Abstract
Actinobacillus suis secretes metalloproteases into its medium. These secreted proteins, when concentrated by precipitation with 70% (NH4)2SO4 or methanol, displayed proteolytic activity at >200 kDa molecular mass bands in 10% polyacrylamide gels copolymerized with bovine casein (1%). They showed activity in a broad pH range (from pH 5 to pH 10) and were inhibited by 20 mM EDTA or EGTA, but could be reactivated by calcium. They were found heat stable at 40°C, 50°C, 60°C, and 70°C, but their activity diminished at 80°C or higher. They degraded pig and bovine IgG and cross-reacted with a polyclonal serum against a high molecular mass secreted protease from A. pleuropneumoniae. Extracellular proteases could play a role in diseases caused by A. suis.
Similar content being viewed by others
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Negrete-Abascal, ., Pacheco, ., Paniagua, . et al. Metalloproteases Secreted by Actinobacillus suis . Curr Microbiol 49, 55–58 (2004). https://doi.org/10.1007/s00284-004-4279-6
Issue Date:
DOI: https://doi.org/10.1007/s00284-004-4279-6