메뉴 건너뛰기




Volumn 279, Issue 20, 2012, Pages 3981-3995

A non-canonical caleosin from Arabidopsis efficiently epoxidizes physiological unsaturated fatty acids with complete stereoselectivity

Author keywords

AtClO4; caleosin; epoxygenase; fatty acid epoxide; peroxygenase

Indexed keywords

9,10 15,16 DIEPOXIDE; CALEOSIN; EPOXIDE; EPOXYGENASE; EPOXYGENATED FATTY ACID; FATTY ACID; HEMOPROTEIN; HYDROPEROXIDE; LINOLEIC ACID; LINOLENIC ACID; OXYGENASE; PEROXYGENASE; UNCLASSIFIED DRUG; UNSATURATED FATTY ACID; VEGETABLE PROTEIN;

EID: 84867098820     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2012.08757.x     Document Type: Article
Times cited : (40)

References (58)
  • 1
  • 2
    • 78650051942 scopus 로고    scopus 로고
    • Naturally occurring monoepoxides of eicosapentaenoic acid and docosahexaenoic acid are bioactive antihyperalgesic lipids
    • Morisseau C, Inceoglu B, Schmelzer K, Tsai HJ, Jinks SL, Hegedus CM, &, Hammock BD, (2010) Naturally occurring monoepoxides of eicosapentaenoic acid and docosahexaenoic acid are bioactive antihyperalgesic lipids. J Lipid Res 51, 3481-3490.
    • (2010) J Lipid Res , vol.51 , pp. 3481-3490
    • Morisseau, C.1    Inceoglu, B.2    Schmelzer, K.3    Tsai, H.J.4    Jinks, S.L.5    Hegedus, C.M.6    Hammock, B.D.7
  • 5
    • 0033993749 scopus 로고    scopus 로고
    • Cytochrome P450 and arachidonic bioactivation: Molecular and functional properties of the arachidonate monoxygenase
    • Capdevila JH, Falck JR, &, Harris RC, (2000) Cytochrome P450 and arachidonic bioactivation: molecular and functional properties of the arachidonate monoxygenase. J Lipid Res 41, 163-181.
    • (2000) J Lipid Res , vol.41 , pp. 163-181
    • Capdevila, J.H.1    Falck, J.R.2    Harris, R.C.3
  • 6
    • 0035965327 scopus 로고    scopus 로고
    • Epoxygenase pathways of arachidonic acid metabolism
    • Zeldin DC, (2001) Epoxygenase pathways of arachidonic acid metabolism. J Biol Chem 276, 36059-36062.
    • (2001) J Biol Chem , vol.276 , pp. 36059-36062
    • Zeldin, D.C.1
  • 7
    • 66349109660 scopus 로고    scopus 로고
    • Arachidonic acid cytochrome P450 epoxygenase pathway
    • Spector AA, (2009) Arachidonic acid cytochrome P450 epoxygenase pathway. J Lipid Res 50 (Supplement), S52-S56.
    • (2009) J Lipid Res , vol.50
    • Spector, A.A.1
  • 8
    • 51249189351 scopus 로고
    • Naturally occurring epoxy oils
    • Krewson CF, (1967) Naturally occurring epoxy oils. J Am Oil Chem Soc 45, 250-256.
    • (1967) J Am Oil Chem Soc , vol.45 , pp. 250-256
    • Krewson, C.F.1
  • 9
    • 0029976635 scopus 로고    scopus 로고
    • Uses of biotechnology in modifying plant lipids
    • Budziszewski GJ, Croft KP, &, Hildebrand DF, (1996) Uses of biotechnology in modifying plant lipids. Lipids 31, 557-569.
