Abstract
1. Cytoplasmic malate dehydrogenase (cMDH) was purified 200-fold. 2. Disc gel electrophoresis showed a single major band of activity of cMDH. 3. MDH in crude cytoplasmic extract was less sensitive to Cd2+ than purified cytoplasmic MDH. 4. Purified cMDH had a Km of 0.14 mM OAA. 5. Concentrations of Cd2+ of 0.312 mM significantly inhibited the cMDH. 6. The inhibition by Cd2+ was completely reversed by 1.54 and partly reversed by 0.56 mM 2-mercaptoethanol. 7. The inhibition by Cd2+ was non-competitive. Calculated Ki values are below those reported for Cd2+-imidazole and Cd2+-cysteine interactions, but above those reported for other Cd2+-thiol group interactions.
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