Abstract

1. 1. The electron transport particle (ETP) has been fractionated with a mixture of cholate and ammonium sulfate. A particulate fraction has been obtained (DPNH-DC-SDC) which catalyzes the oxidation of both DPNH and succinate by cytochrome c. At a higher concentration of ammonium sulfate, another particulate fraction (SDC) has been obtained which is active only with succinate. 2. 2. DPNH-DC-SDC contains cytochromes b and c 1 (but not c or cytochrome oxidase) in the molecular ratio 1:8:1.0. The enzyme bound hemoproteins are reduced to the same degree by either succinate or DPNH. 65% of the total cytochrome b is reducible by substrate whereas 80% of the total cytochrome c 1 is reducible by substrate. 3. 3. In aged preparations, the rates of reduction of cytochromes b, c 1 and of externally added c by DPNH are greatly decreased and the extent of reduction of cytochrome b is diminished. The reducibility of the hemes by succinate is less labile.

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