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. 1972 Oct;129(4):831-9.
doi: 10.1042/bj1290831.

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

D D Davies, S Davies

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

D D Davies et al. Biochem J. 1972 Oct.

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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