Cytosolic malate dehydrogenase in muscle extracts of Toxocara canis

1. Malate dehydrogenase (L-malic acid:NAD+ oxydoreductase, EC 1.1.1.37) was partially purified from muscle extracts of Toxocara canis by means of gel chromatography in Sephadex G-150 and affinity chromatography in Sepharose-4B-Blue dextran. 2. The purified enzyme was very active in reducing oxalacetate and less active in oxidizing L-malate. It was inhibited by excess oxalacetate but not by L-malate. 3. The kinetic parameters of the enzyme were obtained and these included: pH and temperature optima and apparent Michaelis constants for the substrates. 4. The results suggest that the enzyme from Toxocara canis behaves like the enzyme of the model helminth Ascaris lumbricoides.