Simple and unique purification by size-exclusion chromatography for an oligomeric enzyme, rat liver cytosolic acetyl-coenzyme A hydrolase

2003 ◽  
Vol 790 (1-2) ◽  
pp. 239-244 ◽  
Author(s):  
Naoya Suematsu ◽  
Kazuki Okamoto ◽  
Fumihide Isohashi
Keyword(s):  
Size Exclusion Chromatography ◽  
Rat Liver ◽  
Coenzyme A ◽  
Size Exclusion ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Exclusion Chromatography

Acetyl-coenzyme A carboxylase mRNA metabolism in the rat liver

Metabolism ◽  
1992 ◽  
Vol 41 (2) ◽  
pp. 201-207 ◽  
Author(s):  
Fernando López-Casillas ◽  
M.Verónica Ponce-Castañeda ◽  
Ki-Han Kim
Keyword(s):  
Rat Liver ◽  
Coenzyme A ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Mrna Metabolism ◽  
Acetyl Coenzyme A Carboxylase

Effects of nucleotides on a cold labile acetyl-coenzyme A hydrolase from the supernatant fraction of rat liver

Biochemistry ◽  
1983 ◽  
Vol 22 (3) ◽  
pp. 584-590 ◽  
Author(s):  
Fumihide Isohashi ◽  
Yoko Nakanishi ◽  
Yukiya Sakamoto
Keyword(s):  
Rat Liver ◽  
Coenzyme A ◽  
Supernatant Fraction ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme

scholarly journals Acetyl-coenzyme A deacylase activity in liver is not an artifact. Subcellular distribution and substrate specificity of acetyl-coenzyme A deacylase activities in rat liver

1979 ◽  
Vol 177 (1) ◽  
pp. 71-79 ◽  
Author(s):  
Klaus-P. Grigat ◽  
Klaus Koppe ◽  
Claus-D. Seufert ◽  
Hans-D Söling
Keyword(s):  
Rat Liver ◽  
Coenzyme A ◽  
Liver Mitochondria ◽  
Acid Oxidation ◽  
Matrix Space ◽  
Acetyl Coa ◽  
Acetyl Coenzyme A ◽  
Lysosomal Fraction ◽  
Total Enzyme Activity ◽  
Acetyl Coenzyme

Whole liver and isolated liver mitochondria are able to release free acetate, especially under conditions of increased fatty acid oxidation. In the present paper it is shown that rat liver contains acetyl-CoA deacylase (EC 3.1.2.1) activity (0.72μmol/min per g wet wt. of liver at 30°C and 0.5mm-acetyl-CoA). At 0.5mm-acetyl-CoA 73% of total enzyme activity was found in the mitochondria, 8% in the lysosomal fraction and 19% in the postmicrosomal supernatant. Mitochondrial subfractionation shows that mitochondrial acetyl-CoA deacylase activity is restricted to the matrix space. Mitochondrial acetyl-CoA deacylase showed almost no activity with either butyryl- or hexanoyl-CoA. Acetyl-CoA hydrolase activity from purified rat liver lysosomes exhibited a very low affinity for acetyl-CoA (apparent Km>15mm compared with an apparent Km value of 0.5mm for the mitochondrial enzyme) and reacted at about the same rate with acetyl-, n-butyryl- and hexanoyl-CoA. We could not confirm the findings of Costa & Snoswell [(1975) Biochem. J.152, 167–172] according to which mitochondrial acetyl-CoA deacylase was considered to be an artifact resulting from the combined actions of acetyl-CoA–l-carnitine acetyltransferase (EC 2.3.1.7) and acetylcarnitine hydrolase. The results are in line with the concept that free acetate released by the liver under physiological conditions stems from the intramitochondrial deacylation of acetyl-CoA.

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