Kennell W L, Egli C, Hancock R E, Holt S C
Department of Periodontics, University of Texas Health Science Center-San Antonio 78284-7894.
Infect Immun. 1992 Feb;60(2):380-4. doi: 10.1128/iai.60.2.380-384.1992.
Three major outer membrane proteins with apparent molecular masses of 43, 45, and 51 kDa were purified from Wolinella recta ATCC 33238, and their pore-forming abilities were determined by the black lipid bilayer method. The non-heat-modifiable 45-kDa protein (Omp 45) showed no pore-forming activity even at high KCl concentrations. The single-channel conductances in 1 M KCl of the heat-modifiable proteins with apparent molecular masses of 43 kDa (Omp 43) and 51 kDa (Omp 51) were 0.49 and 0.60 nS, respectively. The proteins formed nonselective channels and, as determined by experiments of ion selectivity and zero-current potential, were weakly anion selective.
从直肠沃氏菌ATCC 33238中纯化出三种表观分子量分别为43、45和51 kDa的主要外膜蛋白，并通过黑脂质双层法测定它们的成孔能力。不可热修饰的45 kDa蛋白（Omp 45）即使在高KCl浓度下也没有成孔活性。表观分子量为43 kDa（Omp 43）和51 kDa（Omp 51）的可热修饰蛋白在1 M KCl中的单通道电导分别为0.49和0.60 nS。这些蛋白形成非选择性通道，并且通过离子选择性和零电流电位实验确定，它们对阴离子有较弱的选择性。
