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Journal of Bacteriology, January 2001, p. 800-803, Vol. 183, No. 2
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.2.800-803.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Identification of the Outer Membrane Porin of Thermus thermophilus HB8: the Channel-Forming Complex Has an Unusually High Molecular Mass and an Extremely Large Single-Channel Conductance

Elke Maier,1 Georg Polleichtner,1 Birgit Boeck,2 Reinhard Schinzel,2 and Roland Benz1,*

Lehrstuhl für Biotechnologie1 and Lehrstuhl für Physiologische Chemie I,2 Theodor-Boveri-Institut (Biozentrum) der Universität Würzburg, D-97074 Würzburg, Germany

Received 28 June 2000/Accepted 20 October 2000

The outer membrane of the thermophilic bacterium Thermus thermophilus was isolated using sucrose step gradient centrifugation. Its detergent extracts contained an ion-permeable channel with an extremely high single-channel conductance of 20 nS in 1 M KCl. The channel protein was purified by preparative sodium dodecyl sulfate (SDS)-polyacylamide gel electrophoresis. It has a high molecular mass of 185 kDa, and its channel-forming ability resists boiling in SDS for 10 min.

* Corresponding author. Mailing address: Lehrstuhl für Biotechnologie, Theodor-Boveri-Institut (Biozentrum) der Universität Würzburg, Am Hubland, D-97074 Würzburg, Germany. Phone: 49-931-888-4501. Fax: 49-931-888-4509. E-mail: roland.benz{at}mail.uni-wuerzburg.de.

Journal of Bacteriology, January 2001, p. 800-803, Vol. 183, No. 2
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.2.800-803.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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