메뉴 건너뛰기




Volumn 87, Issue 7, 2007, Pages 1417-1423

Purification and characterization of a cationic peroxidase from artichoke leaves

Author keywords

AE HPLC; Class III peroxidases; Cynara scolymus; MS MS de novo sequencing; SDS PAGE

Indexed keywords

CYNARA SCOLYMUS;

EID: 34248212286     PISSN: 00225142     EISSN: 10970010     Source Type: Journal    
DOI: 10.1002/jsfa.2882     Document Type: Article
Times cited : (18)

References (43)
  • 1
    • 0003320513 scopus 로고
    • Some molecular aspects of plant peroxidase biosynthetic studies
    • Van Huystee RB, Some molecular aspects of plant peroxidase biosynthetic studies. Annu Rev Plant Physiol 38:205-219 (1987).
    • (1987) Annu Rev Plant Physiol , vol.38 , pp. 205-219
    • Van Huystee, R.B.1
  • 2
    • 12944305786 scopus 로고
    • Superfamily of plant, fungal and bacterial peroxidases
    • Welinder KG, Superfamily of plant, fungal and bacterial peroxidases. Curr Opin Struct Biol 2:388-393 (1992).
    • (1992) Curr Opin Struct Biol , vol.2 , pp. 388-393
    • Welinder, K.G.1
  • 4
    • 0000711907 scopus 로고
    • Interrelationship between lignin deposition and the activities of peroxidase isoenzymes in differentiating tracheary elements of Zinnia
    • Sato Y, Sugiyama M, Gorecki RJ, Fukuda H and Komamine A, Interrelationship between lignin deposition and the activities of peroxidase isoenzymes in differentiating tracheary elements of Zinnia. Planta 189:584-589 (1993).
    • (1993) Planta , vol.189 , pp. 584-589
    • Sato, Y.1    Sugiyama, M.2    Gorecki, R.J.3    Fukuda, H.4    Komamine, A.5
  • 5
    • 0028829961 scopus 로고
    • Stress-induced phenylpropanoid metabolism
    • Dixon RA and Palva NL, Stress-induced phenylpropanoid metabolism. Plant Cell 7:1085-1097 (1995).
    • (1995) Plant Cell , vol.7 , pp. 1085-1097
    • Dixon, R.A.1    Palva, N.L.2
  • 6
    • 84985165999 scopus 로고
    • Peroxidase and its relationship to food flavor and quality: A review
    • Burnette FS, Peroxidase and its relationship to food flavor and quality: a review. J Food Sci 42:1-6 (1977).
    • (1977) J Food Sci , vol.42 , pp. 1-6
    • Burnette, F.S.1
  • 7
    • 1542440741 scopus 로고
    • Polyphenol oxidase peroxidase enzyme activities and their isoenzyme pattern in ripening fruits
    • Prabha TN and Patwardhan MV, Polyphenol oxidase peroxidase enzyme activities and their isoenzyme pattern in ripening fruits. Acta Aliment 15:199-207 (1986).
    • (1986) Acta Aliment , vol.15 , pp. 199-207
    • Prabha, T.N.1    Patwardhan, M.V.2
  • 8
    • 0032907135 scopus 로고    scopus 로고
    • Characterization of soybean peroxidase for the treatment of aqueous phenols
    • Wright H and Nicell JA, Characterization of soybean peroxidase for the treatment of aqueous phenols. Bioresour Technol 70:69-79 (1999).
    • (1999) Bioresour Technol , vol.70 , pp. 69-79
    • Wright, H.1    Nicell, J.A.2
  • 9
    • 0023385298 scopus 로고
    • Polymerization of phenols catalyzed by peroxidase in nonaqueous media
    • Dordick SJ, Marletta MA and Klibanov AM, Polymerization of phenols catalyzed by peroxidase in nonaqueous media. Biotechnol Bioeng 30:31-36 (1987).
    • (1987) Biotechnol Bioeng , vol.30 , pp. 31-36
    • Dordick, S.J.1    Marletta, M.A.2    Klibanov, A.M.3
  • 10
    • 0023654492 scopus 로고
    • Peroxidase-based colorimetric determination of L-ascorbic acid
    • Thompson RQ, Peroxidase-based colorimetric determination of L-ascorbic acid. Anal Chem 59:1119-1121 (1987).
    • (1987) Anal Chem , vol.59 , pp. 1119-1121
    • Thompson, R.Q.1
  • 12
    • 0030130979 scopus 로고    scopus 로고
    • Removal of phenols from a foundry wastewater using horseradish peroxidase
    • Cooper VA and Nicell JA, Removal of phenols from a foundry wastewater using horseradish peroxidase. Water Res 30:934-964 (1996).
    • (1996) Water Res , vol.30 , pp. 934-964
    • Cooper, V.A.1    Nicell, J.A.2
  • 13
    • 0031554260 scopus 로고    scopus 로고
    • Model development for horseradish peroxidase-catalyzed removal of aqueous phenol
    • Buchanan ID and Nicell JA, Model development for horseradish peroxidase-catalyzed removal of aqueous phenol. Biotechnol Bioeng 54:251-261 (1997).
    • (1997) Biotechnol Bioeng , vol.54 , pp. 251-261
    • Buchanan, I.D.1    Nicell, J.A.2
  • 14
    • 34248179799 scopus 로고    scopus 로고
    • Krell HW, Peroxidase: an important enzyme for diagnostic test kits, in Biological, Molecular and Physiological Aspects from Plant Peroxidases, ed. by Lobarsewki J, Greppin H, Penel C and Gaspar T. University M Curie-Sklodowska and University of Geneva, Lublin and Geneva, pp. 469-478 (1991).
    • Krell HW, Peroxidase: an important enzyme for diagnostic test kits, in Biological, Molecular and Physiological Aspects from Plant Peroxidases, ed. by Lobarsewki J, Greppin H, Penel C and Gaspar T. University M Curie-Sklodowska and University of Geneva, Lublin and Geneva, pp. 469-478 (1991).
  • 15
    • 0037194336 scopus 로고    scopus 로고
    • Extremely high stability of African oil palm tree peroxidase
    • Sakharov IY and Sakharova IV, Extremely high stability of African oil palm tree peroxidase. Biochim Biophys Acta 1598:108-114 (2002).
    • (2002) Biochim Biophys Acta , vol.1598 , pp. 108-114
    • Sakharov, I.Y.1    Sakharova, I.V.2
  • 16
    • 0015872949 scopus 로고
    • Peroxidases of Cynara scolymus (global artichoke) leaves: Purification and properties
    • Kamel MY and Ghazy AM, Peroxidases of Cynara scolymus (global artichoke) leaves: purification and properties. Acta Biol Med Germ 31:39-49 (1973).
    • (1973) Acta Biol Med Germ , vol.31 , pp. 39-49
    • Kamel, M.Y.1    Ghazy, A.M.2
  • 18
    • 34248221851 scopus 로고    scopus 로고
    • Di Venere D, Sergio L, Cardinali A, Linsalata V and Pieralice M, Modification of phenolic and peroxidase isoenzymatic patterns in early growth stages of seed propagated artichoke seedlings, in Polyphenols Communications 2002, ed. by El Hadrami I. Imprimerie Papeterie el Watanya, Marrakech pp. 49-50 (2002).
    • Di Venere D, Sergio L, Cardinali A, Linsalata V and Pieralice M, Modification of phenolic and peroxidase isoenzymatic patterns in early growth stages of seed propagated artichoke seedlings, in Polyphenols Communications 2002, ed. by El Hadrami I. Imprimerie Papeterie el Watanya, Marrakech pp. 49-50 (2002).
  • 19
    • 34248154017 scopus 로고    scopus 로고
    • Di Venere D, Sergio L and Cardinali A, Polimorfismo isoenzimatico di perossidasi in foglie e capolini di carciofo (Cynara cardunculus L. var. scolymus (L.) Fiori), in V Giornate Scientifiche SOI, ed. by Failla O and Piagnani C, Edizioni Tecnos s.r.l., Milan, pp. 153-154 (2000).
    • Di Venere D, Sergio L and Cardinali A, Polimorfismo isoenzimatico di perossidasi in foglie e capolini di carciofo (Cynara cardunculus L. var. scolymus (L.) Fiori), in V Giornate Scientifiche SOI, ed. by Failla O and Piagnani C, Edizioni Tecnos s.r.l., Milan, pp. 153-154 (2000).
  • 20
    • 34248194075 scopus 로고    scopus 로고
    • Characterization and partial purification of peroxidase from artichoke leaves
    • Cardinali A, Di Venere D, Sergio L and Linsalata V, Characterization and partial purification of peroxidase from artichoke leaves. Acta Hortic 681:445-452 (2005).
    • (2005) Acta Hortic , vol.681 , pp. 445-452
    • Cardinali, A.1    Di Venere, D.2    Sergio, L.3    Linsalata, V.4
  • 21
    • 0343570017 scopus 로고    scopus 로고
    • Characterization of catecholase and cresolase activities of eggplant polyphenol oxidase
