Isolation and characterization of a zinc-containing metalloprotease expressed by Vibrio tubiashii-Reference-Cited by-同舟云学术

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

Published:2003-08-01 Issue:8 Volume:49 Page:525-529
ISSN:0008-4166
Container-title:Canadian Journal of Microbiology
language:en
Short-container-title:Can. J. Microbiol.

Author:

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

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.

Publisher

Canadian Science Publishing

Subject

Genetics,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Immunology,Microbiology

Link

http://www.nrcresearchpress.com/doi/pdf/10.1139/w03-067

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