Isolation and characterization of a zinc-containing metalloprotease expressed by Vibrio tubiashii

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Abstract:

A Vibrio tubiashii hemagglutinin, a protease, was purified by ammonium sulfate precipitation, gel filtration, and hydrophobic interaction chromatography. It agglutinates sheep, chicken, bovine, rabbit, guinea pig, and human erythrocytes. It has a molecular mass of 35 kDa, isoelectric points of 3.5 and 3.7, and is inhibited by ortho-phenanthro line, phosphoramidon, and Zincov. The N-terminal amino acid sequence (Ala-Gln-Ala-Thr-Gly-Thr-Gly- Pro-Gly-Gly-Asn-Gln-Lys-Thr-Gly-Gln- Tyr-Asn-Phe-Gly) has strong homology to other Vibrio proteases.Key words: Vibrio tubiashii, metalloprotease, hemagglutinin.

Une hémagglutinine/protéase de Vibrio tubiashii a été purifiées par précipitation au sulfate d'ammonium, filtration sur gel et chromatographie hydrophobe. Elle agglutine les érythrocytes du mouton, du poulet, bovins, du lapin, du cobaye, et humains. Elle a une masse moléculaire de 35 kDa, des points isoélectriques de 3,5 et 3,7, et est inhibée par l'ortho-phenanthroline, le phosphoramidon et le Zincov. L'ordre des acides aminés en N-terminal (Ala-Gln-Ala-Thr-Gly-Thr-Gly- Pro-Gly-Gly-Asn-Gln-Lys-Thr-Gly-Gln- Tyr-Asn-Phe-Gly) démontre une forte homologie à d'autres protéases de Vibrio.Mots clés : Vibrio tubiashii, métalloprotéase, hémagglutinine.

Document Type: Research Article

Publication date: August 1, 2003

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  • Published since 1954, this monthly journal contains new research in the field of microbiology including applied microbiology and biotechnology; microbial structure and function; fungi and other eucaryotic protists; infection and immunity; microbial ecology; physiology, metabolism and enzymology; and virology, genetics, and molecular biology. It also publishes review articles and notes on an occasional basis, contributed by recognized scientists worldwide.
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