Abstract
Treatment of rat liver mitochondria with the nonionic surfactant Brij 56 yields a non-sedimentable supernatant fraction containing over 60 percent of the original atractyloside-sensitive ADP(ATP) binding activity and a sedimentable (membrane) fraction showing atractyloside-insensitive ADP binding. The supernatant fraction exhibited no atractyloside-sensitive binding of AMP, GDP, or CDP. Atractyloside-sensitive binding of ADP was not inhibited by oligomycin, antimycin A, 2,4-dinitrophenol, or azide. The atractyloside-sensitivity of ADP binding was lost on heating. The properties of the non-sedimentable ADP (ATP) binding factor agree closely with those of the ADP-ATP translocase of the inner mitochondrial membrane.
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