Primary structure of chicken liver acetyl-CoA carboxylase deduced from cDNA sequence.
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چکیده
منابع مشابه
Primary structure of chicken liver acetyl-CoA carboxylase deduced from cDNA sequence.
The complete amino acid sequence of acetyl-CoA carboxylase from chicken liver has been deduced by cloning and sequence analysis of DNA complementary to its messenger RNA. The results were confirmed by Edman degradation of peptide fragments obtained by digestion of the enzyme polypeptide with Achromobacter proteinase I or staphylococcal serine proteinase. Chicken liver acetyl-CoA carboxylase is ...
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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 ...
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Recent investigations in this laboratory have shownl 2 that the isocitrate(or citrate-) activated form of liver acetyl CoA carboxylase (E.C. 6.4.1.2) is a large protein structure having a molecular weight of about four million. Electron microscopic examination of the carboxylase in the presence of isocitrate reveals' that it has a filamentous structure with dimensions of SG-100 A by up to 5000 ...
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.
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1988
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)69116-1