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Current Microbiology

, Volume 38, Issue 1, pp 64–67 | Cite as

Secretion of Proteases from Pasteurella multocida Isolates

  • Erasmo  Negrete-Abascal
  • Victor R.  Tenorio
  • Mireya  de la Garza

Abstract.

The capability of Pasteurella multocida to secrete proteases to the culture medium and their characterization were studied in five animal isolates (bovine, chicken, sheep, and two from pig). All the isolates produced proteases in a wide range of molecular mass. It is suggested that they are neutral metalloproteases, since they were optimally active between pH 6 and 7, inhibited by chelating agents but not by other protease inhibitors, and reactivated by calcium. Proteases from isolates were able to degrade IgG. Several proteins from supernatants of cultures precipitated with 70% (NH4)2SO4 of all the P. multocida isolates were recognized by a polyclonal antiserum raised against a purified protease from Actinobacillus pleuropneumoniae. Protease production might play an important role during tissue colonization and in P. multocida diseases.

Keywords

Calcium Molecular Mass Protease Inhibitor Protease Production Polyclonal Antiserum 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag New York Inc. 1999

Authors and Affiliations

  • Erasmo  Negrete-Abascal
    • 1
  • Victor R.  Tenorio
    • 2
  • Mireya  de la Garza
    • 1
  1. 1.Departamento de Biología Celular, Centro de Investigación y de Estudios Avanzados del IPN. Apdo. Postal 14-740 México, D.F. 07000, Mexico MX
  2. 2.CENID-Microbiología, Carr. México-Toluca Km 15.5, Cuajimalpa, México, D.F. 05110, Mexico MX

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