메뉴 건너뛰기




Volumn 120, Issue 3, 1996, Pages 633-641

Purification and properties of rat D-3-hydroxyacyl-CoA dehydratase: D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein

Author keywords

Bifunctional protein; D 3 hydroxyacyl CoA dehydratase; D 3 hydroxyacyl CoA dehydrogenase; Peroxisomal; Rat enzyme

Indexed keywords

ENOYL COENZYME A HYDRATASE; LIVER ENZYME;

EID: 0029771660     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021459     Document Type: Article
Times cited : (39)

References (27)
  • 1
    • 0029771659 scopus 로고    scopus 로고
    • Purification and properties of human D-3-hydroxyacyl-CoA dehydratase: Medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase
    • Jiang, L.L., Kobayashi, A., Matsuura, H., Fukushima, H., and Hashimoto, T. (1996) Purification and properties of human D-3-hydroxyacyl-CoA dehydratase: Medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase. J. Biochem. 120, 624-632
    • (1996) J. Biochem. , vol.120 , pp. 624-632
    • Jiang, L.L.1    Kobayashi, A.2    Matsuura, H.3    Fukushima, H.4    Hashimoto, T.5
  • 2
    • 0025181353 scopus 로고
    • D-3-Hydroxyacyl coenzyme A dehydratase from rat liver peroxisomes. Purification and characterization of a novel enzyme necessary for the epimerization of 3-hydroxyacyl-CoA thioesters
    • Li, J., Smeland, T.E., and Schulz, H. (1990) D-3-Hydroxyacyl coenzyme A dehydratase from rat liver peroxisomes. Purification and characterization of a novel enzyme necessary for the epimerization of 3-hydroxyacyl-CoA thioesters. J. Biol. Chem. 265, 13629-13634
    • (1990) J. Biol. Chem. , vol.265 , pp. 13629-13634
    • Li, J.1    Smeland, T.E.2    Schulz, H.3
  • 3
    • 0026793845 scopus 로고
    • Evidence that β-hydroxyacyl-CoA dehydrase purified from rat liver microsomes is of peroxisomal origin
    • Cook, L., Nagi, M.N., Suneja, S.K., Hand, A.R., and Cinti, D.L. (1992) Evidence that β-hydroxyacyl-CoA dehydrase purified from rat liver microsomes is of peroxisomal origin. Biochem. J. 287, 91-100
    • (1992) Biochem. J. , vol.287 , pp. 91-100
    • Cook, L.1    Nagi, M.N.2    Suneja, S.K.3    Hand, A.R.4    Cinti, D.L.5
  • 4
  • 5
    • 0019048796 scopus 로고
    • Purification and properties of mitochondrial and peroxisomal 3-hydroxyacyl-CoA dehydrogenase from rat liver
    • Osumi, T. and Hashimoto, T. (1980) Purification and properties of mitochondrial and peroxisomal 3-hydroxyacyl-CoA dehydrogenase from rat liver. Arch. Biochem. Biophys. 203, 372-383
    • (1980) Arch. Biochem. Biophys. , vol.203 , pp. 372-383
    • Osumi, T.1    Hashimoto, T.2
  • 6
    • 0029880653 scopus 로고    scopus 로고
    • Two mitochondrial 3-hydroxyacyl-CoA dehydrogenases in bovine liver
    • Kobayashi, A., Jiang, L.L., and Hashimoto, T. (1996) Two mitochondrial 3-hydroxyacyl-CoA dehydrogenases in bovine liver. J. Biochem. 119, 775-782
    • (1996) J. Biochem. , vol.119 , pp. 775-782
    • Kobayashi, A.1    Jiang, L.L.2    Hashimoto, T.3
  • 7
    • 77049229661 scopus 로고
    • Tissue fractionation studies. Intracellular distribution patterns of enzymes in rat liver tissue
    • de Duve, C., Pressman, B.C., Gianetto, R., Wattiaux, R., and Appelmans, F. (1955) Tissue fractionation studies. Intracellular distribution patterns of enzymes in rat liver tissue. Biochem. J. 60, 604-617
    • (1955) Biochem. J. , vol.60 , pp. 604-617
    • De Duve, C.1    Pressman, B.C.2    Gianetto, R.3    Wattiaux, R.4    Appelmans, F.5
  • 8
    • 0017815141 scopus 로고
    • Enhancement of fatty acyl-CoA oxidizing activity in rat liver peroxisomes by di-(2-ethylhexyl)phthalate
    • Osumi, T. and Hashimoto, T. (1978) Enhancement of fatty acyl-CoA oxidizing activity in rat liver peroxisomes by di-(2-ethylhexyl)phthalate. J. Biochem. 83, 1361-1365
    • (1978) J. Biochem. , vol.83 , pp. 1361-1365
    • Osumi, T.1    Hashimoto, T.2
  • 9
