Abstract
THE isolated, purified isozymes of lactate dehydrogenase (LDH) differ from one another in a variety of ways. In addition to electrophoretic mobility and immunological reactivity1, they differ in kinetic behaviour2, thermal stability3,4, sub-unit composition5, and inhibition by lactate6, pyruvate7, urea8, oxalate9, and α-hydroxybutyrate10. This communication describes the finding that the dissimilarity between LDH 1 and LDH 5 in degree of inhibition by lactate can appreciably be reduced by small alterations in pH. This dependence of substrate inhibition on pH illustrates the need to explore other variables before generalizing from limited in vitro to complex in vivo conditions.
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VESELL, E. pH Dependence of Lactate Dehydrogenase Isozyme Inhibition by Substrate. Nature 210, 421–422 (1966). https://doi.org/10.1038/210421a0
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DOI: https://doi.org/10.1038/210421a0
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