title: [Properties and biosynthesis of acetyl-CoA-carboxylase from chicken liver with administration of nicotinic acid during stimulation of lipogenesis].
abstract: Acetyl-CoA-carboxylase is isolated and purified to a homogeneous state from the chicken liver with alimentary lipogenesis stimulation. Under the action of nicotinic acid in vivo the specific enzyme activity is shown to decrease considerably followed by some variations in its properties. According to the results obtained during ultracentrifugation and PAAG electrophoresis nicotinic acid causes partial enzyme deaggregation with simultaneous increase of its phosphorylation. The latter is accompanied by a rise in the content of phosphate labile to alkali on acetyl-CoA-carboxylase subunits. Nicotinic acid in vivo has practically no effect on acetyl-CoA-carboxylase synthesis and decay rate. Its inhibiting action is induced by stimulation of enzyme phosphorylation.
authors.forename: S V
authors.initials: SV
authors.lastname: Pozharun
authors.forename: A G
authors.initials: AG
authors.lastname: Khalmuradov
authors.forename: A I
authors.initials: AI
authors.lastname: Fomenko
authors.forename: L N
authors.initials: LN
authors.lastname: Khustochka
authors.forename: S P
authors.initials: SP
authors.lastname: Stepanenko
mesh_terms: D000103:Acetyl-CoA Carboxylase / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002645:Chickens; D008025:Ligases / Q000378:metabolism*; D008055:Lipids / Q000096:biosynthesis*; D008099:Liver / Q000201:enzymology*; D009525:Niacin / Q000494:pharmacology*; D010766:Phosphorylation
chemical_list: D008055:Lipids; D009525:Niacin; D008025:Ligases; D000103:Acetyl-CoA Carboxylase
vernacular_title: Svoĭstva i biosintez atsetil-CoA-karboksilazy pecheni tsypliat pri vvedenii nikotinovoĭ kisloty na fone stimuliatsii lipogeneza.