SUMMARY: NADP-dependent isocitrate dehydrogenase (EC from ATCC 354 was purified to homogeneity by ammonium sulphate fractionation, followed by DEAE cellulose and Sephadex G-200 chromatography. The pH optimum of the enzyme was 8·5. The values for isocitrate and NADP were 74 and 53 μ, respectively. Mn was essential for enzyme activity. The enzyme lost all activity on incubation at 70°C for 15 min; isocitrate and NADP protected against this thermal inactivation. -Chloromercuribenzoate inhibited the enzyme; pre-incubation of enzyme with isocitrate + Mn prevented this inhibition. The purified enzyme showed concerted inhibition by glyoxylate + oxaloacetate and was inhibited by oxalomalate.


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