Abstract
1. 1. The inhibition of H4-isozyme of lactate dehydrogenase (H4-LDH) by oxalate and oxamate was studied in 0.5 M sodium chloride. At 20 C. oxalate inhibition was a mixed type and at 40 C, the inhibition was uncompetitive. 2. 2. Oxamate inhibition was shown as two different types. The inhibition was non-competitive at low pyruvate concentrations and competitive at high pyruvate concentrations. Inhibition type did not differ as temperature changed. 3. 3. The inhibition mechanism is proposed on the basis of quaternary enzyme complex with two kinds of pyruvate as reported previously. The distribution of ternary and quaternary enzyme complexes may determine the inhibition type.
Published Version
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