caa a22 4500 397556616 CHVBK 20180308164804.0 cr unu---uuuuu 161202e199609 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021458 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021458 Purification and Properties of Human D-3-Hydroxyacyl-CoA Dehydratase: Medium-Chain Enoyl-CoA Hydratase Is D-3-Hydroxyacyl-CoA Dehydratase [Elektronische Daten] [Ling Ling Jiang, Akio Kobayashi, Hitomi Matsuura, Hirofumi Fukushima, Takashi Hashimoto] Human medium-chain enoyl-CoA hydratase was purified from liver, because we noticed the presence of a high medium-chain enoyl-CoA hydratase activity in human skin fibroblasts catalyzed by an enzyme different from the known enzymes catalyzing the enoyl-CoA hydratase reaction. Two enzyme preparations were obtained. One of them, preparation I, consisted of 46-kDa polypeptide, and its molecular mass was estimated to be 86 kDa. The other, preparation n, consisted of a major 77-kDa polypeptide and minor smaller poly-peptides including 46-kDa polypeptide. The molecular mass of preparation II was 154 kDa. Both enzyme preparations catalyzed reversible dehydration of medium-chain D-3-hy-droxyacyl-CoA to 2-trans-enoyl-CoA, but did not react with L-3-hydroxyacyl-CoA. Catalytic properties and immunochemical reactivities of these enzyme preparations were nearly the same. The cross-reactive material to the antibody was confirmed to be in peroxisomes by immunohistochemical study of cultured human skin fibroblasts. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence enoyl-CoA hydratase nationallicence human enzyme nationallicence D-3-hydroxyacyl-CoA dehydratase nationallicence medium-chain nationallicence peroxisomal nationallicence Jiang Ling Ling Department of Biochemistry, Shinshu University School of Medicine 3-1-1 Asahi, Matsumoto, Nagano 390 aut Kobayashi Akio Department of Biochemistry, Shinshu University School of Medicine 3-1-1 Asahi, Matsumoto, Nagano 390 aut Matsuura Hitomi Department of Biochemistry, Shinshu University School of Medicine 3-1-1 Asahi, Matsumoto, Nagano 390 aut Fukushima Hirofumi Department of Legal Medicine, 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), 624-632 0021-924X 120:3<624 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021458 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021458 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- Kobayashi Akio Department of Biochemistry, Shinshu University School of Medicine 3-1-1 Asahi, Matsumoto, Nagano 390 aut NATIONALLICENCE 700 1- Matsuura Hitomi Department of Biochemistry, Shinshu University School of Medicine 3-1-1 Asahi, Matsumoto, Nagano 390 aut NATIONALLICENCE 700 1- Fukushima Hirofumi Department of Legal Medicine, 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), 624-632 0021-924X 120:3<624 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