Abstract
Clofibrate treatment caused a 2-3-fold increase in rat liver aldehyde dehydrogenase activity. The induced enzyme has a high Km for acetaldehyde and was found to be located in mitochondrial peroxisomes and microsomes. Disruption of the purified peroxisomes by different treatments with subsequent centrifugation of subpe-roxisomal components in a sucrose density gradient indicates that aldehyde dehydrogenase is located in the peroxisomal membrane. Partial purification of clofibrate-induced aldehyde dehydrogenases from microsomes and peroxisomes was undertaken. The enzymes are active with several aliphatic and aromatic aldehydes less formaldehyde and glyceraldehyde. According to its basic kinetic properties peroxisomal aldehyde dehydrogenase seems to be similar to a clofibrate-induced microsomal enzyme. The functional role of both enzymes in the liver cells is discussed.
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Antonenkov, V.D., Pirozhkov, S.V., Panchenko, L.F. (1987). Aldehyde Dehydrogenase in Mammalian Peroxisomes. In: Fahimi, H.D., Sies, H. (eds) Peroxisomes in Biology and Medicine. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71325-5_24
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DOI: https://doi.org/10.1007/978-3-642-71325-5_24
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