Hydrodynamic properties of porin isolated from outer membranes of rat liver mitochondria.
The hydrodynamic properties of purified porin (Mr = 30 000), isolated from outer membranes of rat liver mitochondria has been studied. After gel filtration, active porin was eluted in a symmetrical peak with an estimated Stokes radius of 5.4 nm. The sedimentation coefficient (s) and partial specific volume (v) were found to be 2.6 S and 0.908 cm3/g, respectively, for the purified porin-Triton X-100 complex. Based on these determinations, a molecular weight of 170 000 for the porin-Triton X-100 complex was calculated. Correcting for bound Triton X-100, 1.8 g/g of protein, a molecular weight of 60 000 was estimated for the protein portion of the complex. Thus, isolated active porin appears to exist as a dimer.
D000818:Animals; D002850:Chromatography, Gel; D007425:Intracellular Membranes / Q000032:analysis*; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000302:isolation & purification* / Q000378:metabolism; D008930:Mitochondria, Liver / Q000032:analysis*; D008970:Molecular Weight; D017830:Octoxynol; D011092:Polyethylene Glycols / Q000378:metabolism; D018272:Porins; D051381:Rats
D046911:Macromolecular Substances; D008565:Membrane Proteins; D018272:Porins; D011092:Polyethylene Glycols; D017830:Octoxynol