[Physico-chemical properties of specific protein kinases during intensification of lipogenesis and treatment with nicotinic acid].
Protein kinase strong-associated with acetyl-CoA-carboxylase is isolated from the liver of chicken and 300-fold purified with alimentary intensification of lipogenesis and under the effect of nicotinic acid against this background. The obtained enzymes are studied comparatively. It is found that their preparations are phosphorylated with different rate, have two pH optima and differ in the sensitivity to cAMP and to thermostable protein inhibitor. The hydrophobic chromatography was used to separate components of the acetyl-CoA-carboxylase-protein kinase complex and to reveal in the chicken liver cAMP-dependent and cAMP-independent protein kinases highly specific to acetyl-CoA-carboxylase and strongly bound with it.
Khustochka
L N
LN
Khalmuradov
A G
AG
Fomenko
A I
AI
D000103:Acetyl-CoA Carboxylase / Q000378:metabolism; D000818:Animals; D002645:Chickens; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D000242:Cyclic AMP / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008055:Lipids / Q000096:biosynthesis*; D008099:Liver / Q000201:enzymology*; D009525:Niacin / Q000494:pharmacology*; D047428:Protein Kinase Inhibitors; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism*; D013379:Substrate Specificity
D008055:Lipids; D047428:Protein Kinase Inhibitors; D009525:Niacin; D000242:Cyclic AMP; D011494:Protein Kinases; D000103:Acetyl-CoA Carboxylase
Fiziko-khimicheskie svoĭstva spetsificheskikh proteinkinaz pri intensifikatsii lipogeneza i deĭstvii nikotinovoĭ kisloty.