Characterization and Isolation of Enzymes that Hydrolyze Short-Chain acyl-CoA in Rat-Liver Mitochondria
| Autor: | J. Kalervo Hiltunen, Stefan E.H. Alexson, L. Thomas Svensson, Seppo H. Kilpeläinen |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Male
Mitochondria Liver Mitochondrion Biology Cell Fractionation Acetyl-CoA Hydrolase Biochemistry Substrate Specificity Rats Sprague-Dawley Animals chemistry.chemical_classification Acyl-CoA hydrolase Chromatography Molecular mass Hydrolysis Acetyl-CoA hydrolase Metabolism Molecular biology Rats Molecular Weight Cytosol Durapatite Enzyme chemistry Chromatography Gel Ketone bodies Electrophoresis Polyacrylamide Gel Acyl Coenzyme A |
| Zdroj: | European Journal of Biochemistry. 239:526-531 |
| ISSN: | 1432-1033 0014-2956 |
| Popis: | In this study we investigated the presence of short-chain acyl-CoA hydrolases in rat liver mitochondria. One acetyl-CoA-hydrolyzing enzyme with a molecular mass of about 48 kDa was purified to apparent homogeneity as judged by SDS/PAGE. Immunoprecipitation experiments with antibodies raised to the purified protein showed that this enzyme corresponds to a minor portion of the total mitochondrial acetyl-CoA hydrolase activity, most (about 90%) of the total activity being due to an enzyme which was labile and required Triton X-100 for its stability. Neither of these acetyl-CoA-hydrolyzing enzymes appeared to be induced by treatment of rats with di(2-ethylhexyl)phthalate, a peroxisome proliferator which mediates induction of several cytosolic and mitochondrial long-chain acyl-CoA thioesterases. In addition, an enzyme that hydrolyzed acetoacetyl-CoA was partially purified; it was induced about 3.5-fold by di(2-ethylhexyl)phthalate treatment. In conclusion, these results demonstrate that rat liver mitochondria contain several enzymes capable of hydrolyzing short-chain acyl-CoA, indicating that regulation of the metabolism of short-chain acyl-CoAs and formation of ketone bodies, could be complex. |
| Databáze: | OpenAIRE |
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