Open AccessOuter membrane porin protein of Campylobacter jejuni
Author(s) -
Huyer M.,
Parr T.R.,
Hancock R.E.W.,
Page W.J.
Publication year - 1986
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1986.tb01803.x
Subject(s) - porin , bacterial outer membrane , campylobacter jejuni , conductance , membrane , lipid bilayer , chemistry , ion channel , membrane protein , biophysics , campylobacter fetus , microbiology and biotechnology , biology , biochemistry , bacteria , escherichia coli , physics , receptor , genetics , gene , condensed matter physics
Protein e, a 43‐kDa protein from the outer membrane of Campylobacter jejuni UA580, was purified and reconstituted into lipid bilayer membranes. It was shown to form small channels with a single channel conductance of 8.82 nS in 1M KCl. Zero current potential measurements demonstrated that the channel was approx. 10‐fold selective for K + over Cl − ions. A porin with a similar single channel conductance was observed in fractions from the outer membrane of Campylobacter fetus UA60.