caa a22 4500 397557507 CHVBK 20180308164807.0 cr unu---uuuuu 161202e199604 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021307 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021307 Two Mitochondrial 3-Hydroxyacyl-CoA Dehydrogenases in Bovine Liver [Elektronische Daten] [Akio Kobayashi, Ling Ling Jiang, Takashi Hashimoto] 3-Hydroxyacyl-CoA dehydrogenase catalyzes the third reaction of fatty acid β-oxidation spiral. There are three enzymes catalyzing the 3-hydroxyacyl-CoA dehydrogenase reaction: mitochondrial monofunctional 3-hydroxyacly-CoA dehydrogenase, mitochondrial enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase tri-functional protein, and peroxisomal enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase bifunctional protein. The presence of isozymes of monofunctional 3-hydroxyacyl-CoA dehydrogenase was not known. In the present study, two monofunctional mitochondrial 3-hydroxyacyl-CoA dehydrogenases were purified from bovine liver. Type I enzyme was composed of two identical subunits with molecular mass of 35 kDa, and type II enzyme was a homotetramer of a 28 kDa polypeptide. In respect to the molecular structures, immunochemical properties, and carbon chain length specificities of acyl-CoA substrates, type I enzyme was the same as the well-known classical enzyme purified from various tissues, but type II enzyme was concluded to be a new enzyme. Type I enzyme was ubiquitous, but type II enzyme was rich in bovine and sheep, of several animal livers so far examined. © by the Journal of Biochemistry Regular Papers nationallicence bovine nationallicence 3-hydroxyacyl-CoA dehydrogenase nationallicence isozyme nationallicence mitochondria nationallicence Kobayashi Akio Department of Biochemistry, Shinshu University School of Medicine, 3-1-1 Asahi, Matsumoto, Nagano 390 aut Jiang Ling Ling 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 119/4(1996-04), 775-782 0021-924X 119:4<775 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021307 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021307 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Kobayashi Akio Department of Biochemistry, Shinshu University School of Medicine, 3-1-1 Asahi, Matsumoto, Nagano 390 aut 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- 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 119/4(1996-04), 775-782 0021-924X 119:4<775 1996 119 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