Abstract
The inhibitory activity of an aqueous extract of liver mitochondria (I.C.S.) was observed with Triton-treated rats. Fractionation of I.C.S. on Sephadex indicated that the active principle comes off the Sephadex with the protein fraction. Inhibitory activity was shown to be present in the 100,000 × g supernate of the liver homogenate of a starved rat, indicating that the active principle moves from the mitochondrion to the surrounding cytoplasm.Electrodialysis of the mitochondrial extract revealed that the inhibitor is permeable and moves to the cathode. The electrodialyzed material was found to be active as an inhibitor of cholesterol synthesis in vitro and in vivo.It is concluded that the active principle is associated with protein and may be separated therefrom by electrodialysis.

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