Functional reconstitution of ion channels from Paramecium cortex into artificial liposomes View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1995-04

AUTHORS

X. -L. Zhou, C. W. M. Chan, Y. Saimi, C. 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. More... »

PAGES

199-208

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00236833

DOI

http://dx.doi.org/10.1007/bf00236833

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1012268315

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/7544831


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