Abstract
MITOCHONDRIAL malate dehydrogenase (MDH) isozymes are strongly inhibited by 10−3 molar oxalo-acetate, while under comparable conditions the cytoplasmic MDH shows no substrate inhibition1–5. This catalytic test readily distinguishes the two types of MDH isozymes2. Further refinement of catalytic discrimination between MDH isozymes was recently achieved by the determination of velocity ratios in presence of oxalo-acetate and its fluoro analogues4. The present communication describes the observation that catalytic activity of mitochondrial MDH is highly susceptible to relatively small changes in ionic strength (μ) as well as to the qualitative composition of ionic environment. On the other hand, the cytoplasmic isozyme is completely insensitive to these influences.
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KUN, E., EANES, R. & VOLFIN, P. Selective Modification of Mitochondrial Malate Dehydrogenase Activity by Changes in Ionic Strength. Nature 214, 1328–1330 (1967). https://doi.org/10.1038/2141328a0
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DOI: https://doi.org/10.1038/2141328a0
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