Evidence against protein-induced 'internal pressure' in biological membranes. Partition of 8-anilinonaphthalene-1-sulphonate into Triton X-100 micelles and submitochondrial particles.
It has recently been proposed that although small amphiphilic molecules partition into phospholipid vesicles this partition is reduced by a factor of 10(3)-10(4)-fold by the presence of proteins in biological membranes [Conrad & Singer (1979) Proc. Natl. Acad. Sci. U.S.A.76, 5202-5206 and (1981) Biochemistry20, 808-818]. However, the affinity with which 8-anilinonaphthalene-1-sulphonate partitions into, or binds to, Triton X-100 micelles and submitochondrial particles is very similar and therefore does not support this proposal.
D000817:Anilino Naphthalenesulfonates / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D003902:Detergents; D005456:Fluorescent Dyes / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D008823:Micelles; D008928:Mitochondria / Q000378:metabolism*; D008954:Models, Biological; D017830:Octoxynol; D011092:Polyethylene Glycols; D011312:Pressure; D013367:Submitochondrial Particles / Q000378:metabolism*
D000817:Anilino Naphthalenesulfonates; D003902:Detergents; D005456:Fluorescent Dyes; D008565:Membrane Proteins; D008823:Micelles; D011092:Polyethylene Glycols; C027132:1-anilino-8-naphthalenesulfonate; D017830:Octoxynol