Abstract
An inhibitor of cholesterol synthesis (ICS) was extracted from the mitochondria of starved rats' liver, and purified by dialysis, tryptic digestion, precipitation at pH 3.0 and Sephadex column chromatography. This preparation was inhibitory to cholesterol synthesis and produced one protein band in acrylamide disc electrophoresis.
The acid precipitate consisted of 68% protein and produced a 20-fold increase in in vitro inhibition compared to the original ICS. Inhibition by ICS was also demonstrated in vivo.
