Isolation and Characterization of Vibrio tubiashii Outer Membrane Proteins and Determination of a toxR Homolog
Author(s) -
Junia Jean-Gilles Beaubrun,
Mahendra H. Kothary,
Sherill K. Curtis,
Noemí Flores,
Broderick E. Eribo,
Ben D. Tall
Publication year - 2007
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.02052-07
Subject(s) - bacterial outer membrane , biology , gel electrophoresis , polyacrylamide gel electrophoresis , vibrio cholerae , biochemistry , sodium dodecyl sulfate , membrane protein , bacteria , vibrionaceae , peptide sequence , vibrio , amino acid , gene , microbiology and biotechnology , escherichia coli , genetics , membrane , enzyme
Outer membrane proteins (OMPs) expressed by Vibrio tubiashii under different environmental growth conditions were characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, N-terminal amino acid sequencing, and PCR analyses. Results showed the presence of a 38- to 40-kDa OmpU-like protein and ompU gene, a maltoporin-like protein, several novel OMPs, and a regulatory toxR homolog.
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