Open AccessCharacterization and Isolation of Enzymes that Hydrolyze Short‐Chain acyl‐CoA in Rat‐Liver Mitochondria
Author(s) -
Svensson L. Thomas,
Kilpeläinen Seppo H.,
Hiltunen J. Kalervo,
Alexson Stefan E. H.
Publication year - 1996
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1996.0526u.x
Subject(s) - biochemistry , enzyme , mitochondrion , acyl coa , cytosol , immunoprecipitation , molecular mass , peroxisome , chemistry , phthalate , biology , gene , organic chemistry
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.