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. 1965 Feb;94(2):384–389. doi: 10.1042/bj0940384

Organ specificity and lactate-dehydrogenase activity. Differential inhibition by urea and related compounds

Wendy A Withycombe 1, D T Plummer 1,*, J H Wilkinson 1
PMCID: PMC1206520  PMID: 14348198

Abstract

1. The effect of urea on the lactate-dehydrogenase activities of human-heart and -liver tissue extracts and on crystalline ox-heart and rabbit-muscle enzyme have been determined. Similar studies on electrophoretically separated isoenzyme fractions have shown an inverse relationship between sensitivity to urea inhibition and electrophoretic mobility. 2. With pyruvate as substrate a sharp change in the nature of the inhibition of tissue lactate dehydrogenase with increasing concentrations of urea occurs at 1 m or 4 m with the electrophoretically slow and fast isoenzymes respectively. 3. At concentrations of urea less than 1 m, inhibition of the purified enzymes is competitive with respect to pyruvate and 2-oxobutyrate. 4. Similar studies have been carried out with methylurea and hydantoic acid, both of which are more potent inhibitors than urea.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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