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Volumn 40, Issue 12, 2005, Pages 3742-3748

Purification and characterization of UDPG:ginsenoside Rd glucosyltransferase from suspended cells of Panax notoginseng

Author keywords

Bioactive compounds; Chinese traditional medicinal plant; Ginsenoside heterogeneity; Plant cell culture; Purification; UDPG:ginsenoside Rd glucosyltransferase

Indexed keywords

AMMONIUM COMPOUNDS; CELLS; CHROMATOGRAPHIC ANALYSIS; GLUCOSE; ION EXCHANGE; METABOLITES; PH EFFECTS; PLANT CELL CULTURE; PRECIPITATION (CHEMICAL); PURIFICATION;

EID: 26844582530     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2005.05.001     Document Type: Article
Times cited : (54)

References (35)
  • 1
    • 0034354508 scopus 로고    scopus 로고
    • Search for new lead compounds from higher plants
    • J. Buckingham Chapman & Hall/CRC Press England
    • K. Hostettmann, and C. Terreaux Search for new lead compounds from higher plants J. Buckingham Dictionary of Natural Products on CD 54 2000 Chapman & Hall/CRC Press England 652 6578 Chimia (Aarau)
    • (2000) Dictionary of Natural Products on CD , vol.54 , pp. 652-6578
    • Hostettmann, K.1    Terreaux, C.2
  • 4
    • 0002729980 scopus 로고    scopus 로고
    • Getting to the root of ginseng
    • O. Sticher Getting to the root of ginseng Chemtech 28 1998 26 32
    • (1998) Chemtech , vol.28 , pp. 26-32
    • Sticher, O.1
  • 5
    • 0035653529 scopus 로고    scopus 로고
    • Preventing activities of ginseng saponins and some related triterpenoid compounds
    • S. Shibata Preventing activities of ginseng saponins and some related triterpenoid compounds J Korean Med Sci 16 2001 S28 S37
    • (2001) J Korean Med Sci , vol.16
    • Shibata, S.1
  • 6
    • 0036185851 scopus 로고    scopus 로고
    • Manipulation of ginsenoside heterogeneity in cell cultures of Panax notoginseng by addition of jasmonates
    • W. Wang, and J.J. Zhong Manipulation of ginsenoside heterogeneity in cell cultures of Panax notoginseng by addition of jasmonates J Biosci Bioeng 93 2002 48 53
    • (2002) J Biosci Bioeng , vol.93 , pp. 48-53
    • Wang, W.1    Zhong, J.J.2
  • 7
    • 0034789134 scopus 로고    scopus 로고
    • Improvement of Panax notoginseng cell culture for production of ginseng saponin and polysaccharide by high density cultivation in pneumatically agitated bioreactors
    • W.W. Hu, H. Yao, and J.J. Zhong Improvement of Panax notoginseng cell culture for production of ginseng saponin and polysaccharide by high density cultivation in pneumatically agitated bioreactors Biotechnol Prog 17 2001 838 846
    • (2001) Biotechnol Prog , vol.17 , pp. 838-846
    • Hu, W.W.1    Yao, H.2    Zhong, J.J.3
  • 8
    • 0037416688 scopus 로고    scopus 로고
    • Effects of oxygen partial pressure on cell growth and ginsenoside and polysaccharide production in high density cell cultures of Panax notoginseng
    • J. Han, and J.J. Zhong Effects of oxygen partial pressure on cell growth and ginsenoside and polysaccharide production in high density cell cultures of Panax notoginseng Enzyme Microb Technol 32 2003 498 503
    • (2003) Enzyme Microb Technol , vol.32 , pp. 498-503
    • Han, J.1    Zhong, J.J.2
  • 9
    • 14244260586 scopus 로고    scopus 로고
    • 1 biosynthesis by Panax notoginseng cells
    • 1 biosynthesis by Panax notoginseng cells Biotechnol Bioeng 89 2005 444 452
