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proshow_branch 9.0 proshow_version 9.0 proshow_os 9.0 proshow.ini [...] . Binding was rapid (t 1/2 less than 15 s) and specific and was inhibited by the presence of unlabeled carboxyfluorescein and cyclic AMP, but not by dinitrophenol, 4-acetamido-4'-isothiocyanostilbene-2,2'-disulfonic acid, or tryptophan. The apparent dissociation constant for the bound CF-mitochondria complex was about 500 microM. Mitochondrial hydrophobic binding sites were identified using the fluorescent probe 1-anilinonaphtalene-8-sulfonate (ANS). These sites were also capable of binding CF, and the complexes formed were readily dissociated by treatment with unlabeled CF. ANS-mitochondria complexes were also dissociated by treatment with an anionic detergent such as deoxycholate. Thus, the CF-mitochondria complex was not composed of a hydrophobic membrane protein such as cytochrome c. It was further determined that the CF-mitochondria complexes were composed of a large number of individual binding sites. Scatchard plots of the binding data for the CF-mitochondria complex
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