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-Reference-Cited by-同舟云学术

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

Published:2001-01-15 Issue:2 Volume:183 Page:800-803
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Maier Elke¹,Polleichtner Georg¹,Boeck Birgit²,Schinzel Reinhard²,Benz Roland¹

Affiliation:

1. Lehrstuhl für Biotechnologie1 and

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

Abstract

ABSTRACT 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.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JB.183.2.800-803.2001

Reference37 articles.

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