Negrete-Abascal E, Tenorio V R, de la Garza M
Departamento de Biología Celular, Centro de Investigación y de Estudios Avanzados del IPN. Apdo. Postal 14-740 México, D.F. 07000, Mexico.
Curr Microbiol. 1999 Jan;38(1):64-7. doi: 10.1007/pl00006775.
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.
研究了多杀巴斯德菌向培养基中分泌蛋白酶的能力及其特性，所用菌株来自5种动物（牛、鸡、羊以及2株猪源菌株）。所有分离株均能产生多种分子量的蛋白酶。这些蛋白酶被认为是中性金属蛋白酶，因为它们在pH 6至7之间活性最佳，受螯合剂抑制，但不受其他蛋白酶抑制剂抑制，且可被钙重新激活。分离株产生的蛋白酶能够降解IgG。用70%硫酸铵沉淀所有多杀巴斯德菌分离株培养上清液中的几种蛋白质，能被针对胸膜肺炎放线杆菌纯化蛋白酶制备的多克隆抗血清识别。蛋白酶的产生可能在组织定植及多杀巴斯德菌相关疾病过程中发挥重要作用。
