Abstract
The inhibitor was prepared from hemolysates of acutely anemic rabbits. The stroma was spun down, and the inhibitor present in the supernatant could be stored at -20[degree]C for 2 weeks without loss of activity. The inhibitory effect was tested on heart succinoxidase. Phosphate was kept constant at 0.1 [image]. Inhibitions of up to 90% were observed. When the components of the succinoxidase system were tested separately, it was found that there was inhibition in all systems using succinate, including succinic dehydrogenase. Furthermore, DPNH-cytochrome c reductase was inhibited also, while DPNH[forward arrow]O2 oxidase was unaffected. It is postulated that the point at which the reaction chains from succinate and DPNH meet is sytochrome b, which is thought to be part of the succinic dehydrogenase enzyme complex, and that the inhibitor acts on cytochrome b.