Subcellular Distribution of Rat Liver NADPH-2, 4-Dienoyl-CoA Reductase

The subcellular distribution of 2, 4-dienoyl-CoA reductase (EC. 1.3.1.34, DCR) in rat liver was studied biochemically and immunochemically after the induction of clofibrate. DCR activity was mainly detected in the mitochondrial fraction by sucrose density gradient centrifugation in the livers of bot...

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Published inBiological & pharmaceutical bulletin Vol. 19; no. 2; pp. 176 - 181
Main Authors MIZUGAKI, Michinao, HIROSE, Akihiko, SUZUKI, Hideaki, MIURA, Koichi, EDO, Kiyoto, TOMIOKA, Yoshihisa
Format Journal Article
LanguageEnglish
Published Tokyo The Pharmaceutical Society of Japan 1996
Maruzen
Japan Science and Technology Agency
Subjects
2, 4-dienoyl-CoA reductase
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Blotting, Western
Enzymes and enzyme inhibitors
Fatty Acid Desaturases - immunology
Fatty Acid Desaturases - metabolism
Fundamental and applied biological sciences. Psychology
Liver - enzymology
Male
Microbodies - enzymology
Mitochondria, Liver - enzymology
mitochondrial enzyme
Oxidoreductases
Oxidoreductases Acting on CH-CH Group Donors
peroxisomal enzyme
Precipitin Tests
rat liver
Rats
Rats, Wistar
unsaturated fatty acid
β-oxidation
Rat
Enzyme
Liver
Rodentia
Vertebrata
Mitochondria
Mammalia
Animal
Distribution
Peroxisome
Oxidoreductases
Intracellular
2,4-Dienoyl-CoA reductase (NADPH)
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Summary:The subcellular distribution of 2, 4-dienoyl-CoA reductase (EC. 1.3.1.34, DCR) in rat liver was studied biochemically and immunochemically after the induction of clofibrate. DCR activity was mainly detected in the mitochondrial fraction by sucrose density gradient centrifugation in the livers of both normal and clofibrate-treated rats. It was also shown that the polyclonal antibody against purified DCR detected the enzyme in the mitochondrial fraction. However, the antibodies, which were affinity purified using the purified mitochondrial DCR or were epitope-selected using the fusion-polypeptide expressed from the mitochondrial cDNA clone (λgt11-RDR181), were cross-reacted with the peroxisomal DCR. These results suggest that peroxisomal DCR is immunochemically indistinguishable from mitochondrial DCR.
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ISSN:0918-6158
1347-5215
DOI:10.1248/bpb.19.176