    • (1996) Lipids , vol.31 , pp. 557-569
    • Budziszewski, G.J.1    Croft, K.P.2    Hildebrand, D.F.3
  • 10
    • 33847111226 scopus 로고    scopus 로고
    • Synthesis, characterization, antibacterial and corrosion properties of epoxides, epoxy-polyols and epoxy-polyurethane coating from linseed and Pongamia glabra seed oils
    • Sharmin E, Ashraf SM, &, Ahmad S, (2007) Synthesis, characterization, antibacterial and corrosion properties of epoxides, epoxy-polyols and epoxy-polyurethane coating from linseed and Pongamia glabra seed oils. Int J Biol Macromol 40, 407-422.
    • (2007) Int J Biol Macromol , vol.40 , pp. 407-422
    • Sharmin, E.1    Ashraf, S.M.2    Ahmad, S.3
  • 12
    • 0035032084 scopus 로고    scopus 로고
    • Transgenic expression of a Î12-epoxygenase gene in Arabidopsis seeds inhibits accumulation of linoleic acid
    • Singh S, Thomaeus S, Lee M, Stymne S, &, Green A, (2001) Transgenic expression of a Î12-epoxygenase gene in Arabidopsis seeds inhibits accumulation of linoleic acid. Planta 212, 872-879.
    • (2001) Planta , vol.212 , pp. 872-879
    • Singh, S.1    Thomaeus, S.2    Lee, M.3    Stymne, S.4    Green, A.5
  • 13
    • 5344259652 scopus 로고    scopus 로고
    • Level of accumulation of epoxy fatty acid in Arabidopsis thaliana expressing a linoleic acid Î12-epoxygenase is influenced by the availability of the substrate linoleic acid
    • Rezzonico E, Moire L, Delessert S, &, Poirier Y, (2004) Level of accumulation of epoxy fatty acid in Arabidopsis thaliana expressing a linoleic acid Î12-epoxygenase is influenced by the availability of the substrate linoleic acid. Theor Appl Genet 109, 1077-1082.
    • (2004) Theor Appl Genet , vol.109 , pp. 1077-1082
    • Rezzonico, E.1    Moire, L.2    Delessert, S.3    Poirier, Y.4
  • 14
    • 0027317790 scopus 로고
    • Biosynthesis of vernolate (cis-12-epoxyoctadeca-cis-9-enoate) in microsomes preparations from developing endospems of Euphorbia lagascae
    • Bafor M, Smith MA, Jonsson I, Stobart K, &, Stymne S, (1993) Biosynthesis of vernolate (cis-12-epoxyoctadeca-cis-9-enoate) in microsomes preparations from developing endospems of Euphorbia lagascae. Arch Biochem Biophys 303, 145-151.
    • (1993) Arch Biochem Biophys , vol.303 , pp. 145-151
    • Bafor, M.1    Smith, M.A.2    Jonsson, I.3    Stobart, K.4    Stymne, S.5
  • 15
    • 85047686495 scopus 로고    scopus 로고
    • Transgenic production of epoxy fatty acids by expression of a cytochrome P450 enzyme from Euphorbia lagascae seed
    • Cahoon EB, Ripp KG, Hall SE, &, McGonicle B, (2002) Transgenic production of epoxy fatty acids by expression of a cytochrome P450 enzyme from Euphorbia lagascae seed. Plant Physiol 128, 615-624.
    • (2002) Plant Physiol , vol.128 , pp. 615-624
    • Cahoon, E.B.1    Ripp, K.G.2    Hall, S.E.3    McGonicle, B.4
  • 16
    • 0001026326 scopus 로고
    • Biopolyesters of plants: Cutin and suberin
    • Kolattukudy PE, (1980) Biopolyesters of plants: cutin and suberin. Science 208, 990-1000.
    • (1980) Science , vol.208 , pp. 990-1000
    • Kolattukudy, P.E.1
  • 19
    • 0000799562 scopus 로고
    • Oxygenated fatty acids with anti-rice blast fungus activity in rice plants
    • Kato T, Yamaguchi Y, Namai T, &, Hirukawa T, (1993) Oxygenated fatty acids with anti-rice blast fungus activity in rice plants. Biosci Biotechnol Biochem 57, 283-287.
