[Citrate influence on acetyl-CoA-carboxylase activation and phosphorylation in chicken liver with lipogenesis inhibited by nicotinic acid].

Nicotinic acid in vivo affects the citrate demand for acetyl-CoA-carboxylase activation in the chicken liver under conditions of alimentary lipogenesis stimulation. Stoichiometry of the citrate binding with the dissociation constant of the enzyme-allosteric activator complex is determined under experimental conditions. Endogenic phosphorylation of acetyl-CoA-carboxylase completely correlates with its inactivation and depends on the citrate level. cAMP is established to have an activating effect on phosphorylation of acetyl-CoA-carboxylase of test animals.