Ludwig O, Krause J, Hay R, Benz R
Lehrstuhl für Biotechnologie, Universität Würzburg, Federal Republic of Germany.
Eur Biophys J. 1988;15(5):269-76. doi: 10.1007/BF00256477.
One of the major outer membrane proteins of yeast mitochondria was isolated and purified. It migrated as a single band with an apparent molecular weight of 30 kDa on a SDS-electrophoretogram. When reconstituted in lipid bilayer membranes the protein formed pores with a single channel conductance of 0.45 nS in 0.1 M KCl. The pores had the characteristics of general diffusion pores with an estimated diameter of 1.7 nm. The pore of mitochondrial outer membranes of yeast shared some similarities with the pores formed by mitochondrial and bacterial porins. The pores switched to substates at voltages higher than 20 mV. The possible role of this voltage-dependence in the metabolism of mitochondria is discussed.
酵母线粒体的一种主要外膜蛋白被分离和纯化。在SDS电泳图上，它迁移为一条单一的条带，表观分子量为30 kDa。当该蛋白重组到脂质双分子层膜中时，在0.1 M KCl中形成了单通道电导为0.45 nS的孔。这些孔具有一般扩散孔的特征，估计直径为1.7 nm。酵母线粒体外膜的孔与线粒体和细菌孔蛋白形成的孔有一些相似之处。在高于20 mV的电压下，这些孔会转变为亚状态。文中讨论了这种电压依赖性在线粒体代谢中的可能作用。
