title: Channel-forming (Porin) activity in Herpetosiphon aurantiacus Hp a2.
abstract: Detergent extracts of cell envelopes of the gliding bacterium Herpetosiphon aurantiacus formed channels in lipid bilayers. Fast protein liquid chromatography across a HiTrap-Q cation-exchange column demonstrated that a 45-kDa protein forms the channel. The observation of a channel-forming protein suggests that Herpetosiphon aurantiacus Hp a2 has a permeability barrier on its surface.
authors.affiliation: Institut für Biologie II, Mikrobiologie, Albert-Ludwigs-Universität, Freiburg, Germany.
authors.forename: Rainer
authors.initials: R
authors.lastname: Harwardt
authors.forename: Elke
authors.initials: E
authors.lastname: Maier
authors.forename: Hans
authors.initials: H
authors.lastname: Reichenbach
authors.forename: Jürgen
authors.initials: J
authors.lastname: Weckesser
authors.forename: Roland
authors.initials: R
authors.lastname: Benz
mesh_terms: D041862:Chloroflexi / Q000378:metabolism*; D007473:Ion Channels / Q000502:physiology*; D010539:Permeability; D018272:Porins / Q000032:analysis*
chemical_list: D007473:Ion Channels; D018272:Porins