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AEM Accepts, published online ahead of print on 14 December 2007
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Appl. Environ. Microbiol. doi:10.1128/AEM.02052-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

The Isolation and Characterization of Outer Membrane Proteins and the Determination of a toxR Homolog in Vibrio tubiashii

J. Jean-Gilles Beaubrun*, M. H. Kothary, S. K. Curtis, N. C. Flores, B. E. Eribo, and B. D. Tall

Howard University, Washington, DC, 20050, and U.S. Food and Drug Administration, Laurel, MD 20708

* To whom correspondence should be addressed. Email: junia.beaubrun{at}fda.hhs.gov.


   Abstract

Outer membrane proteins (OMPs) expressed by Vibrio tubiashii under different environmental growth conditions were characterized by SDS-PAGE, N-terminal amino acid sequencing, and PCR analyses. Results showed the presence of a 38-40 kDa OmpU-like protein and ompU gene, a maltoporin-like protein, several novel OMPs, and a regulatory toxR homolog.







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