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.
D000818:Animals; D003600:Cytosol / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008291:Malate Dehydrogenase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D009132:Muscles / Q000201:enzymology; D010071:Oxaloacetates / Q000378:metabolism; D013379:Substrate Specificity; D013696:Temperature; D014119:Toxocara / Q000201:enzymology*
D010071:Oxaloacetates; D008291:Malate Dehydrogenase