Abstract
The kinetic properties of lactate dehydrogenase (LDH) (EC 1.1.1.27) from spinach leaves were studied in order to evaluate the possible roles of LDH in the production of oxalate. LDH was purified by affinity chromatography on affigel blue and oxamate agarose columns. The pH optimum for the reduction of pyruvate was 7.25, while that for the reduction of glyoxylate was 7. The rate of reduction of glyoxylate at the optimum pH indicated substrate inhibition at concentrations above 8 and 40 mM, respectively. The maximum activity of LDH with pyruvate was about three times greater than with glyoxylate. The pH optimum for the oxidation of lactate was 9, with very low activity below pH 8. Substrate inhibition was apparent at lactate concentrations above 10 mM. LDH was inactive with glyoxylate in the oxidative reaction, which would lead to the biosynthesis of oxalate.
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