Glyoxylate as a Substrate for Lactate Dehydrogenase

descriptionPublicationkeyboard_double_arrow_right Article 01 Feb 1967 English Publisher:Springer Science and Business Media LLCJournal:Nature, volume 213, pages 726-727 (issn: 0028-0836, eissn: 1476-4687,

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Authors: M R, Banner; S B, Rosalki;

doi: 10.1038/213726a0

pmid: 6031790

Glyoxylate as a Substrate for Lactate Dehydrogenase

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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.

Related Organizations

St Mary's Hospital
United Kingdom
Imperial College Healthcare NHS Trust
United Kingdom
St Mary's Hospital
Canada

Keywords

Isoenzymes, Oxalates, L-Lactate Dehydrogenase, Swine, Animals, Glyoxylates, Urea, Rabbits, Pyruvates, Enzymes

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