Abstract
During an investigation of the kinetic properties of the NAD-linked isocitrate dehydrogenase (NAD-IDH) of mitochondria derived from the thorax of Caliphora vomitora (a species of blowfly) it became apparent that this enzyme was inhibited by ATP and NADH2 and was activated by ADP, Mg2+, isocitrate and phosphate. A particularly striking feature was the dependence on phosphate. A plot of activity versus concentration resulted in a sigmoidal curve. At 5mM phosphate the enzyme produced 4–5% of its maximal activity and at 30mM 80%. Sacktor & Hurlbut (1966) have reported that at rest the phosphate content of whole blowfly thorax is 6.8μmoles/gm. wet wt. and in activity 7.5μmoles/gm.

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