caa a22 4500 397556454 CHVBK 20180308164803.0 cr unu---uuuuu 161202e199609 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021459 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021459 Purification and Properties of Rat D-3-Hydroxyacyl-CoA Dehydratase: D-3-Hydroxyacyl-CoA Dehydratase/D-3-Hydroxyacyl-CoA Dehydrogenase Bifunctional Protein [Elektronische Daten] [Ling Ling Jiang, Shoko Miyazawa, Takashi Hashimoto] We have previously purified two D-3-hydroxyacyl-CoA dehydratase preparations from human liver. One preparation contained a 77-kDa polypeptide and smaller polypeptides, and the other was a homodimer of a 46-kDa polypeptide. Three different purified rat peroxisomal D-3-hydroxyacyl-CoA dehydratase preparations have been reported. Therefore, rat enzyme was purified in this study to confirm the enzyme structure. Two preparations with similar molecular structures to the human enzyme preparations were obtained, and these were similar to each other in immunochemical and catalytic properties. It was suggested that the native enzyme was a homodimer of the 77-kDa polypeptide, and this enzyme was modified to a homodimer of the 46-kDa polypeptide, because conversion of the 77-kDa polypeptide to smaller polypeptides including the 46-kDa polypeptide was clearly observed during purification. Rat liver subcellular fractionation study indicates that this enzyme is located in peroxisomes. The enzyme preparation containing the 77-kDa polypeptide catalyzed the D-3-hydroxyacyl-CoA dehydrogenase reaction as well as the dehydratase reaction. Thus, it is proposed that this enzyme is D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence bifunctional protein nationallicence D-3-hydroxyacyl-CoA dehydratase nationallicence D-3-hydroxyacyl-CoA dehydrogenase nationallicence peroxisomal nationallicence rat enzyme nationallicence Jiang Ling Ling Department of Biochemistry, Shinshu University School of Medicine, 3-1-1 Asahi, Matsumoto, Nagano 390 aut Miyazawa Shoko Department of Biochemistry, Shinshu University School of Medicine, 3-1-1 Asahi, Matsumoto, Nagano 390 aut Hashimoto Takashi Department of Biochemistry, Shinshu University School of Medicine, 3-1-1 Asahi, Matsumoto, Nagano 390 aut The Journal of Biochemistry Oxford University Press 120/3(1996-09), 633-641 0021-924X 120:3<633 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021459 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021459 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Jiang Ling Ling Department of Biochemistry, Shinshu University School of Medicine, 3-1-1 Asahi, Matsumoto, Nagano 390 aut NATIONALLICENCE 700 1- Miyazawa Shoko Department of Biochemistry, Shinshu University School of Medicine, 3-1-1 Asahi, Matsumoto, Nagano 390 aut NATIONALLICENCE 700 1- Hashimoto Takashi Department of Biochemistry, Shinshu University School of Medicine, 3-1-1 Asahi, Matsumoto, Nagano 390 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/3(1996-09), 633-641 0021-924X 120:3<633 1996 120 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford