Purification and properties of L(+)-lactate dehydrogenase from potato tubers.
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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.
SUBMITTER: Davies DD
PROVIDER: S-EPMC1174228 | biostudies-other | 1972 Oct
REPOSITORIES: biostudies-other
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