Ludwig O, De Pinto V, Palmieri F, Benz R
Biochim Biophys Acta. 1986 Aug 21;860(2):268-76. doi: 10.1016/0005-2736(86)90523-7.
The porin of the outer membrane of rat-brain mitochondria was isolated and purified. The protein showed a single band of apparent Mr 35,500 on dodecyl sulfate-containing polyacrylamide gels. The incorporation of rat-brain porin into artificial lipid bilayer membranes showed that it is able to form pores with an average single-channel conductance of 400 pS in 0.1 M KCI. The pores were found to be voltage-dependent and switched to substrates at higher transmembrane potentials. The voltage-dependence of the rat brain pore was considerably smaller than that of the other known eukaryotic porins. The possible role of the rat-brain porin in the regulation of transport process across the outer mitochondrial membrane is discussed.
大鼠脑线粒体外膜孔蛋白被分离和纯化。该蛋白在含十二烷基硫酸钠的聚丙烯酰胺凝胶上呈现出一条表观分子量为35,500的单带。将大鼠脑孔蛋白整合到人工脂质双分子层膜中表明,它能够在0.1 M KCl中形成平均单通道电导为400 pS的孔。发现这些孔是电压依赖性的,并且在较高的跨膜电位下转变为底物。大鼠脑孔的电压依赖性明显小于其他已知的真核孔蛋白。讨论了大鼠脑孔蛋白在外线粒体膜跨膜运输过程调节中的可能作用。