PEROXISOMAL BETA-OXIDATION SYSTEM OF RAT-LIVER - COPURIFICATION OF ENOYL-COA HYDRATASE AND 3-HYDROXYACYL-COA DEHYDROGENASE

Activity of enoyl-CoA hydratase in rat liver was elevated about 6-fold by the administration of di-(2-ethylhexyl)phthalate, a hepatic peroxisome proliferator. Almost all of the increased activity was the peroxisomal enzyme, which was distinguished by its heat-lability from mitochondrial one. Heat-labile enoyl-CoA hydratase was copurified with peroxisomal 3-hydroxyacyl-CoA dehydrogenase. The purified enzyme corresponded to a peroxisome specific peptide with a molecular weight of 80,000. © 1979.