    • (1993) Biosci Biotechnol Biochem , vol.57 , pp. 283-287
    • Kato, T.1    Yamaguchi, Y.2    Namai, T.3    Hirukawa, T.4
  • 20
    • 0000799568 scopus 로고
    • Anti-rice blast activity and resistance induction of C-18 oxygenated fatty acids
    • Namai T, Kato T, Yamaguchi Y, &, Hirukawa T, (1993) Anti-rice blast activity and resistance induction of C-18 oxygenated fatty acids. Biosci Biotechnol Biochem 57, 611-613.
    • (1993) Biosci Biotechnol Biochem , vol.57 , pp. 611-613
    • Namai, T.1    Kato, T.2    Yamaguchi, Y.3    Hirukawa, T.4
  • 21
    • 79953901318 scopus 로고    scopus 로고
    • Epoxygenase fatty acids and soluble epoxide hydrolase inhibition: Novel mediators of pain reduction
    • Wagner K, Inceoglu B, Gill SS, &, Hammock BD, (2011) Epoxygenase fatty acids and soluble epoxide hydrolase inhibition: novel mediators of pain reduction. Agric Food Chem 59, 2816-2824.
    • (2011) Agric Food Chem , vol.59 , pp. 2816-2824
    • Wagner, K.1    Inceoglu, B.2    Gill, S.S.3    Hammock, B.D.4
  • 22
    • 79851501898 scopus 로고    scopus 로고
    • Soluble epoxide hydrolase inhibitors and their potential for treatment of multiple pathologic conditions
    • Ingraham RH, Gless RD, &, Lo HY, (2011) Soluble epoxide hydrolase inhibitors and their potential for treatment of multiple pathologic conditions. Curr Med Chem 18, 587-603.
    • (2011) Curr Med Chem , vol.18 , pp. 587-603
    • Ingraham, R.H.1    Gless, R.D.2    Lo, H.Y.3
  • 23
    • 0028485440 scopus 로고
    • Characterization of an Arabidopsis cDNA for a soluble epoxide hydrolase gene that is inducible by auxin and water stress
    • Kiyosue T, Beetham JK, Pinot F, Hammock BD, Yamaguchishinozaki K, &, Shinozaki K, (1994) Characterization of an Arabidopsis cDNA for a soluble epoxide hydrolase gene that is inducible by auxin and water stress. Plant J 6, 259-269.
    • (1994) Plant J , vol.6 , pp. 259-269
    • Kiyosue, T.1    Beetham, J.K.2    Pinot, F.3    Hammock, B.D.4    Yamaguchishinozaki, K.5    Shinozaki, K.6
  • 25
    • 0030951913 scopus 로고    scopus 로고
    • Epoxide hydrolase activities in the microsomes and the soluble fraction from Vicia sativa seedlings
    • Pinot F, Bosch H, Salaun JP, Durst F, Mioskowski C, &, Hammock BD, (1997) Epoxide hydrolase activities in the microsomes and the soluble fraction from Vicia sativa seedlings. Plant Physiol Biochem 35, 103-110.
    • (1997) Plant Physiol Biochem , vol.35 , pp. 103-110
    • Pinot, F.1    Bosch, H.2    Salaun, J.P.3    Durst, F.4    Mioskowski, C.5    Hammock, B.D.6
  • 26
    • 0000153776 scopus 로고
    • The occurrence of lipid-hydroperoxide-decomposing activities in rice and the relationship of such activities to the formation of antifungal substances
    • Ohta H, Shida K, Peng YL, Furusawa I, Shishiyama J, Aibara S, &, Morita Y, (1990) The occurrence of lipid-hydroperoxide-decomposing activities in rice and the relationship of such activities to the formation of antifungal substances. Plant Cell Physiol 31, 1117-1122.
