Purification of a serine protease of Vibrio parahaemolyticus and its characterization

Masami Ishihara, Ayako Kawanishi, Hirofumi Watanabe, Ken Ichi Tomochika, Shin Ichi Miyoshi, Sumio Shinoda

Research output: Contribution to journalArticlepeer-review

21 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)299-303
Number of pages5
Issue number4
Publication statusPublished - 2002


  • Serine protease
  • Vibrio parahaemolyticus

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Virology


Dive into the research topics of 'Purification of a serine protease of Vibrio parahaemolyticus and its characterization'. Together they form a unique fingerprint.

Cite this