Abstract
Different ions affect the H 4 and M 4 isoenzymes of porcine lactate dehyrogenase ( l-lactate:NAD + oxidoreductase, EC 1.1.1.27) in the same way, inhibiting the enzyme at low pyruvate concentrations, whereas at high pyruvate concentrations, the activities were enhanced. The inhibition was competitive with regard to pyruvate and NADH. The enhancement of the enzyme activity at high pyruvate concentration is due to the increase in the K m value for pyruvate, implying that higher substrate concentrations are needed to obtain substrate inhibition. Sulphate behaved differently from the other ions. It inhibited in a noncompetitive manner with regard to pyruvate and did not activate the enzyme at high pyruvate concentration. The effect of ions increased with the size of the anion. The ionic strength was of less importance.
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