    • (1990) Plant Cell Physiol , vol.31 , pp. 1117-1122
    • Ohta, H.1    Shida, K.2    Peng, Y.L.3    Furusawa, I.4    Shishiyama, J.5    Aibara, S.6    Morita, Y.7
  • 27
    • 12044250894 scopus 로고
    • A lipoxygenase pathway is activated in rice after infection with the rice blast fungus Magnaporthe grisea
    • Ohta H, Shida K, Peng YL, Furasawa I, Shishiyama J, Aibara S, &, Morita Y, (1991) A lipoxygenase pathway is activated in rice after infection with the rice blast fungus Magnaporthe grisea. Plant Physiol 97, 94-98.
    • (1991) Plant Physiol , vol.97 , pp. 94-98
    • Ohta, H.1    Shida, K.2    Peng, Y.L.3    Furasawa, I.4    Shishiyama, J.5    Aibara, S.6    Morita, Y.7
  • 28
    • 0025323367 scopus 로고
    • Efficient epoxidation of unsaturated fatty acids by a hydroperoxide-dependent oxygenase
    • Blée E, &, Schuber F, (1990) Efficient epoxidation of unsaturated fatty acids by a hydroperoxide-dependent oxygenase. J Biol Chem 265, 12887-12894.
    • (1990) J Biol Chem , vol.265 , pp. 12887-12894
    • Blée, E.1    Schuber, F.2
  • 29
    • 0025642481 scopus 로고
    • Hydroperoxide-dependent epoxidation of unsaturated fatty acids in the broad bean (Vicia faba L.)
    • Hamberg M, &, Hamberg G, (1990) Hydroperoxide-dependent epoxidation of unsaturated fatty acids in the broad bean (Vicia faba L.). Arch Biochem Biophys 283, 409-416.
    • (1990) Arch Biochem Biophys , vol.283 , pp. 409-416
    • Hamberg, M.1    Hamberg, G.2
  • 30
    • 0001152788 scopus 로고
    • Biosynthesis of cutin monomers - Involvement of a lipoxygenase/ peroxygenase pathway
    • Blée E, &, Schuber F, (1993) Biosynthesis of cutin monomers-involvement of a lipoxygenase/peroxygenase pathway. Plant J 4, 113-123.
    • (1993) Plant J , vol.4 , pp. 113-123
    • Blée, E.1    Schuber, F.2
  • 31
    • 0142134234 scopus 로고    scopus 로고
    • Formation of plant cuticule: Evidence for the occurrence of the peroxygenase pathway
    • Lequeu J, Fauconnier ML, Chammai A, Bronner R, &, Blée E, (2003) Formation of plant cuticule: evidence for the occurrence of the peroxygenase pathway. Plant J 36, 155-164.
    • (2003) Plant J , vol.36 , pp. 155-164
    • Lequeu, J.1    Fauconnier, M.L.2    Chammai, A.3    Bronner, R.4    Blée, E.5
  • 32
    • 33845929997 scopus 로고    scopus 로고
    • Plant seed peroxygenase is an original heme-oxygenase with an EF-hand calcium binding motif
    • Hanano A, Burcklen M, Flenet M, Ivancich A, Louwagie M, Garin J, &, Blée E, (2006) Plant seed peroxygenase is an original heme-oxygenase with an EF-hand calcium binding motif. J Biol Chem 281, 33140-33151.
    • (2006) J Biol Chem , vol.281 , pp. 33140-33151
    • Hanano, A.1    Burcklen, M.2    Flenet, M.3    Ivancich, A.4    Louwagie, M.5    Garin, J.6    Blée, E.7
  • 33
    • 80052393168 scopus 로고    scopus 로고
    • A peroxygenase pathway involved in the biosynthesis of epoxy fatty acids in oat (Avena sativa L.)
    • Meesapyodsuk D, &, Qiu X, (2011) A peroxygenase pathway involved in the biosynthesis of epoxy fatty acids in oat (Avena sativa L.). Plant Physiol 157, 454-463.
    • (2011) Plant Physiol , vol.157 , pp. 454-463
    • Meesapyodsuk, D.1    Qiu, X.2
  • 35
    • 0035967969 scopus 로고    scopus 로고
    • Gene families from the Arabidopsis thaliana pollen coat proteome
    • Mayfield JA, Fiebig A, Johnstone SE, &, Preuss D, (2001) Gene families from the Arabidopsis thaliana pollen coat proteome. Science 292, 2482-2485.
