Summary
The kinetic properties — apparentK m of pyruvate, pyruvate inhibition pattern, and maximal velocity — of M4 (skeletal muscle) lactate dehydrogenases of marine elasmobranch fishes resemble those of the homologous lactate dehydrogenases of non-elasmobranchs only when physiological concentrations of urea (approximately 400 mM) are present in the assay medium. Urea increases the apparentK m of pyruvate to values typical of other vertebrates (Fig. 2), and reduces pyruvate inhibition to levels seen with other M4-lactate dehydrogenases (Fig. 3). Urea reduces the activation enthalpy of the reaction, and increasesV max at physiological temperatures (Fig. 4).
The M4-lactate dehydrogenase of the freshwater elasmobranch,Potamotrygon sp., resembles a teleost lactate dehydrogenase, i.e., although it is sensitive to urea, it does not require the presence of urea for the establishment of optimal kinetic properties.
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Yancey, P.H., Somero, G.N. Urea-requiring lactate dehydrogenases of marine elasmobranch fishes. J Comp Physiol B 125, 135–141 (1978). https://doi.org/10.1007/BF00686749
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DOI: https://doi.org/10.1007/BF00686749