Letter | Published:

Lactic Dehydrogenase and Cytochrome

Nature volume 143, page 557 (01 April 1939) | Download Citation

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Abstract

THE bulk of the respiration of most animal tissues, yeast, etc., takes place through the alternate oxidation and reduction of cytochrome. The reduction of cytochrome is mainly due (a) to a small group of dehydrogenases which are believed to reduce cytochrome directly, and (b) to flavoproteins which transport hydrogen from other dehydrogenases through coenzymes I and II. A typical dehydrogenase of the first class is the lactic dehydrogenase of yeast, which does not depend upon these coenzymes or flavoprotein, but which in the crude state reduces cytochrome c readily in the presence of lactate. Some months ago we observed that a partially purified preparation of this dehydrogenase failed to reduce cytochrome, though it still reduced other hydrogen acceptorslike methylene blue. We are at present engaged in the purification and isolation of this enzyme. We find that the purified enzyme still reduces methylene blue freely in the presence of lactate, but is completely inactive towards cytochrome. The following experiment shows this very clearly.

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References

  1. 1.

    , Biochem. Z., 298, 378 (1938).

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Affiliations

  1. Biochemical Laboratory, Cambridge. Feb. 22.

    • MALCOLM DIXON
    •  & L. G. ZERFAS

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DOI

https://doi.org/10.1038/143557a0

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