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Pyridine Nucleotide-Dependent Dehydrogenases pp 413–438Cite as

Regulation of the Redox State of the Pyridine Nucleotides in Rat Liver

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Abstract

Cells contain many pyridine nucleotide-linked dehydrogenases, each of which, on isolation, is a self-contained system: given a substrate and the coenzyme these dehydrogenases catalyse a reaction in a manner which is predictable on the basis of the known kinetic properties. But though the behaviour of isolated dehydrogenases may be understandable and predictable, the details of their behaviour in the intact cell are not immediately understood. Why, for example, is lactate dehydrogenase in most animal tissues at equilibrium when the ratio [lactate]/[pyruvate] is approximately 10? The isolated enzyme can of course be at equilibrium with any [lactate]/[pyruvate] ratio provided that the ratio [NAD+]/[NADH] also varies. The analogous question can be asked for almost every other pyridine nucleotide-linked dehydrogenase.

This work was carried out in collaboration with D. H. Williamson, P. Lund, L. Raijman, L. V. Eggleston and K. Dalziel.

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Author information

Authors and Affiliations

  1. Metabolic Research Laboratory, Nuffield Department of Clinical Medicine, University of Oxford, England

    H. A. Krebs & R. L. Veech

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  1. H. A. Krebs
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  2. R. L. Veech
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Editors and Affiliations

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

    Horst Sund

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Krebs, H.A., Veech, R.L. (1970). Regulation of the Redox State of the Pyridine Nucleotides in Rat Liver. In: Sund, H. (eds) Pyridine Nucleotide-Dependent Dehydrogenases. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-49974-6_35

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  • DOI: https://doi.org/10.1007/978-3-642-49974-6_35

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  • Print ISBN: 978-3-642-49976-0

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