PMID: 7544831Apr 1, 1995Paper

Functional reconstitution of ion channels from Paramecium cortex into artificial liposomes

The Journal of Membrane Biology
X L ZhouC Kung

Abstract

Toward isolating channel proteins from Paramecium, we have explored the possibility of functionally reconstituting ion channels in an artificial system. Proteins from Paramecium cortex reconstituted with soybean azolectin retained several channels whose activities were readily registered under patch clamp. The most commonly encountered activities were three: (i) a 71-pS cation channel that opens at all voltages unless di- or trivalent cations were added to close them, (ii) a 40 pS monovalent cation channel, and (iii) a large-conductance channel that prefers anions and exhibits many subconductance states. These channels survived mild detergent treatments without observable functional alterations. The possible origin of these channels from internal membranes, the possible role of 71-pS channel in internal Ca2+ release, and the prospects of their purification are discussed.

Citations

Apr 22, 2009·Molecular and Cellular Biology·Eva-Maria LadenburgerHelmut Plattner
May 1, 2004·Annual Review of Physical Chemistry·Mattias KarlssonOwe Orwar
Jun 22, 1999·The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society·H PlattnerL Bachmann

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