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

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Abstract

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.

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Authors and Affiliations

  1. Institute of Theoretical and Experimental Biophysics, Russian Academy of Science, Pushchino, Russia

    Galina D. Mironova, Yuri Yu. Skarga, Serguei M. Grigoriev, Alexander E. Negoda & Benjamen S. Marinov

  2. Department of Physiology and Biophysics, Pushchino State University, Pushchino, Russia

    Galina D. Mironova, Serguei M. Grigoriev & Alexander E. Negoda

  3. Institute of Cell Biophysics, Russian Academy of Sciences, Pushchino, Russia

    Oleg V. Kolomytkin

Authors
  1. Galina D. Mironova
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  2. Yuri Yu. Skarga
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  3. Serguei M. Grigoriev
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  4. Alexander E. Negoda
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  5. Oleg V. Kolomytkin
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  6. Benjamen S. Marinov
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Mironova, G.D., Skarga, Y.Y., Grigoriev, S.M. et al. Reconstitution of the Mitochondrial ATP-Dependent Potassium Channel into Bilayer Lipid Membrane1. J Bioenerg Biomembr 31, 159–163 (1999). https://doi.org/10.1023/A:1005408029549

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  • DOI: https://doi.org/10.1023/A:1005408029549

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