The solute selectivity of porin pores of Escherichia coli and Salmonella typhimurium.
The solute selectivity of porin pores of Escherichia coli and Salmonella typhimurium was examined using vesicle membranes reconstituted from phospholipids and purified porin trimers. OmpE- and 34K-porin-pores allowed a preferential diffusion of phosphorylated and/or negatively charged compounds. They allowed the diffusion of positively charged solutes reasonably well. OmpF- and 35K-porin-pores favored the diffusion of positively charged solutes a little more than negatively charged solutes. OmpC- and 36K-porin-pores showed poor diffusibility to all solute tested. B-porins from E. coli B formed highly efficient pores for the diffusion of both positively and negatively charged solutes. On the basis of these observations, possible mechanisms of solute selectivity were discussed.
D002462:Cell Membrane / Q000378:metabolism / Q000648:ultrastructure; D004926:Escherichia coli / Q000378:metabolism / Q000648:ultrastructure*; D007473:Ion Channels / Q000378:metabolism / Q000648:ultrastructure*; D008565:Membrane Proteins / Q000378:metabolism*; D008970:Molecular Weight; D010539:Permeability; D018272:Porins; D012486:Salmonella typhimurium / Q000378:metabolism / Q000648:ultrastructure*; D013045:Species Specificity; D013329:Structure-Activity Relationship
D007473:Ion Channels; D008565:Membrane Proteins; D018272:Porins