Development of Liver Mitochondrial Aldehyde Dehydrogenase Activities in the Foetal and Neonatal Rat

  • Alan A. Horton
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 126)


Changes in the activities of a number of enzymes in the mammalian liver during foetal and postnatal development appear to reflect the different physiological needs of the developing animal faced with environmental alteration (Greengard, 1971). A study of the developmental histories of a number of enzymes in the mammalian liver has resulted in the emergence of two important features. One is that the activities of most enzymes studied do not increase steadily over a prolonged period but increase within hours or days to the activity seen in the adult. Secondly, the emergence of new enzymes or the upsurge of enzymes present at low activities is not evenly distributed along the age axis but occurs in clusters. In rat liver three eventful periods have been discerned (Greengard, 1971). One occurs in late foetal life, another on the first day after birth and another in the third postnatal week.


Alcohol Dehydrogenase Aldehyde Dehydrogenase Barbituric Acid Postnatal Development Mammalian Liver 
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  1. Chappell, J.B. and Hansford, R.G. (1972) in Subcellular Components: Preparations and Fractionation (Birnie, G.D. and Fox, S.M. eds.) 2nd edition, pp 77–91, Butterworths, LondonGoogle Scholar
  2. de Duve, C., Pressman, B.C., Gianetto, R., Wattiaux, R. and Appelmans, F. (1955) Biochem. J. 60, 604–617Google Scholar
  3. Greengard, O. (1971) in Essays in Biochemistry (Campbell, P.N. and Dickens, F.) vol 7, pp 159–205, Academic Press, London and New YorkGoogle Scholar
  4. Hallman, M. (1971) Biochim. Biophys. Acta 253, 360–372PubMedCrossRefGoogle Scholar
  5. Horton, A.A. and Barrett, M.C. (1975) Arch. Biochem. Biophys. 167, 426–436PubMedCrossRefGoogle Scholar
  6. Koivula, T. and Koivusalo, M. (1975) Biochim. Biophys. Acta 397, 9–23PubMedCrossRefGoogle Scholar
  7. Lowry, O.H., Rosebrough, N.J., Farr, A.L. and Randall, R.J. (1951) J. Biol. Chem. 193, 265–275PubMedGoogle Scholar
  8. Marjanen, L. (1972) Biochem. J. 127, 635–639Google Scholar
  9. Nakazawa, T., Asami, K., Suzuki, H. and Yukawa, O. (1973) J. Biochem. 73, 397–406PubMedGoogle Scholar
  10. Pollak, J.K. (1975) Biochem. J. 150, 477–488PubMedGoogle Scholar
  11. Raiha, N.C.R., Koskinen, M. and Pikkarainen, P. (1967) Biochem. J. 103, 623–626PubMedGoogle Scholar
  12. Tottmar, S.O.C., Pettersson, H. and Kiessling, K.H. (1973) Biochem. J. 135, 577–586PubMedGoogle Scholar

Copyright information

© Plenum Press, New York 1980

Authors and Affiliations

  • Alan A. Horton
    • 1
  1. 1.Department of BiochemistryUniversity of BirminghamBirmingham B15 2TTEngland

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