151. Subcellular distribution of rat liver NADPH-2,4-dienoyl-CoA reductase
- Author
-
Hideaki Suzuki, Akihiko Hirose, Michinao Mizugaki, Yoshihisa Tomioka, Koichi Miura, and Kiyoto Edo
- Subjects
Fatty Acid Desaturases ,Male ,Oxidoreductases Acting on CH-CH Group Donors ,Blotting, Western ,Pharmaceutical Science ,2,4 Dienoyl-CoA reductase ,Mitochondria, Liver ,Reductase ,Mitochondrion ,Microbodies ,medicine ,Animals ,Rats, Wistar ,Unsaturated fatty acid ,Pharmacology ,chemistry.chemical_classification ,Clofibrate ,biology ,General Medicine ,Peroxisome ,Molecular biology ,Precipitin Tests ,eye diseases ,Rats ,Enzyme ,Biochemistry ,chemistry ,Liver ,Polyclonal antibodies ,biology.protein ,sense organs ,medicine.drug - Abstract
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 (lambda gt11-RDR181), were cross-reacted with the peroxisomal DCR. These results suggest that peroxisomal DCR is immunochemically indistinguishable from mitochondrial DCR.
- Published
- 1996