Abstract
Porcine hepatocyte organelles were separated by isopycnic sucrose gradient centrifugation from livers of 6-month-old Yorkshire pigs. The presence of a peroxisomal palmitoyl-CoA oxidizing system and a peroxisomal NAD:aldehyde dehydrogenase (ALDH) with high K m for acetaldehyde was demonstrated. Peroxisomal palmitate oxidizing capacity was found to be equal to that of the surviving mitochondria. The high K m isozyme of ALDH was mainly located in the mitochondria (54%), with a significant portion in the peroxisome (32%). Remaining activity is distributed among the microsomes (8.3%) and cytosol (4.6%). The low K m 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.
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call