    • (2001) Science , vol.292 , pp. 2482-2485
    • Mayfield, J.A.1    Fiebig, A.2    Johnstone, S.E.3    Preuss, D.4
  • 36
    • 79956125692 scopus 로고    scopus 로고
    • A stress-responsive caleosin-like protein, AtCLO4, acts as a negative regulator of ABA responses in Arabidopsis
    • Kim YY, Jung KW, Yoo KS, Jeung JU, &, Shin JS, (2011) A stress-responsive caleosin-like protein, AtCLO4, acts as a negative regulator of ABA responses in Arabidopsis. Plant Cell Physiol 52, 874-884.
    • (2011) Plant Cell Physiol , vol.52 , pp. 874-884
    • Kim, Y.Y.1    Jung, K.W.2    Yoo, K.S.3    Jeung, J.U.4    Shin, J.S.5
  • 37
    • 0033213638 scopus 로고    scopus 로고
    • Cloning and secondary structure analysis of caleosin, a unique calcium-binding protein in oil bodies of plant seeds
    • Chen JCF, Tsai CCY, &, Tzen JTC, (1999) Cloning and secondary structure analysis of caleosin, a unique calcium-binding protein in oil bodies of plant seeds. Plant Cell Physiol 40, 1079-1086.
    • (1999) Plant Cell Physiol , vol.40 , pp. 1079-1086
    • Chen, J.C.F.1    Tsai, C.C.Y.2    Tzen, J.T.C.3
  • 38
    • 14844314796 scopus 로고    scopus 로고
    • Soybean epoxide hydrolase. Identification of the catalytic residues and probing of the reaction mechanism with secondary kinetic isotope effects
    • Blée E, Summerer S, Flenet M, Rogniaux H, Van Dorsselaer A, &, Schuber F, (2005) Soybean epoxide hydrolase. Identification of the catalytic residues and probing of the reaction mechanism with secondary kinetic isotope effects. J Biol Chem 280, 6479-6487.
    • (2005) J Biol Chem , vol.280 , pp. 6479-6487
    • Blée, E.1    Summerer, S.2    Flenet, M.3    Rogniaux, H.4    Van Dorsselaer, A.5    Schuber, F.6
  • 39
    • 0032700710 scopus 로고    scopus 로고
    • On the specificity of allene oxide cyclase
    • Ziegler J, Wasternack C, &, Hamberg M, (1999) On the specificity of allene oxide cyclase. Lipids 34, 1005-1015.
    • (1999) Lipids , vol.34 , pp. 1005-1015
    • Ziegler, J.1    Wasternack, C.2    Hamberg, M.3
  • 40
    • 0000608573 scopus 로고
    • On the specificity of a fatty acid epoxygenase in broad bean (Vicia faba L.)
    • Hamberg M, &, Fahlstadius P, (1992) On the specificity of a fatty acid epoxygenase in broad bean (Vicia faba L.). Plant Physiol 99, 987-995.
    • (1992) Plant Physiol , vol.99 , pp. 987-995
    • Hamberg, M.1    Fahlstadius, P.2
  • 41
    • 0027532881 scopus 로고
    • Mechanism of reaction of fatty acid hydroperoxides with soybean peroxygenase
    • Blée E, Wilcox AL, Marnett LJ, &, Schuber F, (1993) Mechanism of reaction of fatty acid hydroperoxides with soybean peroxygenase. J Biol Chem 268, 1708-1715.
    • (1993) J Biol Chem , vol.268 , pp. 1708-1715
    • Blée, E.1    Wilcox, A.L.2    Marnett, L.J.3    Schuber, F.4
  • 42
    • 0023318929 scopus 로고
    • Hydroperoxide-dependent sulfoxidation catalyzed by soybean microsomes
    • Blée E, &, Durst F, (1987) Hydroperoxide-dependent sulfoxidation catalyzed by soybean microsomes. Arch Biochem Biophys 254, 43-52.
