Hartmann L, Schröder W, Lübke-Becker A
Institut für Mikrobiologie and Tierseuchen, Freie Universität Berlin, Germany.
Zentralbl Bakteriol. 1996 Jun;284(1):47-51. doi: 10.1016/s0934-8840(96)80152-6.
A polyclonal antibody prepared against the 35 kDa outer membrane protein (a putative porin) of Pasteurella (P.) multocida revealed binding to the 36 kDa major outer membrane protein (major Omp) of Haemophilus (H.) paragallinarum, to the 38 kDa major Omp of P.gallinarum, to the 39 kDa major Omp of P.volantium and to the 38.5 kDa major Omp of P. avium in immunoblotting studies. Comparison of N-terminal amino acid sequences also confirmed the relationship between the major Omps of most of the members of the family Pasteurellaceae.
一种针对多杀性巴氏杆菌(P. multocida)35 kDa外膜蛋白(一种假定的孔蛋白)制备的多克隆抗体,在免疫印迹研究中显示与副鸡嗜血杆菌(H. paragallinarum)的36 kDa主要外膜蛋白(主要Omp)、鸡巴氏杆菌(P.gallinarum)的38 kDa主要Omp、鸡新城疫杆菌(P.volantium)的39 kDa主要Omp以及鸟巴氏杆菌(P. avium)的38.5 kDa主要Omp发生结合。N端氨基酸序列的比较也证实了巴氏杆菌科大多数成员的主要Omp之间的关系。