Biochemical, Immunological, and Molecular Characterization of a “High KM” Aldehyde Dehydrogenase

  • Rolf Eckey
  • Rüdiger Timmann
  • John Hempel
  • Dharam P. Agarwal
  • H. Werner Goedde
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 284)


Aldehyde dehydrogenase (ALDH), the enzyme mainly responsible for the oxidation of acetaldehyde and other aliphatic and aromatic aldehydes, plays an important role in the toxic consequences of a deranged acetaldehyde metabolism in alcohol-related disorders (Agarwal and Goedde, 1989, 1990; Goedde and Agarwal, 1989). Two broadly defined groups of ALDHs have been recognized based upon their Michaelis constants (“low Km” and “high Km” isozymes). The mammalian liver ALDHs differ in their electrophoretic mobility, isoelectric point, molecular size, kinetic properties, inhibition with disulfiram, subunit structure, as well as in their cellular and tissue distribution, and chromosomal assignment.


Aldehyde Dehydrogenase Aldehyde Substrate Mitochondrial Aldehyde Dehydrogenase ALDH Isozyme Human Aldehyde Dehydrogenase 
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Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Rolf Eckey
    • 1
  • Rüdiger Timmann
    • 1
  • John Hempel
    • 2
  • Dharam P. Agarwal
    • 1
  • H. Werner Goedde
    • 1
  1. 1.Institute of Human GeneticsUniversity of HamburgHamburgGermany
  2. 2.Department of Microbiology, Biochemistry and Molecular BiologyUniversity of Pittsburgh Medical SchoolPittsburghUSA

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