Kozaki S, Asao T, Kamata Y, Sakaguchi G
Department of Veterinary Science, College of Agriculture, University of Osaka Prefecture, Japan.
J Clin Microbiol. 1989 Aug;27(8):1782-6. doi: 10.1128/jcm.27.8.1782-1786.1989.
Aeromonas sobria produces hemolysin in a form activable with trypsin under defined cultural conditions. In immunoblotting analyses with the culture supernatant of A. sobria, the monoclonal antibody reacting specifically to Aeromonas hydrophila CA-11 hemolysin bound to the 53,000- and 49,000-dalton bands before and after trypsinization, respectively. The monoclonal antibody reacting to A. hydrophila AH-1 hemolysin did not bind either band. A. sobria hemolysin is, therefore, related antigenically to CA-11 hemolysin, while the molecular weights before and after activation differ from those of A. hydrophila hemolysins, being 54,000 and 51,000, respectively. The hemolytic and enterotoxigenic activities of A. sobria hemolysin were both neutralized by the monoclonal antibody against CA-11 hemolysin. It seems, therefore, that the same site on A. sobria hemolysin is responsible for both biological activities.
温和气单胞菌在特定培养条件下产生一种可被胰蛋白酶激活的溶血素。在用温和气单胞菌培养上清液进行的免疫印迹分析中,与嗜水气单胞菌CA - 11溶血素特异性反应的单克隆抗体,分别与胰蛋白酶处理前后的53,000道尔顿和49,000道尔顿条带结合。与嗜水气单胞菌AH - 1溶血素反应的单克隆抗体未与任何一条带结合。因此,温和气单胞菌溶血素在抗原性上与CA - 11溶血素相关,而激活前后的分子量与嗜水气单胞菌溶血素不同,分别为54,000和51,000。温和气单胞菌溶血素的溶血活性和产肠毒素活性均被抗CA - 11溶血素的单克隆抗体中和。因此,似乎温和气单胞菌溶血素上的同一部位负责这两种生物学活性。