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Aldehyde Dehydrogenase in Mammalian Peroxisomes

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Peroxisomes in Biology and Medicine

Part of the book series: Proceedings in Life Sciences ((LIFE SCIENCES))

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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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References

  1. Lindros, K.O. (1978) Ins Research advances in alcohol and drug problems, Vol. 4, Plenum Press, New York, USA, pp. 111–176.

    Google Scholar 

  2. Pietruszko, R. (1983) In: Isozymes; current topics in biological and medical research, Vol. 8, Alan R. Liss Inc., New York, USA, pp. 195–217.

    Google Scholar 

  3. Holmes, R.S., Duley, J.A., Algar, E.MC, Mather, P.B., and Rout, U.K. (1986) Alcohol Alcoholism, 21, 41–56.

    CAS  Google Scholar 

  4. Deitrich, R.A., Bludeau, Pc, Stock, T., and Roper, M0 (1977) J. Biol. Chem., 252, 6169–6176.

    PubMed  CAS  Google Scholar 

  5. Lindahl, R., and Evces, So (1984) Jo Biol. Chem., 259, 11991–11996.

    CAS  Google Scholar 

  6. Jones, G.LC, and Teng, Y.-S0 (1983) Biochim. Biophys. Acta, 745, 162–174.

    Google Scholar 

  7. Ikawa, M., Impraim, C.C., Wang, G., and Yoshida, A. (1983) J. Biol. Chem., 258, 6282–6287.

    Google Scholar 

  8. Forte-McRobbie, C.M., and Pietruszko, R. (1985) Alcohol, 2, 375–381.

    Article  PubMed  CAS  Google Scholar 

  9. Lamboeuf, Y., and De Saint Blanquat, G. (1980) Arch. Into Pharmacodyn., 243, 17–26.

    CAS  Google Scholar 

  10. Panchenko, L.F., Pirozhkov, S.V., and Antonenkov, V.D. (1982) Bull. Exp. Biol. Med., 44, 52–58 (in Russian).

    Google Scholar 

  11. Panchenko, L.F., Pirozhkov, S.Y., and Antonenkov, V.D. (1985) Biochem. Pharmacol., 34, 471–479.

    Article  PubMed  CAS  Google Scholar 

  12. Antonenkov, V.D., Pirozhkov, S.V., and Panchenko, LCF. (1985) Eur. Jo Biochem., 149, 159–167.

    Article  CAS  Google Scholar 

  13. Kramer, R., and Kremser, K. (1984) Enzyme, 31, 17–20.

    Google Scholar 

  14. Nakayasu, H., Mihara, K., and Sato, R. (1978) Biochem. Biophys. Res. Commune, 83, 697–703.

    Google Scholar 

  15. Reddy, J.K., Warren, J.R., Reddy, M.D., and Lalwani, N.D. (1982) Ann. N.I. Acad. Sci., 386, 81–111.

    Google Scholar 

  16. Smith, H.E., and Lindahl, R. (1980) Pharmacol. Biochem. Behavior, 13, suppl. 1, 111–118.

    Article  Google Scholar 

  17. Lazarow, P.B., and de Duve, C. (1976) Proc. Natl. Acado Sci. USA, 73, 2043–2046.

    Google Scholar 

  18. Chance, B., Sies, H., and Boveris, A (1979) Physiol. Rev., 59, 527–605c

    PubMed  CAS  Google Scholar 

  19. Hollta, E. (1977) Biochemistry, 16, 91–100.

    Article  Google Scholar 

  20. Benedetti, A., Comporti, M., and Esterbauer, H. (1980) Biochim. Biophys. Acta, 620, 281–2960

    Google Scholar 

  21. Poli, G., Dianzani, M.U., Cheeseman, K.H., Slater, T.F., Lang, J., and Esterbauer, Hc (1985) Biochem. J., 227, 629–638.

    PubMed  CAS  Google Scholar 

  22. Hjelle, J.J., Grubbs, J.H. and Petersen, D.R. (1982) Toxicol. Lett., 14, 35–43.

    Article  PubMed  CAS  Google Scholar 

  23. Cadenas, E., Muller, A., Brigelius, R., Esterbauer, H., and Sies, H. (1983) Biochem0 Jo, 214, 479–487.

    CAS  Google Scholar 

  24. Benedetti, A., Pulceri, R., Ferrari, M., Ciccoli, L., Esterbauer, Ho, and Comporti, M. (1982) Biochem. Biophys. Acta, 712, 628–638.

    Google Scholar 

  25. Benedetti, A., Comporti, M., and Esterbauer, H. (1980) Biochim. Biophys. Acta, 620, 281–296.

    PubMed  CAS  Google Scholar 

  26. Tamburini, P.P., Masson, H.A., Bains, A.K., Makowski, R.J., Morris, B., and Gibson, G.G. (1984) Eur. J. Biochem., 139, 235–246

    Article  PubMed  CAS  Google Scholar 

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© 1987 Springer-Verlag Berlin Heidelberg

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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

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-71327-9

  • Online ISBN: 978-3-642-71325-5

  • eBook Packages: Springer Book Archive

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