    • Perez-Gilabert M and Garcia Carmona F, Characterization of catecholase and cresolase activities of eggplant polyphenol oxidase. J Agric Food Chem 48:695-700 (2000).
    • (2000) J Agric Food Chem , vol.48 , pp. 695-700
    • Perez-Gilabert, M.1    Garcia Carmona, F.2
  • 22
    • 0028861444 scopus 로고
    • Peroxidase isozyme polymorphism as a potential marker for detection of field resistance in Cucumis sativus to cucumber downy mildew (Pseudoperonospora cubensis (Berk, et Curt.) Rostov.)
    • Lebeda A and Dolezal K, Peroxidase isozyme polymorphism as a potential marker for detection of field resistance in Cucumis sativus to cucumber downy mildew (Pseudoperonospora cubensis (Berk, et Curt.) Rostov.). J Plant Dis Protect 102:467-471 (1995).
    • (1995) J Plant Dis Protect , vol.102 , pp. 467-471
    • Lebeda, A.1    Dolezal, K.2
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the hand of bacteriophage T4
    • Laemmli UK, Cleavage of structural proteins during the assembly of the hand of bacteriophage T4. Nature 227:680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0000523686 scopus 로고
    • An improved periodic acid fuchsin sulfite staining method for evaluation of glycoprotein
    • McGuckin WF and McKenzie BF, An improved periodic acid fuchsin sulfite staining method for evaluation of glycoprotein. Clin Chem 4:476-483 (1958).
    • (1958) Clin Chem , vol.4 , pp. 476-483
    • McGuckin, W.F.1    McKenzie, B.F.2
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-253 (1976).
    • (1976) Anal Biochem , vol.72 , pp. 248-253
    • Bradford, M.M.1
  • 26
    • 34248187341 scopus 로고
    • Alteration of oxidative enzymes in potato tuber tissue by infection with Phytophthora infestans
    • Tomiyama K and Stahmann MA, Alteration of oxidative enzymes in potato tuber tissue by infection with Phytophthora infestans. Plant Physiol 39:483-490 (1964).
    • (1964) Plant Physiol , vol.39 , pp. 483-490
    • Tomiyama, K.1    Stahmann, M.A.2
  • 29
    • 0028983813 scopus 로고
    • Improvement of an 'In-Gel' digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing
    • Hellmann U, Wernstedt C, Gonez J and Heldin CH, Improvement of an 'In-Gel' digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing. Anal Biochem 224:451-455 (1995).
    • (1995) Anal Biochem , vol.224 , pp. 451-455
    • Hellmann, U.1    Wernstedt, C.2    Gonez, J.3    Heldin, C.H.4
  • 30
    • 0034072280 scopus 로고    scopus 로고
    • Isolation and partial characterization of a thermostable isoperoxidases from potato (Solanum tuberosum L.) tuber sprouts
    • Boucoiran CFS, Kijne JW and Recourt K, Isolation and partial characterization of a thermostable isoperoxidases from potato (Solanum tuberosum L.) tuber sprouts. J Agric Food Chem 48:701-707 (2000).
    • (2000) J Agric Food Chem , vol.48 , pp. 701-707
    • Boucoiran, C.F.S.1    Kijne, J.W.2    Recourt, K.3
  • 31
    • 34248166268 scopus 로고    scopus 로고
    • Di Venere D, Sergio L, Cardinali A and Kroczynska B, Soluble and bound peroxidases from artichoke: distribution and thermostability, in Polyphenols Communications 2000, ed. by Martens S, Treutter D and Forkmann G. TUM, Munich, pp. 125-126 (2000).
    • Di Venere D, Sergio L, Cardinali A and Kroczynska B, Soluble and bound peroxidases from artichoke: distribution and thermostability, in Polyphenols Communications 2000, ed. by Martens S, Treutter D and Forkmann G. TUM, Munich, pp. 125-126 (2000).
  • 32
    • 0018488111 scopus 로고
    • Amino acid sequence studies of horseradish peroxidase: Amino and carboxyl termini, cyanogen bromide and tryptic fragments, the complete sequence, and some structural characteristics of horseradish peroxidase. C
