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Volumn 80, Issue 2, 2011, Pages 268-273

Optimized refolding and characterization of S-peroxidase (CWPO-C of Populus alba) expressed in E. coli

Author keywords

Cell wall peroxidase; Populus alba L; Refolding; S peroxidase; Sinapyl alcohol

Indexed keywords

2,2' AZINO DI (3 ETHYLBENZOTHIAZOLINE) 6 SULFONIC ACID; 2,2'-AZINO-DI-(3-ETHYLBENZOTHIAZOLINE)-6-SULFONIC ACID; BENZOTHIAZOLE DERIVATIVE; CONIFERYL ALCOHOL; GLUTATHIONE DISULFIDE; HEMIN; HORSERADISH PEROXIDASE; PEROXIDASE; PHENOL DERIVATIVE; PHENYLPROPIONIC ACID DERIVATIVE; SINAPYL ALCOHOL; SULFONIC ACID DERIVATIVE; VEGETABLE PROTEIN;

EID: 80054083263     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2011.08.003     Document Type: Article
Times cited : (10)

References (21)
  • 1
    • 0028050797 scopus 로고
    • Covalent cross-links in cell walls isolated from maize cell the cell wall
    • K. Iiyama, T.B.T. Lam, and B. Stone Covalent cross-links in cell walls isolated from maize cell the cell wall Plant Physiol. 104 1994 315 320
    • (1994) Plant Physiol. , vol.104 , pp. 315-320
    • Iiyama, K.1    Lam, T.B.T.2    Stone, B.3
  • 2
    • 0042823502 scopus 로고    scopus 로고
    • A lignin-specific peroxidase in tobacco whose antisense suppression leads to vascular tissue modification
    • DOI 10.1016/S0031-9422(03)00212-7
    • K.A. Blee, J.W. Choi, A.P. O'Connell, W. Schuch, N.G. Lewis, and G.P. Bolwell A lignin-specific peroxidase in tobacco whose antisense suppression leads to vascular tissue modification Phytochemistry 64 2003 163 176 (Pubitemid 37101802)
    • (2003) Phytochemistry , vol.64 , Issue.1 , pp. 163-176
    • Bleea, K.A.1    Choib, J.W.2    O'Connella, A.P.3    Schuchc, W.4    Lewis, N.G.5    Bolwell, G.P.6
  • 3
    • 0001563457 scopus 로고
    • Some properties of syringaldazine oxidase, a peroxidase specifically involved in the lignifications processes
    • R. Goldberg, A.M. Catesson, and Y. Czaninski Some properties of syringaldazine oxidase, a peroxidase specifically involved in the lignifications processes Z. Pflanzenphysiol. Bd. 110 1983 267 279
    • (1983) Z. Pflanzenphysiol. Bd. , vol.110 , pp. 267-279
    • Goldberg, R.1    Catesson, A.M.2    Czaninski, Y.3
  • 4
    • 84989698471 scopus 로고
    • Properties of syringaldazine oxidase peroxidase in maize roots
    • R. Grison, and P.E. Pilet Properties of syringaldazine oxidase peroxidase in maize roots J. Plant Physiol. 118 1985 201 208
    • (1985) J. Plant Physiol. , vol.118 , pp. 201-208
    • Grison, R.1    Pilet, P.E.2
  • 5
    • 33644835373 scopus 로고    scopus 로고
    • Cloning and molecular characterization of the basic peroxidase isoenzyme from Zinnia elegans, an enzyme involved in lignin biosynthesis
    • DOI 10.1104/pp.105.069674
    • C. Gabaldón, L.S. Matías, A.P. María, and A.R. Barcelo Cloning and molecular characterization of the basic peroxidase isoenzyme from Zinnia elegans, an enzyme involved in lignin biosynthesis Plant Physiol. 139 2005 1138 1154 (Pubitemid 43786818)
    • (2005) Plant Physiology , vol.139 , Issue.3 , pp. 1138-1154
    • Gabaldon, C.1    Lopez-Serrano, M.2    Pedreno, M.A.3    Barcelo, A.R.4
  • 6
    • 33750898437 scopus 로고    scopus 로고
    • The cationic cell-wall-peroxidase having oxidation ability for polymeric substrate participates in the late stage of lignification of Populus alba L
    • DOI 10.1007/s11103-006-9057-3
    • S. Sasaki, K. Baba, T. Nishida, Y. Tsutsumi, and R. Kondo The cationic cell-wall-peroxidase having oxidation ability for polymeric substrate participates in the late stage of lignifications of Populus alba L Plant Mol. Biol. 62 2006 797 807 (Pubitemid 44730319)
    • (2006) Plant Molecular Biology , vol.62 , Issue.6 , pp. 797-807
    • Sasaki, S.1    Baba, K.2    Nishida, T.3    Tsutsumi, Y.4    Kondo, R.5
  • 7
    • 23744484454 scopus 로고    scopus 로고
    • Characterization of basic p-coumaryl and coniferyl alcohol oxidizing peroxidases from a lignin-forming Picea abies suspension culture
    • DOI 10.1007/s11103-005-5345-6
    • S. Koutaniemi, M.M. Toikka, A. Karkonen, M. Mustonen, T. Lundell, L.K. Simola, I.A. Kilpelainen, and T.H. Teeri Characterization of basic p-coumaryl and coniferyl alcohol oxidizing peroxidases from a lignin-forming Picea abies suspension culture Plant Mol. Biol. 58 2005 141 157 (Pubitemid 41125997)
    • (2005) Plant Molecular Biology , vol.58 , Issue.2 , pp. 141-157
