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. 1972 Oct;129(4):831–839. doi: 10.1042/bj1290831

Purification and properties of l(+)-lactate dehydrogenase from potato tubers

D D Davies 1, S Davies 1
PMCID: PMC1174228  PMID: 4144124

Abstract

1. A purification of l(+)-lactate dehydrogenase is described. 2. The final preparation is active with NADH and NADPH and with a number of keto acids, but evidence is presented to support the view that a single enzyme is involved. 3. NAD+ showed product inhibition, but at slightly acid pH values there was evidence of co-operative binding. 4. At acid pH values ATP was a potent inhibitor and appears to be an allosteric effector. At neutral or alkaline pH values ATP behaved as a weak competitive inhibitor. 5. The physiological significance of inhibition by ATP is discussed.

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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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