[Reconstitution of high-affinity galactose transport of Salmonella typhimurium in proteoliposomes: energization by lipoamide and NAD or by the membrane potential; inhibition by ATP].

The binding protein-dependent galactose transport of Salmonella typhimurium has been reconstituted in proteoliposomes made from a partially purified protein fraction (containing the three membrane protein implicated in this transport and a lipoamide dehydrogenase activity) and soybean phospholipids. The reconstitution of galactose transport requires the addition of the purified galactose binding protein. Transport is energized either by reduced lipoamide and NAD or by the membrane potential and is inhibited by ATP.