Purification of the Primary Dihydroorotate Dehydrogenase (Oxidase) from Rat Liver Mitochondria

Abstract
Dihydroorotate dehydrogenase was purified to homogeneity from rat liver mitochondria by Triton X-100 solubilization, diethylaminoethyl cellulose chromatography and gel electrophoresis. The overall yield was 30 percent. The enzyme has a subunit molecular weight of 61, 000.