    • (2005) Biotechnol Bioeng , vol.89 , pp. 444-452
    • Yue, C.J.1    Zhong, J.J.2
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Leaemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Leaemmli, U.K.1
  • 11
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • H. Lineweaver, and D. Burk The determination of enzyme dissociation constants J Am Chem Soc 56 1934 658 666
    • (1934) J Am Chem Soc , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 12
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal Biochem 72 1976 248 254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 13
    • 0000690878 scopus 로고
    • Partial purification and properties of an inducible uridine-5′- diphosphate-glucose: Salicylic acid glucosyltransferase from oat roots
    • N. Yalpani, M. Shulz, M.P. Davis, and N.E. Balke Partial purification and properties of an inducible uridine-5′-diphosphate-glucose: salicylic acid glucosyltransferase from oat roots Plant Physiol 100 1992 457 463
    • (1992) Plant Physiol , vol.100 , pp. 457-463
    • Yalpani, N.1    Shulz, M.2    Davis, M.P.3    Balke, N.E.4
  • 14
    • 0037182233 scopus 로고    scopus 로고
    • Towards manipulation of post-biosynthetic events in secondary metabolism of plant cell cultures
    • W. Zhang, C. Curtin, and C. Franco Towards manipulation of post-biosynthetic events in secondary metabolism of plant cell cultures Enzyme Microb Technol 30 2002 688 696
    • (2002) Enzyme Microb Technol , vol.30 , pp. 688-696
    • Zhang, W.1    Curtin, C.2    Franco, C.3
  • 15
    • 0034937480 scopus 로고    scopus 로고
    • Glycosyltransferases in secondary plant metabolism: Tranquilizers and stimulant controllers
    • P. Jones, and T. Vogt Glycosyltransferases in secondary plant metabolism: tranquilizers and stimulant controllers Planta 213 2001 164 174
    • (2001) Planta , vol.213 , pp. 164-174
    • Jones, P.1    Vogt, T.2
  • 18
    • 0037171641 scopus 로고    scopus 로고
    • Purification and characterization of gentisc acid glucosyltransferase from the cultured cells of Catharanthus roseus
    • S. Yamane, K. Shimoda, K. Watanabe, and T. Hirata Purification and characterization of gentisc acid glucosyltransferase from the cultured cells of Catharanthus roseus J Mol Catal B-Enzym 17 2002 59 63
    • (2002) J Mol Catal B-Enzym , vol.17 , pp. 59-63
    • Yamane, S.1    Shimoda, K.2    Watanabe, K.3    Hirata, T.4
  • 19
    • 0038038342 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of a novel UDP-glucose:anthocyanin 3′-O-glucosyltransferase, a key enzyme for blue anthocyanin biosynthesis, from gentian
    • M. Fukuchi-Mizutani, H. Okuhara, Y. Fukui, M. Nakao, Y. Katsumoto, and K. Yonekura-Sakakibara Biochemical and molecular characterization of a novel UDP-glucose:anthocyanin 3′-O-glucosyltransferase, a key enzyme for blue anthocyanin biosynthesis, from gentian Plant Physiol 132 2003 1652 1663
    • (2003) Plant Physiol , vol.132 , pp. 1652-1663
    • Fukuchi-Mizutani, M.1    Okuhara, H.2    Fukui, Y.3    Nakao, M.4    Katsumoto, Y.5    Yonekura-Sakakibara, K.6
  • 20
    • 0037517067 scopus 로고    scopus 로고
    • Isolation of a glucosyltransferase from Arabidopsis thaliana active in the metabolism of the persistent pollutant 3,4-dichloroaniline
    • C. Loutre, D.P. Dixon, M. Brazier, M. Slater, D.J. Cole, and R. Edwards Isolation of a glucosyltransferase from Arabidopsis thaliana active in the metabolism of the persistent pollutant 3,4-dichloroaniline Plant J 34 2003 485 493