    • 0000024078 scopus 로고
    • Catalase
    • Bergmeyer, H.U., ed. Verlag Chemie, Weinheim
    • Aebi, H. (1974) Catalase in Methods of Enzymatic Analysis, 2nd ed. (Bergmeyer, H.U., ed.) Vol. 2, pp. 673-678, Verlag Chemie, Weinheim
    • (1974) Methods of Enzymatic Analysis, 2nd Ed. , vol.2 , pp. 673-678
    • Aebi, H.1
  • 10
    • 0001652288 scopus 로고
    • Glutamate dehydrogenase, UV-Assay
    • Bergmeyer, H.U., ed. Verlag Chemie, Weinheim
    • Schmidt, E. (1974) Glutamate dehydrogenase, UV-Assay in Methods of Enzymatic Analysis, 2nd ed. (Bergmeyer, H.U., ed.) Vol. 2, pp. 650-656, Verlag Chemie, Weinheim
    • (1974) Methods of Enzymatic Analysis, 2nd Ed. , vol.2 , pp. 650-656
    • Schmidt, E.1
  • 11
    • 77957003927 scopus 로고
    • The preparation and properties of microsomal TPNH-cytochrome c reductase from pig liver
    • Estabrook, R.W. and Pullman, M.E., eds. Academic Press, New York
    • Masters, B.S.S., Williams, C.H., Jr., and Kamin, H. (1967) The preparation and properties of microsomal TPNH-cytochrome c reductase from pig liver in Methods in Erizymology (Estabrook, R.W. and Pullman, M.E., eds.) Vol. 10, pp. 565-573, Academic Press, New York
    • (1967) Methods in Erizymology , vol.10 , pp. 565-573
    • Masters, B.S.S.1    Williams Jr., C.H.2    Kamin, H.3
  • 12
    • 0018178434 scopus 로고
    • A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples
    • Markwell, M.A.K., Haas, S.M., Bieber, L.L., and Tolbert, N.E. (1978) A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal. Biochem. 87, 206-210
    • (1978) Anal. Biochem. , vol.87 , pp. 206-210
    • Markwell, M.A.K.1    Haas, S.M.2    Bieber, L.L.3    Tolbert, N.E.4
  • 14
    • 0014949207 scopus 로고
    • Cleavageof structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavageof structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0009482260 scopus 로고
    • Electrophoretic transfer of protein from acrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T., and Gordon, J. (1979) Electrophoretic transfer of protein from acrylamide gels to nitrocellulose sheets: Procedure and some applications Proc. Natl. Acad. Sci. USA 76, 4350-4354
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 16
    • 0019076516 scopus 로고
    • Properties of mitochondrial and peroxisomal enoyl-CoA hydratases from rat liver
    • Furuta, S., Miyazawa, S., Osumi, T., Hashimoto, T., and Ui, N. (1980) Properties of mitochondrial and peroxisomal enoyl-CoA hydratases from rat liver. J. Biochem. 88, 1059-1070
    • (1980) J. Biochem. , vol.88 , pp. 1059-1070
    • Furuta, S.1    Miyazawa, S.2    Osumi, T.3    Hashimoto, T.4    Ui, N.5
  • 17
    • 0026515859 scopus 로고
    • Novel fatty acid β-oxidation enzymes in rat liver mitochondria. II. Purification and properties of enoyl-coenzyme A (CoA) hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein
    • Uchida, Y., Izai, K., Orii. T., and Hashimoto, T. (1992) Novel fatty acid β-oxidation enzymes in rat liver mitochondria. II. Purification and properties of enoyl-coenzyme A (CoA) hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein. J. Biol. Chem. 267, 1034-1041
    • (1992) J. Biol. Chem. , vol.267 , pp. 1034-1041
    • Uchida, Y.1    Izai, K.2    Orii, T.3    Hashimoto, T.4
  • 18
    • 0017613305 scopus 로고
    • Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis
    • Cleveland, D.W., Fischer, S.G., Kirschner, M.W., and Laemmli, U.K. (1977) Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. J. Biol. Chem. 252, 1102-1106
    • (1977) J. Biol. Chem. , vol.252 , pp. 1102-1106
    • Cleveland, D.W.1    Fischer, S.G.2    Kirschner, M.W.3    Laemmli, U.K.4
  • 19
    • 0018977041 scopus 로고
    • The presence of a new 3- oxoacyl-CoA thiolase in rat liver peroxisomes
    • Miyazawa, S., Osumi, T., and Hashimoto, T. (1980) The presence of a new 3- oxoacyl-CoA thiolase in rat liver peroxisomes. Eur. J. Biochem. 103, 589-596
