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Regulation of lactate dehydrogenase activity: Reversible and isoenzyme-specific inhibition of the tetramerization process by peptides

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Summary

The transition of inactive lactic dehydrogenase (LDH) subunits to functional tetramers is controlled by 2 naturally-occurring peptides. One of these peptides inhibits the folding/association/activation process of H-LDH and the other peptide, the reconstitution of M-LDH. NADH and NAD+ are isoenzyme-specific antagonists of the 2 inhibitory peptides.

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Author notes

  1. G. A. Schoenenberger

    Present address: Research Division, Department of Surgery and Research Department, Kantonsspital Basel, Hebelstrasse 20, CH-4031, Basel, Switzerland

Authors and Affiliations

  1. Research Division, Department of Surgery and Research Department, Kantonsspital Basel, Hebelstrasse 20, CH-4031, Basel, Switzerland

    H. Döbeli

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  1. H. Döbeli
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  2. G. A. Schoenenberger
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Döbeli, H., Schoenenberger, G.A. Regulation of lactate dehydrogenase activity: Reversible and isoenzyme-specific inhibition of the tetramerization process by peptides. Experientia 39, 281–282 (1983). https://doi.org/10.1007/BF01955304

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  • DOI: https://doi.org/10.1007/BF01955304

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