Letter | Published:

Lactic Dehydrogenase and Cytochrome

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



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.

Access optionsAccess options

Rent or Buy article

Get time limited or full article access on ReadCube.


All prices are NET prices.


  1. 1.

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

Download references

Author information


  1. Biochemical Laboratory, Cambridge. Feb. 22.

    •  & L. G. ZERFAS


  1. Search for MALCOLM DIXON in:

  2. Search for L. G. ZERFAS in:

About this article

Publication history




Further reading


By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.