Obara M, Nakae T
Department of Molecular Life Science, Tokai University School of Medicine, Isehara, Japan.
Biochem Biophys Res Commun. 1992 Jul 31;186(2):645-51. doi: 10.1016/0006-291x(92)90795-m.
Protein E1, a porin of the outer membrane of Pseudomonas aeruginosa, was reconstituted into planar lipid bilayers. Single channel conductance of the protein appeared to be 230 pS (pico siemens) in 1 M KCl-10 mM Hepes, pH7.2. This value is approximately 5 times lower than the conductance of the OmpF channel of Escherichia coli. Conductance increased linearly as the membrane potential was raised from -200 mV to +200 mV, and was nearly proportional to the KCl concentration. These results show that protein E1 is probably a genuine porin in the P. aeruginosa outer membrane supporting the earlier conclusion that protein E1 forms a small channel.
蛋白质E1是铜绿假单胞菌外膜的一种孔蛋白,被重组到平面脂质双分子层中。在1 M KCl - 10 mM Hepes(pH7.2)中,该蛋白的单通道电导似乎为230皮西门子(pS)。这个值大约比大肠杆菌OmpF通道的电导低5倍。当膜电位从 - 200 mV升高到 + 200 mV时,电导呈线性增加,并且几乎与KCl浓度成正比。这些结果表明,蛋白质E1可能是铜绿假单胞菌外膜中的一种真正的孔蛋白,支持了早期关于蛋白质E1形成小通道的结论。