Interaction of acetyl-CoA fragments with rat liver acetyl-CoA carboxylase
نویسندگان
چکیده
منابع مشابه
Plant acetyl-CoA carboxylase.
medium containing [” Plphosphate, the distribution of 32P-labelled acetyl-CoA carboxylase in the fractions can be investigated and it has been found that a greater proportion of the phosphorylated enzyme is present in the polymeric form after exposure of the intact tissue to insulin. Present studies are concerned with investigating whether this polymeric active form is phosphorylated to a great...
متن کاملRegulation of acetyl-coA carboxylase: properties of coA activation of acetyl-coA carboxylase.
Acetyl-CoA carboxylase [acetyl-CoA:carbon-dioxide ligase (ADP-forming), EC 6.4.1.2] is activated by physiological concentrations of CoA. The CoA concentration dependency of this activation is sigmoidal; below 60 microM there is little or no activation, but the activation observed between 60 and 120 microM indicates that small changes in the concentration of CoA can cause significant changes in ...
متن کاملRegulation of purified rat liver acetyl CoA carboxylase by phosphorylation.
Acetyl CoA carboxylase was purified from liver of fasted-refed rats to near homogeneity, based on electrophoretic analysis and biotin content. These preparations contained an endogenous protein kinase that catalyzed the transfer of radioactive phosphate from [gamma-32P]ATP to acetyl CoA carboxylase, accompanied by a decrease in acetyl CoA carboxylase activity. Phosphate incorporated into acetyl...
متن کاملInhibition of rat liver acetyl CoA carboxylase by chloride.
The activity of acetyl CoA carboxylase in both crude and purified rat liver preparations was reduced in the presence of sodium or potassium chloride and increased in the presence of potassium acetate. The chloride inhibition was not competitive with bicarbonate. The use of Trischloride buffer did not alter the apparent pH optimum of the enzyme when compared with Tris-acetate buffer.
متن کاملHeat activation of rat liver acetyl-CoA carboxylase in vitro.
Acetyl-CoA carboxylase in rat liver homogenates was activated in vitro in a time- and temperature-dependent manner. The activity of acetyl-CoA carboxylase in rat liver preparations was determined in a 1-min assay to preclude the possibility of citrate activation of the enzyme during the assay period. Activation of the enzyme occurred more rapidly in liver preparations continuously maintained at...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1990
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1990.tb19345.x