Abstract
Oxidation of citrate was markedly depressed in homogenates of kidneys from rats treated with fluoroacetate, but oxidation of other substrates of the Krebs cycle, including cis-aconitate, was depressed only to a relatively small extent. No inhibition of aconitase was found when cis-aconitate was the substrate. Evidently its conversion to citrate was relatively unaffected under conditions which strongly inhibited the reverse reaction.

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