    • (1987) Arch Biochem Biophys , vol.254 , pp. 43-52
    • Blée, E.1    Durst, F.2
  • 44
    • 0017724271 scopus 로고
    • Hydroperoxide-dependent hydroxylation involving 'H2O2-reducible hemoprotein' in microsomes of pea seeds
    • Ishimaru A, &, Yamazaki I, (1977) Hydroperoxide-dependent hydroxylation involving 'H2O2-reducible hemoprotein' in microsomes of pea seeds. J Biol Chem 252, 6118-6124.
    • (1977) J Biol Chem , vol.252 , pp. 6118-6124
    • Ishimaru, A.1    Yamazaki, I.2
  • 45
    • 4344717788 scopus 로고    scopus 로고
    • Expression of a Stokesia laevis epoxygenase gene
    • Hatanaka T, Shimizu R, &, Hildebrand D, (2004) Expression of a Stokesia laevis epoxygenase gene. Phytochemistry 65, 2189-2196.
    • (2004) Phytochemistry , vol.65 , pp. 2189-2196
    • Hatanaka, T.1    Shimizu, R.2    Hildebrand, D.3
  • 46
    • 58449111346 scopus 로고    scopus 로고
    • Arabidopsis thaliana CYP77A4 is the first cytochrome P450 able to catalyze the epoxidation of free fatty acids in plants
    • Sauveplane V, Kandel S, Kastner PE, Ehlting J, Compagnon V, Werck-Reichhart D, &, Pinot F, (2008) Arabidopsis thaliana CYP77A4 is the first cytochrome P450 able to catalyze the epoxidation of free fatty acids in plants. FEBS J 276, 719-735.
    • (2008) FEBS J , vol.276 , pp. 719-735
    • Sauveplane, V.1    Kandel, S.2    Kastner, P.E.3    Ehlting, J.4    Compagnon, V.5    Werck-Reichhart, D.6    Pinot, F.7
  • 47
    • 0027716061 scopus 로고
    • Regio- and stereoselectivity of cytochrome P-450 and peroxygenase- dependent formation of cis-12,13-epoxy-9(Z)- octadecenoic acid (vernolic acid) in Euphorbia lagascae
    • Blée E, Stahl U, Schuber F, &, Stymne S, (1993) Regio- and stereoselectivity of cytochrome P-450 and peroxygenase- dependent formation of cis-12,13-epoxy-9(Z)- octadecenoic acid (vernolic acid) in Euphorbia lagascae. Biochem Biophys Res Commun 197, 778-784.
    • (1993) Biochem Biophys Res Commun , vol.197 , pp. 778-784
    • Blée, E.1    Stahl, U.2    Schuber, F.3    Stymne, S.4
  • 48
    • 33846408654 scopus 로고    scopus 로고
    • Early accumulation of non- enzymatically synthesised oxylipins in Arabidopsis thaliana after infection with Pseudomonas syringae
    • Grun C, Berger S, Matthes D, &, Mueller MJ, (2006) Early accumulation of non- enzymatically synthesised oxylipins in Arabidopsis thaliana after infection with Pseudomonas syringae. Funct Plant Biol 34, 65-71.
    • (2006) Funct Plant Biol , vol.34 , pp. 65-71
    • Grun, C.1    Berger, S.2    Matthes, D.3    Mueller, M.J.4
  • 49
    • 33748334331 scopus 로고    scopus 로고
    • A role for caleosin in degradation of oil-body storage lipid during seed germination
    • Poxleitner M, Rogers SW, Samuels AL, Browse J, &, Rogers J, (2006) A role for caleosin in degradation of oil-body storage lipid during seed germination. Plant J 47, 917-933.
