, several channels worked simultaneously (clusters) when many channelswere incorporated into the BLM. The elementary channel and the clusters wereboth highly potassium selective. At concentrations of 1 to 10 μM, ATPfavors channel opening, while channels become closed at 1-3 mM ATP. GDP(0.5 mM) reactivated the ATP-closed channels without affecting the untreatedchannels. The sulfhydryl-reducing agent ditiothreitol increased the openprobability at concentrations of 1 to 3 mM, but damaged the selectivity ofthe channel.[PUBLICATION ABSTRACT]
ISSN:0145-479X
1573-6881
DOI:10.1023/A:1005408029549