Purification and properties of L(+)-lactate dehydrogenase from potato tubers.
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.
D000255:Adenosine Triphosphate / Q000494:pharmacology; D003956:Dialysis; D006863:Hydrogen-Ion Concentration; D007770:L-Lactate Dehydrogenase / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000494:pharmacology; D009243:NAD; D009249:NADP; D010944:Plants / Q000201:enzymology*; D011773:Pyruvates; D013053:Spectrophotometry; D014675:Vegetables
D011773:Pyruvates; D009243:NAD; D009249:NADP; D000255:Adenosine Triphosphate; D007770:L-Lactate Dehydrogenase