    • Welinder KG, Amino acid sequence studies of horseradish peroxidase: amino and carboxyl termini, cyanogen bromide and tryptic fragments, the complete sequence, and some structural characteristics of horseradish peroxidase. C. Eur J Biochem 96:483-502 (1979).
    • (1979) Eur J Biochem , vol.96 , pp. 483-502
    • Welinder, K.G.1
  • 33
    • 33746977444 scopus 로고
    • Diversity and conservation of plant peroxidases
    • Simon P, Diversity and conservation of plant peroxidases. Plant Peroxidases Newsl 1:4-7 (1993).
    • (1993) Plant Peroxidases Newsl , vol.1 , pp. 4-7
    • Simon, P.1
  • 36
    • 0027143558 scopus 로고
    • Identification of a basic glycoprotein induced by ethylene in primary leaves of adzuki bean as a cationic peroxidase
    • Ishige F, Mori H, Yamazaki K and Imaseki H, Identification of a basic glycoprotein induced by ethylene in primary leaves of adzuki bean as a cationic peroxidase. Plant Physiol 101:193-199 (1993).
    • (1993) Plant Physiol , vol.101 , pp. 193-199
    • Ishige, F.1    Mori, H.2    Yamazaki, K.3    Imaseki, H.4
  • 37
    • 0029066438 scopus 로고
    • Two pathogen-responsive genes in parsley encode a tyrosine-rich hydroxyproline-rich glycoprotein (hrgp) and an anionic peroxidase
    • Kawalleck P, Schmelzer E, Hahlbrock K and Somssich IE, Two pathogen-responsive genes in parsley encode a tyrosine-rich hydroxyproline-rich glycoprotein (hrgp) and an anionic peroxidase. Mol Gen Genet 247:444-452 (1995).
    • (1995) Mol Gen Genet , vol.247 , pp. 444-452
    • Kawalleck, P.1    Schmelzer, E.2    Hahlbrock, K.3    Somssich, I.E.4
  • 38
    • 0001372765 scopus 로고    scopus 로고
    • Cloning of a soybean cDNA (Accession No. U41657) encoding the abundant anionic seed coat peroxidase
    • Huangpu J, Graham MC and Graham J, Cloning of a soybean cDNA (Accession No. U41657) encoding the abundant anionic seed coat peroxidase. Plant Physiol 110:714 (1996).
    • (1996) Plant Physiol , vol.110 , pp. 714
    • Huangpu, J.1    Graham, M.C.2    Graham, J.3
  • 39
    • 0026844641 scopus 로고
    • cDNA, amino acid and carbohydrate sequence of barley seed-specific peroxidase BP 1
    • Johansson A, Rasmussen SK, Harthill JE and Welinder KG, cDNA, amino acid and carbohydrate sequence of barley seed-specific peroxidase BP 1. Plant Mol Biol 18:1151-1161 (1992).
    • (1992) Plant Mol Biol , vol.18 , pp. 1151-1161
    • Johansson, A.1    Rasmussen, S.K.2    Harthill, J.E.3    Welinder, K.G.4
  • 40
    • 0029878517 scopus 로고    scopus 로고
    • A cluster of genes encoding major isozymes of lignin peroxidase and manganese peroxidase from the white-rot fungus Trametes versicolor
    • Johansson T and Nyman PO, A cluster of genes encoding major isozymes of lignin peroxidase and manganese peroxidase from the white-rot fungus Trametes versicolor. Gene 170:31-38 (1996).
    • (1996) Gene , vol.170 , pp. 31-38
    • Johansson, T.1    Nyman, P.O.2
  • 42
    • 34248178080 scopus 로고    scopus 로고
    • Welinder KG, Topic and detailed literature on molecular, biochemical, and physiological aspects, in Plant Peroxidases 1980-1990, ed. by Penel C, Gaspar T and Greppin H. University of Geneva, Geneva, pp. 1-24 (1992).
    • Welinder KG, Topic and detailed literature on molecular, biochemical, and physiological aspects, in Plant Peroxidases 1980-1990, ed. by Penel C, Gaspar T and Greppin H. University of Geneva, Geneva, pp. 1-24 (1992).
  • 43
    • 0019741905 scopus 로고
    • Polyphenoloxidase and peroxidase in fruits and vegetables
    • Vamos-Vigyazo L, Polyphenoloxidase and peroxidase in fruits and vegetables, in CRC Crit Rev Food Sci Nutr 15:49-127 (1981).
    • (1981) CRC Crit Rev Food Sci Nutr , vol.15 , pp. 49-127
    • Vamos-Vigyazo, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.