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X-Ray Studies of Horse Liver Alcohol Dehydrogenase

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Pyridine Nucleotide-Dependent Dehydrogenases

Abstract

Horse liver alcohol dehydrogenase (LADH) catalyses the oxidation of alcohol to aldehyde when in the presence of the co-factor nicotinamide adenine dinucleotide. It is one of the many NAD-dependent dehydrogenases which are composed of two or four subunits each of molecular weight between 35.000 and 40.000. Of these a low resolution X-ray study has been reported for lactate dehydrogenase (l) and preliminary X-ray data for glyceraldehyde-3-phosphate dehydrogenase (2), soluble malate dehydrogenase (3) and liver alcohol dehydrogenase(4).

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References

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Authors and Affiliations

  1. Department of Chemistry, College of Agriculture, Uppsala 7, Sweden

    C.-I. Brändén, E. Zeppezauer, T. Boiwe, G. Söderlund, B.-O. Söderberg & B. Nordström

Authors
  1. C.-I. Brändén
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  2. E. Zeppezauer
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  3. T. Boiwe
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  4. G. Söderlund
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  5. B.-O. Söderberg
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  6. B. Nordström
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Editor information

Editors and Affiliations

  1. Fachbereich Biologie, University of Konstanz, Konstanz, Germany

    Horst Sund

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© 1970 Springer-Verlag Berlin · Heidelberg

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Brändén, CI., Zeppezauer, E., Boiwe, T., Söderlund, G., Söderberg, BO., Nordström, B. (1970). X-Ray Studies of Horse Liver Alcohol Dehydrogenase. In: Sund, H. (eds) Pyridine Nucleotide-Dependent Dehydrogenases. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-49974-6_11

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  • DOI: https://doi.org/10.1007/978-3-642-49974-6_11

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-49976-0

  • Online ISBN: 978-3-642-49974-6

  • eBook Packages: Springer Book Archive

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