    • (2003) Plant J , vol.34 , pp. 485-493
    • Loutre, C.1    Dixon, D.P.2    Brazier, M.3    Slater, M.4    Cole, D.J.5    Edwards, R.6
  • 21
    • 0030773902 scopus 로고    scopus 로고
    • Purification of limonoid glucosyltransferase from navel orange albedo tissues
    • S. Hasegawa, C.G. Suhayda, W.J. Hsu, and G.H. Robsertson Purification of limonoid glucosyltransferase from navel orange albedo tissues Phytochemistry 46 1997 33 37
    • (1997) Phytochemistry , vol.46 , pp. 33-37
    • Hasegawa, S.1    Suhayda, C.G.2    Hsu, W.J.3    Robsertson, G.H.4
  • 22
    • 0030764811 scopus 로고    scopus 로고
    • Purification of UDP-glucose: 4-hydroxybenzoate glucosyltransferase from cell cultures of Lithospermum erythrorhizon
    • S.H. Li, Z.X. Wang, and L. Heide Purification of UDP-glucose: 4-hydroxybenzoate glucosyltransferase from cell cultures of Lithospermum erythrorhizon Phytochemistry 46 1997 27 32
    • (1997) Phytochemistry , vol.46 , pp. 27-32
    • Li, S.H.1    Wang, Z.X.2    Heide, L.3
  • 23
    • 0028871826 scopus 로고
    • Purification and properties of codeinone reductase (NADPH) from Papaver somniferum cell cultures and differentiated plant
    • R. Lenz, and M.H. Zenk Purification and properties of codeinone reductase (NADPH) from Papaver somniferum cell cultures and differentiated plant Eur J Biochem 233 1995 132 139
    • (1995) Eur J Biochem , vol.233 , pp. 132-139
    • Lenz, R.1    Zenk, M.H.2
  • 25
    • 0034077019 scopus 로고    scopus 로고
    • Purification and characterization of multiple forms of α-galactosidase in Cucumis melo plants
    • B. Chrost, and K. Schmitz Purification and characterization of multiple forms of α-galactosidase in Cucumis melo plants J Plant Physiol 156 2000 483 491
    • (2000) J Plant Physiol , vol.156 , pp. 483-491
    • Chrost, B.1    Schmitz, K.2
  • 26
    • 0742285083 scopus 로고    scopus 로고
    • CDNA cloning and expression of isoflavonoid-specific glucosyltransferase from Glycyrrhiza echinata cell-suspension cultures
    • S. Nagashima, R. Inagaki, A. Kubo, M. Hirotani, and T. Yoshikawa cDNA cloning and expression of isoflavonoid-specific glucosyltransferase from Glycyrrhiza echinata cell-suspension cultures Planta 218 2004 456 459
    • (2004) Planta , vol.218 , pp. 456-459
    • Nagashima, S.1    Inagaki, R.2    Kubo, A.3    Hirotani, M.4    Yoshikawa, T.5
  • 27
    • 0032502783 scopus 로고    scopus 로고
    • UDP-glucose:flavonoid 3-O-glucosyltransferase, a homologue of the enzyme encoded by the maize bronze-1 locus that may primarily serve to glucosylate anthocyanidins in vivo
    • C.M. Ford, P.K. Boss, and P.B. Høj UDP-glucose:flavonoid 3-O-glucosyltransferase, a homologue of the enzyme encoded by the maize bronze-1 locus that may primarily serve to glucosylate anthocyanidins in vivo J Biol Chem 273 1998 9224 9233
    • (1998) J Biol Chem , vol.273 , pp. 9224-9233
    • Ford, C.M.1    Boss, P.K.2    Høj, P.B.3
  • 28
    • 0036190402 scopus 로고    scopus 로고
    • Isolation and characterization of limonoid glucosyltransferase from pummelo albedo tissue
    • M.R. Karim, and F. Hashinaga Isolation and characterization of limonoid glucosyltransferase from pummelo albedo tissue Food Chem 76 2002 431 436
    • (2002) Food Chem , vol.76 , pp. 431-436
    • Karim, M.R.1    Hashinaga, F.2
