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Updated: Aug 8, 2026

Mapping Metabolism: Monitoring Lactate Dehydrogenase Activity Directly in Tissue
Published on: June 21, 2018
Metabolite-modulated complex formation between alpha-glycerophosphate dehydrogenase and lactate dehydrogenase
H Yong1, G A Thomas, W L Peticolas
1Department of Chemistry, University of Oregon, Eugene 97403.
Abstract:
A modified Hummel-Dreyer equilibrium chromatography technique was used to test the hypothesis that NADH induces the molecular association of lactate dehydrogenase (LDH) and alpha-glycerol-3-phosphate dehydrogenase (alpha-GDH). In the presence of a very limited NADH concentration, a unique elution profile with a new peak running immediately ahead of a trough at the free alpha-GDH elution position is obtained. The appearance of this peak-trough profile is physical evidence that reversible association between LDH and alpha-GDH occurs over a very limited range of free NADH concentrations. The association constant for this complex formation between LDH and alpha-GDH is estimated to be 2.0 microM-1. With the NADH concentration increased to saturation level, no evidence of binding is observed. Such concentration-dependent behavior suggests that the strong competition between LDH and alpha-GDH for the limited amount of NADH tends to promote the enzyme-enzyme contact in order to make the most efficient use of the shared metabolite. The experimental results described in this article make a convincing argument for a metabolite-modulated enzyme-enzyme interaction along this metabolic pathway.
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