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

Autor:	J. Jean-Gilles Beaubrun, B. E. Eribo, N. C. Flores, S. K. Curtis, Mahendra H. Kothary, Ben D. Tall
Rok vydání:	2008
Předmět:	Molecular Sequence Data Porins Vibrio tubiashii Biology Polymerase Chain Reaction Applied Microbiology and Biotechnology Bacterial Proteins Vibrionaceae Environmental Microbiology Amino Acid Sequence Adhesins Bacterial Peptide sequence Gene Vibrio Gel electrophoresis chemistry.chemical_classification Sequence Homology Amino Acid Ecology Sequence Analysis DNA biology.organism_classification Molecular biology Amino acid DNA-Binding Proteins Biochemistry chemistry Receptors Virus Electrophoresis Polyacrylamide Gel Bacterial outer membrane Bacterial Outer Membrane Proteins Transcription Factors Food Science Biotechnology
Zdroj:	Applied and Environmental Microbiology. 74:907-911
ISSN:	1098-5336 0099-2240
DOI:	10.1128/aem.02052-07
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6905644240907b4c7c305b168beaf6e6 https://doi.org/10.1128/aem.02052-07 Zobrazit plný text záznamu