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Porcine hepatocyte organelles were separated by isopycnic sucrose gradient centrifugation from livers of 6-month-oId Yorkshire pigs. The presence of a peroxisomal palmityl-CoA oxidizing system and a peroxisomal NAD:aldehyde dehydrogenase (ALDH) with high for acetaldehyde was demonstrated. Peroxisomal palmitate oxidizing capacity was found to be equal to that of the surviving mitochondria. The high isozyme of ALDH was located mainly in the mitochondria (54%), with a significant portion in the peroxisome. Remaining activity was distributed among the microsomes (8.3%) and cytosol (4.6%). The low isozyme was confined almost exclusively to the mitochondria. ALDH may exist in the peroxisome as a detoxification mechanism and contribute to shorter half-lives of reactive aldehydes in the cell. Species differences are discussed.

Effects of clofibric acid on porcine hepatocytes: a new model for the study of peroxisomal metabolism