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. 2003 Aug;49(8):525-9.
doi: 10.1139/w03-067.

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

R B Delston  1 , M H Kothary, K A Shangraw, B D Tall
Affiliations

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

R B Delston et al. Can J Microbiol. 2003 Aug.

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.

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