    • (1980) Eur. J. Biochem. , vol.103 , pp. 589-596
    • Miyazawa, S.1    Osumi, T.2    Hashimoto, T.3
  • 20
    • 0024320081 scopus 로고
    • Epimerization of 3-hydroxyacyl-CoA esters in rat liver. Involvement of two 2-enoyl-CoA hydratases
    • Hiltunen, J.K., Palosaari, P.M., and Kunau, W.-H. (1989) Epimerization of 3-hydroxyacyl-CoA esters in rat liver. Involvement of two 2-enoyl-CoA hydratases. J. Biol. Chem. 264, 13536-13540
    • (1989) J. Biol. Chem. , vol.264 , pp. 13536-13540
    • Hiltunen, J.K.1    Palosaari, P.M.2    Kunau, W.-H.3
  • 21
    • 0026713679 scopus 로고
    • Peroxisomal multifunctional protein of Saccharomyces cerevisiae. Molecular analysis of the FOX2 gene and gene product
    • Hiltunen, J.K., Wenzel, B., Beyer, A., Erdmann, R., Fossa, A., and Kunau, W.-H. (1992) Peroxisomal multifunctional protein of Saccharomyces cerevisiae. Molecular analysis of the FOX2 gene and gene product. J. Biol. Chem. 267, 6646-6653
    • (1992) J. Biol. Chem. , vol.267 , pp. 6646-6653
    • Hiltunen, J.K.1    Wenzel, B.2    Beyer, A.3    Erdmann, R.4    Fossa, A.5    Kunau, W.-H.6
  • 22
    • 0001246916 scopus 로고
    • Beta-oxidation of unsaturated fatty acids: A revised pathway
    • Schulz, H. and Kunau, W.-H. (1987) Beta-oxidation of unsaturated fatty acids: A revised pathway. Trends Biochem. Sci. 12, 403-406
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 403-406
    • Schulz, H.1    Kunau, W.-H.2
  • 23
    • 0019028350 scopus 로고
    • Purification and properties of acyl-CoA oxidase from rat liver
    • Osumi, T., Hashimoto, T., and Ui, N. (1980) Purification and properties of acyl-CoA oxidase from rat liver. J. Biochem. 87, 1735-1746
    • (1980) J. Biochem. , vol.87 , pp. 1735-1746
    • Osumi, T.1    Hashimoto, T.2    Ui, N.3
  • 24
    • 0021797006 scopus 로고
    • Molecular cloning and nucleotide sequence of the cDNA for rat peroxisomal enoyl-CoA:hydratase-3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme
    • Osumi, T., Ishii, N., Hijikata, M., Kamijo, K., Ozasa, H., Furuta, S., Miyazawa, S., Kondo, K., Inoue, K., Kagamiyama, H., and Hashimoto, T. (1985) Molecular cloning and nucleotide sequence of the cDNA for rat peroxisomal enoyl-CoA:hydratase-3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme. J. Biol. Chem. 260, 8905-8910
    • (1985) J. Biol. Chem. , vol.260 , pp. 8905-8910
    • Osumi, T.1    Ishii, N.2    Hijikata, M.3    Kamijo, K.4    Ozasa, H.5    Furuta, S.6    Miyazawa, S.7    Kondo, K.8    Inoue, K.9    Kagamiyama, H.10    Hashimoto, T.11
  • 26
    • 0027426259 scopus 로고
    • Molecular cloning of the cDNAs for the subunits of rat mitochondrial fatty acid β-oxidation multienzyme complex. Structural and functional relationships to other mitochondrial and peroxisomal β-oxidation enzymes
    • Kamijo, T., Aoyama, T., Miyazaki, J., and Hashimoto, T. (1993) Molecular cloning of the cDNAs for the subunits of rat mitochondrial fatty acid β-oxidation multienzyme complex. Structural and functional relationships to other mitochondrial and peroxisomal β-oxidation enzymes. J. Biol. Chem. 268, 26452-26460
    • (1993) J. Biol. Chem. , vol.268 , pp. 26452-26460
    • Kamijo, T.1    Aoyama, T.2    Miyazaki, J.3    Hashimoto, T.4
  • 27
    • 0028223596 scopus 로고
    • Structural analysis of cDNAs for subunits of human mitochondrial fatty acid β-oxidation trifunctional protein
    • Kamijo, T., Aoyama, T., Komiyama, A., and Hashimoto, T. (1994) Structural analysis of cDNAs for subunits of human mitochondrial fatty acid β-oxidation trifunctional protein. Biochem. Biophys. Res. Commun. 199, 818-825
    • (1994) Biochem. Biophys. Res. Commun. , vol.199 , pp. 818-825
    • Kamijo, T.1    Aoyama, T.2    Komiyama, A.3    Hashimoto, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.