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[Role of pyruvate dehydrogenase and ATP-citrate (pro-3S)lyase in inhibition of the biosynthesis of fatty acids by nicotinic acid].

The pyruvate dehydrogenase and ATP-citrate(pro-3S)lyase activity in the liver after administration of nicotinic acid to chickens against a background of stimulated lypogenesis is shown to increase in the period of maximum fall of the acetyl-CoA-carboxylase activity. Affinity of ATP-citrate (pro-3S)-lyase to citrate at this time is lowered, the content of citrate and isocitrate is elevated and CoASac is decreased to some extent. A conclusion is made on the absence of substrate limitation of acetyl-CoA-carboxylase with administration of nicotinic acid to chickens under conditions of the fatty acid biosynthesis intensification.