Abstract
1. 1.|The reversibility of citrate synthesis and the effects of citrate and fluorocitrate on citrate synthesis in whole mitochondria have been investigated. 2. 2.|Cleavage of citrate to oxaloacetate (trapped as malate) and acetyl-CoA (trapped as acetylcarnitine) in whole liver mitochondria can be demonstrated. The maximum rate of this reversed reaction is at most 1 40 of the maximum rate of citrate synthesis. 3. 3.|Citrate and fluorocitrate are competitive inhibitors with respect to oxaloacetate of purified pig heart synthase. The K i for both compounds was found to be approx. 1.5 mM. 4. 4.|Both citrate and fluorocitrate inhibit citrate synthesis and increase ketogenesis in whole liver mitochondria. They probably act as competitive inhibitors with respect to oxaloacetate, since malate counteracts this inhibition. 5. 5.|For kinetic reasons it is concluded that the citrate synthesis reaction probably never approaches equilibrium in the intact tissue. The importance of citrate in the regulation of citrate and ketone body formation in the liver is discussed.
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