title: 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.
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.
authors.affiliation: Lehrstuhl für Biotechnologie, Theodor-Boveri-Institut (Biozentrum) der Universität Würzburg, D-97074 Würzburg, Germany.
authors.forename: E
authors.initials: E
authors.lastname: Maier
authors.forename: G
authors.initials: G
authors.lastname: Polleichtner
authors.forename: B
authors.initials: B
authors.lastname: Boeck
authors.forename: R
authors.initials: R
authors.lastname: Schinzel
authors.forename: R
authors.initials: R
authors.lastname: Benz
mesh_terms: D001692:Biological Transport; D002458:Cell Fractionation; D002462:Cell Membrane / Q000737:chemistry; D004553:Electric Conductivity; D008970:Molecular Weight; D018272:Porins / Q000302:isolation & purification*; D017680:Potassium Compounds / Q000378:metabolism; D016963:Thermus thermophilus
chemical_list: D018272:Porins; D017680:Potassium Compounds