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Effect of Oxalate on the Activity of Lactate Dehydrogenase Isoenzymes

Nature volume 202, pages 1337–1338 (1964)Cite this article

Abstract

ELECTROPHORETICALLY separated lactate dehydrogenase isoenzymes differ from each other in several respects, including immunochemical specificity1,2, substrate affinities3,4 ability to utilize coenzyme analogues5, sensitivity to inhibitors6,7, thermal stability8 and substrate specificity9. Among the inhibitors which have been reported to exert different effects on the anodic and cathodic isoenzymes are sulphite, which preferentially inhibits the former6, and urea, which at certain concentrations inhibits the latter without much affecting the activity of the former10,11.

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Authors and Affiliations

  1. Department of Chemical Pathology, Westminster Medical School (University of London), London, S.W.1

    PAULINE M. EMERSON, J. H. WILKINSON & WENDY A. WITHYCOMBE

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  1. PAULINE M. EMERSON
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  2. J. H. WILKINSON
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  3. WENDY A. WITHYCOMBE
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EMERSON, P., WILKINSON, J. & WITHYCOMBE, W. Effect of Oxalate on the Activity of Lactate Dehydrogenase Isoenzymes. Nature 202, 1337–1338 (1964). https://doi.org/10.1038/2021337a0

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