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Glyoxylate as a Substrate for Lactate Dehydrogenase

Nature volume 213, pages 726–727 (1967)Cite this article

Abstract

IF 2-oxobutyrate is substituted for pyruvate as substrate for lactate dehydrogenase (LD), it is found to be more readily reduced by the electrophoretically faster moving LD isoenzymes than by the slower moving LD isoenzymes1,2. Because glyoxylate may also serve as a substrate for LD (ref. 3), we investigated the effect of LD isoenzyme fractions on this compound and compared the findings with those obtained with pyruvate and 2-oxobutyrate.

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Authors and Affiliations

  1. St. Mary's Hospital, London, W.C.2

    M. R. BANNER & S. B. ROSALKI

Authors
  1. M. R. BANNER
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  2. S. B. ROSALKI
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BANNER, M., ROSALKI, S. Glyoxylate as a Substrate for Lactate Dehydrogenase. Nature 213, 726–727 (1967). https://doi.org/10.1038/213726a0

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