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

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Enzymology and Molecular Biology of Carbonyl Metabolism 3

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 284))

Abstract

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.

This work will be a part of the MD thesis of Rüdiger Timmann to be submitted to the Faculty of Medicine, University of Hamburg.

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Author information

Authors and Affiliations

  1. Institute of Human Genetics, University of Hamburg, Hamburg, Germany

    Rolf Eckey, Rüdiger Timmann, Dharam P. Agarwal & H. Werner Goedde

  2. Department of Microbiology, Biochemistry and Molecular Biology, University of Pittsburgh Medical School, Pittsburgh, PA, 15261, USA

    John Hempel

Authors
  1. Rolf Eckey
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  2. Rüdiger Timmann
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  3. John Hempel
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  4. Dharam P. Agarwal
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  5. H. Werner Goedde
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Editor information

Editors and Affiliations

  1. Department of Biochemistry, Purdue University, West Lafayette, Indiana, 47907, USA

    Henry Weiner

  2. Chemisches Zentrallabor, Inselspital, Bern, CH 3010, Switzerland

    Bendicht Wermuth

  3. Indiana University School of Medicine and Veterans Administration Medical Center, Indianapolis, Indiana, 46202, USA

    David W. Crabb

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© 1990 Plenum Press, New York

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Eckey, R., Timmann, R., Hempel, J., Agarwal, D.P., Goedde, H.W. (1990). Biochemical, Immunological, and Molecular Characterization of a “High KM” Aldehyde Dehydrogenase. In: Weiner, H., Wermuth, B., Crabb, D.W. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 3. Advances in Experimental Medicine and Biology, vol 284. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5901-2_6

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  • DOI: https://doi.org/10.1007/978-1-4684-5901-2_6

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-5903-6

  • Online ISBN: 978-1-4684-5901-2

  • eBook Packages: Springer Book Archive

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