Mathes A, Engelhardt H
Max-Planck-Institut für Biochemie, Abteilung Molekulare Strukturbiologie, Martinsried, Germany.
Biophys J. 1998 Sep;75(3):1255-62. doi: 10.1016/S0006-3495(98)74045-7.
The open channel characteristics of the bacterial porin Omp32 from Comamonas acidovorans were investigated by means of conductance measurements in planar lipid bilayers of the Montal-Mueller type. Particularly at low salt conditions (< or = 30 mM KCl) Omp32 exhibited some unusual asymmetric and nonlinear functional properties. Current-voltage relationship measurements showed that conductance depends on the orientation of porin molecules and is a nonlinear function of the applied membrane potential. Conductance also depends on the salt concentration in a manner not common to porins and the salt concentration modulates the nonlinearity of conductance-voltage relationships. Omp32 is strongly anion-selective. The nonlinear and asymmetric conductance of the open channel is a new observation in porins.
通过在蒙塔尔-米勒型平面脂质双层中进行电导测量,研究了嗜酸丛毛单胞菌的细菌孔蛋白Omp32的开放通道特性。特别是在低盐条件下(≤30 mM KCl),Omp32表现出一些不寻常的不对称和非线性功能特性。电流-电压关系测量表明,电导取决于孔蛋白分子的取向,并且是施加膜电位的非线性函数。电导还以一种孔蛋白不常见的方式依赖于盐浓度,并且盐浓度调节电导-电压关系的非线性。Omp32具有很强的阴离子选择性。开放通道的非线性和不对称电导是孔蛋白中的一个新发现。