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Purification of a Serine Protease of Vibrio parahaemolyticus and Its Characterization
Author(s) -
Ishihara Masami,
Kawanishi Ayako,
Watanabe Hirofumi,
Tomochika Kenichi,
Miyoshi Shinichi,
Shinoda Sumio
Publication year - 2002
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.2002.tb02699.x
Subject(s) - protease , vibrio parahaemolyticus , proteases , biology , serine protease , biochemistry , vibrio alginolyticus , masp1 , serine , vibrionaceae , microbiology and biotechnology , enzyme , vibrio , chromatography , bacteria , chemistry , genetics , gene
A 50 kDa protease designated as VPP1 was purified from the culture supernatant of a clinical strain of Vibrio parahaemolyticus by ammonium sulfate fractionation, Sephacryl S‐200 HR gel filtration and Fractogel EMD TMAE 650 ion‐exchange chromatography. VPP1 was inhibited by EDTA, EGTA and serine protease inhibitors, suggesting that it is a calcium‐dependent serine protease. N‐terminal amino acid sequence of VPP1 was quite similar to that of V. metschnikovii protease and antibody against VPP1 inhibited the activity of V. metschnikovii protease, suggesting the similarity of the two proteases. It was demonstrated that VPP1 or its related protease widely distribute in not only V. parahaemolyticus but also V. alginolyticus .