  • 29
    • 0035130438 scopus 로고    scopus 로고
    • Purification and characterization of UDP-glucose:cyclic hydroxamic acid β-glucosyltransferases from maize seedlings
    • K. Ebisui, A. Ishihara, and H. Iwamura Purification and characterization of UDP-glucose:cyclic hydroxamic acid β-glucosyltransferases from maize seedlings Plant Physiol Biochem 39 2001 27 35
    • (2001) Plant Physiol Biochem , vol.39 , pp. 27-35
    • Ebisui, K.1    Ishihara, A.2    Iwamura, H.3
  • 30
    • 4143140277 scopus 로고    scopus 로고
    • Arabidopsis glycosyltransferases as biocatalysts in fermentation for regioselective synthesis of diverse quercetin glucosides
    • E.K. Lim, D.A. Ashford, B. Hou, R.G. Jackson, and D.J. Bowles Arabidopsis glycosyltransferases as biocatalysts in fermentation for regioselective synthesis of diverse quercetin glucosides Biotechnol Bioeng 87 2004 623 631
    • (2004) Biotechnol Bioeng , vol.87 , pp. 623-631
    • Lim, E.K.1    Ashford, D.A.2    Hou, B.3    Jackson, R.G.4    Bowles, D.J.5
  • 31
    • 0742287178 scopus 로고    scopus 로고
    • Bio-fermentation of modified flavonoids: An example of in vivo diversification of secondary metabolites
    • M.G. Willits, M. Giovanni, R.T.N. Prata, C.M. Kramer, V.D. Luca, and J.C. Steffens Bio-fermentation of modified flavonoids: an example of in vivo diversification of secondary metabolites Phytochemistry 65 2004 31 41
    • (2004) Phytochemistry , vol.65 , pp. 31-41
    • Willits, M.G.1    Giovanni, M.2    Prata, R.T.N.3    Kramer, C.M.4    Luca, V.D.5    Steffens, J.C.6
  • 32
    • 0043069756 scopus 로고    scopus 로고
    • Regioselectivity of glucosylation of caffeic acid by a UDP-glucose:glucosyltransferase is maintained in planta
    • E.K. Lim, G.S. Higgins, Y. Li, and D.J. Bowles Regioselectivity of glucosylation of caffeic acid by a UDP-glucose:glucosyltransferase is maintained in planta Biochem J 373 2003 987 992
    • (2003) Biochem J , vol.373 , pp. 987-992
    • Lim, E.K.1    Higgins, G.S.2    Li, Y.3    Bowles, D.J.4
  • 33
    • 0034929830 scopus 로고    scopus 로고
    • Purification and characterization of ginsenoside-β-glucosidase from ginseng
    • C. Zhang, H. Yu, Y. Bao, L. An, and F. Jin Purification and characterization of ginsenoside-β-glucosidase from ginseng Chem Pharm Bull 49 2001 795 798
    • (2001) Chem Pharm Bull , vol.49 , pp. 795-798
    • Zhang, C.1    Yu, H.2    Bao, Y.3    An, L.4    Jin, F.5
  • 34
    • 0036148716 scopus 로고    scopus 로고
    • Purification and characterization of ginsenoside-α-arabinofuranase hydrolyzing ginsenoside Rc into Rd from the fresh root of Panax ginseng
    • C. Zhang, H. Yu, Y. Bao, L. An, and F. Jin Purification and characterization of ginsenoside-α-arabinofuranase hydrolyzing ginsenoside Rc into Rd from the fresh root of Panax ginseng Process Biochem 37 2002 793 798
    • (2002) Process Biochem , vol.37 , pp. 793-798
    • Zhang, C.1    Yu, H.2    Bao, Y.3    An, L.4    Jin, F.5
  • 35
    • 3042761619 scopus 로고    scopus 로고
    • Evaluation of immobilisation effects on metabolic activities and productivity in plant cell processes
    • H. Dornenburg Evaluation of immobilisation effects on metabolic activities and productivity in plant cell processes Process Biochem 39 2004 1369 1375
    • (2004) Process Biochem , vol.39 , pp. 1369-1375
    • Dornenburg, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.