    • Koutaniemi, S.1    Toikka, M.M.2    Karkonen, A.3    Mustonen, M.4    Lundell, T.5    Simola, L.K.6    Kilpelainen, I.A.7    Teeri, T.H.8
  • 8
    • 0041936701 scopus 로고    scopus 로고
    • Sinapyl alcohol-specific peroxidase isoenzyme catalyzes the formation of the dehydrogenative polymer from sinapyl alcohol
    • W. Aoyama, S. Sasaki, S. Matsumura, H. Hirai, Y. Tsutsumi, and T. Nishida Sinapyl alcohol-specific peroxidase isoenzyme catalyzes the formation of the dehydrogenative polymer from sinapyl alcohol J. Wood Sci. 48 2002 497 504 (Pubitemid 37292758)
    • (2002) Journal of Wood Science , vol.48 , Issue.6 , pp. 497-504
    • Aoyama, W.1    Sasaki, S.2    Matsumura, S.3    Mitsunaga, T.4    Hirai, H.5    Tsutsumi, Y.6    Nishida, T.7
  • 9
    • 37549046767 scopus 로고    scopus 로고
    • Role of Tyr residues on the protein surface of cationic cell-wall-peroxidase (CWPO-C) from poplar: Potential oxidation sites for oxidative polymerization of lignin
    • S. Sasaki, D. Nonaka, H. Wariishi, Y. Tsutsumi, and R. Kondo Role of Tyr residues on the protein surface of cationic cell-wall-peroxidase (CWPO-C) from poplar: Potential oxidation sites for oxidative polymerization of lignin Phytochemistry 69 2008 348 355
    • (2008) Phytochemistry , vol.69 , pp. 348-355
    • Sasaki, S.1    Nonaka, D.2    Wariishi, H.3    Tsutsumi, Y.4    Kondo, R.5
  • 10
    • 33745611626 scopus 로고
    • Facile Large-Scale Synthesis of Coniferyl, Sinapyl, and Para-Coumaryl Alcohol
    • S. Quideau, and J. Ralph Facile Large-Scale Synthesis of Coniferyl, Sinapyl, and Para-Coumaryl Alcohol J. Agric. Food Chem. 40 1992 1108 1110
    • (1992) J. Agric. Food Chem. , vol.40 , pp. 1108-1110
    • Quideau, S.1    Ralph, J.2
  • 11
    • 80054054356 scopus 로고    scopus 로고
    • Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
    • J. Buchner, T. Kiefhaber, Protein Folding Handbook, vol. 5, Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, 2005, p. 1263.
    • (2005) Protein Folding Handbook , vol.5 , pp. 1263
    • Buchner, J.1    Kiefhaber, T.2
  • 14
    • 0030587532 scopus 로고    scopus 로고
    • Heterologous expression and reconstitution of fungal Mn peroxidase
    • DOI 10.1006/abbi.1996.0413
    • R. Whitwam, and M. Tien Heterologous expression and reconstitution of fungal Mn peroxidase Arch. Biochem. Biophys. 333 1996 439 446 (Pubitemid 26304912)
    • (1996) Archives of Biochemistry and Biophysics , vol.333 , Issue.2 , pp. 439-446
    • Whitwam, R.1    Tien, M.2
  • 16
    • 0017809275 scopus 로고
    • The renaturation of reduced chymotrypsinogen A in guanidine HC1. Refolding versus aggregation
    • G. Orsini, and M.E. Goldberg The renaturation of Chymotrypsinogen A in guanidine HCl. Refolding versus aggregation J. Biol. Chem. 253 1978 3453 3458 (Pubitemid 8349797)
    • (1978) Journal of Biological Chemistry , vol.253 , Issue.10 , pp. 3453-3458
    • Orsini, G.1    Goldberg, M.E.2
  • 17
    • 80054074081 scopus 로고
    • Process for activation of t-PA or Ing after genetic expression in prokaryotes
    • R. Rudolph, S. Fischer, and R. Mattes Process for activation of t-PA or Ing after genetic expression in prokaryotes US Patent 5 1995 453 463
    • (1995) US Patent , vol.5 , pp. 453-463
    • Rudolph, R.1    Fischer, S.2    Mattes, R.3
  • 18
    • 70349466798 scopus 로고    scopus 로고
    • Escherichia coli expression and in vitro activation of a unique ligninolytic peroxidase that has a catalytic tyrosine residue
    • M. Yuta, M. María, J.R. Francisco, J.M. María, W. Hiroyuki, and T.M. Angel Escherichia coli expression and in vitro activation of a unique ligninolytic peroxidase that has a catalytic tyrosine residue Protein Expr. Purif. 68 2009 208 214
    • (2009) Protein Expr. Purif. , vol.68 , pp. 208-214
    • Yuta, M.1    María, M.2    Francisco, J.R.3    María, J.M.4    Hiroyuki, W.5    Angel, T.M.6
  • 20
    • 79955807332 scopus 로고    scopus 로고
    • Investigating the structural and functional effects of mutating Asn glycosylation sites of horseradish peroxidase to Asp
    • A. Sedigheh, K. Khosro, and G. Nasser Investigating the structural and functional effects of mutating Asn glycosylation sites of horseradish peroxidase to Asp Appl. Biochem. Biotechnol. 164 2010 454 463
    • (2010) Appl. Biochem. Biotechnol. , vol.164 , pp. 454-463
    • Sedigheh, A.1    Khosro, K.2    Nasser, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.