    • (2006) Plant J , vol.47 , pp. 917-933
    • Poxleitner, M.1    Rogers, S.W.2    Samuels, A.L.3    Browse, J.4    Rogers, J.5
  • 50
    • 78651269018 scopus 로고    scopus 로고
    • RD20, a stress-inducible caleosin, participates in stomatal control, transpiration and drought tolerance in Arabidopsis thaliana
    • Aubert Y, Vile D, Pervent M, Aldon D, Randy B, Simonneau T, Vavasseur A, &, Galaud JP, (2010) RD20, a stress-inducible caleosin, participates in stomatal control, transpiration and drought tolerance in Arabidopsis thaliana. Plant Cell Physiol 51, 1975-1987.
    • (2010) Plant Cell Physiol , vol.51 , pp. 1975-1987
    • Aubert, Y.1    Vile, D.2    Pervent, M.3    Aldon, D.4    Randy, B.5    Simonneau, T.6    Vavasseur, A.7    Galaud, J.P.8
  • 52
    • 0032170495 scopus 로고    scopus 로고
    • High- efficiency cloning of Arabidopsis full-length cDNA by biotinylated CAP trapper
    • Seki M, Carninc P, Nishiyama Y, Hayashizaki Y, &, Shinozaki K, (1998) High- efficiency cloning of Arabidopsis full-length cDNA by biotinylated CAP trapper. Plant J 15, 707-720.
    • (1998) Plant J , vol.15 , pp. 707-720
    • Seki, M.1    Carninc, P.2    Nishiyama, Y.3    Hayashizaki, Y.4    Shinozaki, K.5
  • 54
    • 0023275830 scopus 로고
    • A family of yeast expression vectors containing the phage f1 intergenic region
    • Verner T, Dignar D, &, Thomas DY, (1987) A family of yeast expression vectors containing the phage f1 intergenic region. Gene 52, 225-233.
    • (1987) Gene , vol.52 , pp. 225-233
    • Verner, T.1    Dignar, D.2    Thomas, D.Y.3
  • 55
    • 0018722047 scopus 로고
    • Kinetic analysis of progress curves
    • Orsi BA, &, Tipton KF, (1979) Kinetic analysis of progress curves. Methods Enzymol 63, 159-183.
    • (1979) Methods Enzymol , vol.63 , pp. 159-183
    • Orsi, B.A.1    Tipton, K.F.2
  • 56
    • 0026640694 scopus 로고
    • Enantioselectivity of the hydrolysis of linoleic acid monoepoxides catalyzed by soybean fatty acid epoxide hydrolase
    • Blée E, &, Schuber F, (1992) Enantioselectivity of the hydrolysis of linoleic acid monoepoxides catalyzed by soybean fatty acid epoxide hydrolase. Biochem Biophys Res Commun 187, 171-177.
    • (1992) Biochem Biophys Res Commun , vol.187 , pp. 171-177
    • Blée, E.1    Schuber, F.2
  • 57
    • 19644401570 scopus 로고    scopus 로고
    • Analysis of fatty acid epoxidation by high performance liquid chromatography with evaporative light scattering detection and mass spectrometry
    • Orellana-Coca C, Adlercreutz D, Andersson MM, Mattiasson B, &, Hatti-Kaul R, (2005) Analysis of fatty acid epoxidation by high performance liquid chromatography with evaporative light scattering detection and mass spectrometry. Chem Phys Lipids 135, 189-199.
    • (2005) Chem Phys Lipids , vol.135 , pp. 189-199
    • Orellana-Coca, C.1    Adlercreutz, D.2    Andersson, M.M.3    Mattiasson, B.4    Hatti-Kaul, R.5
  • 58
    • 32644481938 scopus 로고    scopus 로고
    • Genome-wide identification and testing of superior reference genes for transcript normalization in Arabidopsis
    • Czechowski T, Stitt M, Altmann T, Udvardi MK, &, Scheible WR, (2005) Genome-wide identification and testing of superior reference genes for transcript normalization in Arabidopsis. Plant Physiol 139, 5-17.
    • (2005) Plant Physiol , vol.139 , pp. 5-17
    • Czechowski, T.1    Stitt, M.2    Altmann, T.3    Udvardi, M.K.4    Scheible, W.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.