A kinetic analysis of the changes in fluorescence on the interaction of 8-anilinonaphthalene-1-sulphonate with submitochondrial particles.
A comparison of the fluorescence change on the addition of 8-anilinonaphthalene-1-sulphonate to succinate-energized submitochondrial particles with that on the addition of succinate to submitochondrial particles incubated with 8-anilinonaphthalene-1-sulphonate shows that these changes in fluorescence may be explained solely in terms of 8-anilinonaphthalene-1-sulphonate binding. This comparison does not support the proposal of an 8-anilinonaphthalene-1-sulphonate-monitored change in the conformation of submitochondrial-particle membranes [Brocklehurst, Freedman, Hancock & Radda (1970) Biochem. J.116, 721-731]. The biphasic nature of the decrease in fluorescence, which was found to follow the addition of uncoupler to submitochondrial particles incubated with ATP or succinate, or of antimycin A to submitochondrial particles incubated with succinate, does not support the existence of 'aplectic' and 'symplectic' states of the mitochondrial membrane [Barrett-Bee & Radda (1972) Biochim, Biophys. Acta 267, 211-215].
D000096:Acetone / Q000031:analogs & derivatives / Q000494:pharmacology; D000255:Adenosine Triphosphate / Q000494:pharmacology; D000817:Anilino Naphthalenesulfonates / Q000378:metabolism*; D000818:Animals; D000968:Antimycin A / Q000494:pharmacology; D001665:Binding Sites / Q000187:drug effects; D002463:Cell Membrane Permeability; D005453:Fluorescence; D006845:Hydrocarbons, Fluorinated / Q000494:pharmacology; D007700:Kinetics; D008931:Mitochondria, Muscle / Q000378:metabolism*; D013386:Succinates / Q000494:pharmacology; D014634:Valinomycin / Q000494:pharmacology
D000817:Anilino Naphthalenesulfonates; D006845:Hydrocarbons, Fluorinated; D013386:Succinates; D000096:Acetone; D014634:Valinomycin; D000968:Antimycin A; D000255:Adenosine Triphosphate