Metalloproteases secreted by Actinobacillus suis.
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 degrees C, 50 degrees C, 60 degrees C, and 70 degrees C, but their activity diminished at 80 degrees 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.
Negrete-Abascal
Erasmo
E
Carrera De Biología, Facultad de Estudios Superiores Iztacala, UNAM, Av. de los Barrios # 1, Los Reyes Iztacala, Tlalnepantla, Estado de México, 54090, México. enegrete@correo.iztacala.unam.mx
Pacheco
Sergio Vaca
SV
Paniagua
Gloria L
GL
Méndez
Alma Pérez
AP
Caballero
Jorge Ibarra
JI
Márquez
Víctor M Pérez
VM
Tenorio
Víctor R
VR
D044132:Actinobacillus suis / Q000201:enzymology*; D000907:Antibodies, Bacterial; D006863:Hydrogen-Ion Concentration; D045726:Metalloproteases / Q000378:metabolism*; D013696:Temperature
D000907:Antibodies, Bacterial; D045726:Metalloproteases