메뉴 건너뛰기




Volumn 54, Issue 26, 2006, Pages 9888-9894

Purification and characterization of windmill palm tree (Trachycarpus fortunei) peroxidase

Author keywords

Localization; Palm; Peroxidase; Purification; Stability; Substrate specificity

Indexed keywords

CALCIUM; HYDROGEN PEROXIDE; PEROXIDASE;

EID: 33846545723     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf0615193     Document Type: Article
Times cited : (17)

References (38)
  • 2
    • 0004277276 scopus 로고    scopus 로고
    • Humana Press: Totowa, NJ, 436 pp
    • Crowther, J. R. ELISA Guidebook; Humana Press: Totowa, NJ, 2001; 436 pp.
    • (2001) ELISA Guidebook
    • Crowther, J.R.1
  • 3
    • 0033121058 scopus 로고    scopus 로고
    • Recent biotechnological developments in the use of peroxidase
    • Colonna, S.; Gaggero, N.; Richelmi, C.; Pasta, P. Recent biotechnological developments in the use of peroxidase. Trends Biotechnol. 1999, 17, 163-168.
    • (1999) Trends Biotechnol , vol.17 , pp. 163-168
    • Colonna, S.1    Gaggero, N.2    Richelmi, C.3    Pasta, P.4
  • 4
    • 0037697761 scopus 로고    scopus 로고
    • 2O production by plant cells: Truths and clues
    • 2O production by plant cells: truths and clues. Curr. Topics Phytochem. 2000, 3, 197-202.
    • (2000) Curr. Topics Phytochem , vol.3 , pp. 197-202
    • Ros Barceló, A.1
  • 5
    • 15844369555 scopus 로고    scopus 로고
    • A comparative study of the purity, enzyme activity, and inactivation by hydrogen peroxide of commercially available horseradish peroxidase isoenzymes A and C
    • Hiner, A. N. P.; Hernández-Ruíz, J.; Arnao, M. D.; Gracía-Cánovas, F.; Acosta, M. A comparative study of the purity, enzyme activity, and inactivation by hydrogen peroxide of commercially available horseradish peroxidase isoenzymes A and C. Biotechnol. Bioeng. 1996, 50, 655-662.
    • (1996) Biotechnol. Bioeng , vol.50 , pp. 655-662
    • Hiner, A.N.P.1    Hernández-Ruíz, J.2    Arnao, M.D.3    Gracía-Cánovas, F.4    Acosta, M.5
  • 6
    • 0029842169 scopus 로고    scopus 로고
    • Unusual thermal stability of soybean peroxidase
    • McEldoon, J. P.; Dordick, J. S. Unusual thermal stability of soybean peroxidase. Biotechnol. Prog. 1996, 12, 555-558.
    • (1996) Biotechnol. Prog , vol.12 , pp. 555-558
    • McEldoon, J.P.1    Dordick, J.S.2
  • 7
    • 0030111427 scopus 로고    scopus 로고
    • Purification and unusual kinetic properties of a tobacco anionic peroxidase
    • Gazaryan, I. G.; Lagrimini, L. M. Purification and unusual kinetic properties of a tobacco anionic peroxidase. Phytochemistry 1996, 41, 1029-1034.
    • (1996) Phytochemistry , vol.41 , pp. 1029-1034
    • Gazaryan, I.G.1    Lagrimini, L.M.2
  • 8
    • 0031200793 scopus 로고    scopus 로고
    • Purification and characterization of a novel class III peroxidase isoenzyme from tea leaves
    • Kvaratskhelia, M.; Winkel, C.; Thorneley, R. N. F. Purification and characterization of a novel class III peroxidase isoenzyme from tea leaves. Plant Physiol. 1997, 114, 1237-1245.
    • (1997) Plant Physiol , vol.114 , pp. 1237-1245
    • Kvaratskhelia, M.1    Winkel, C.2    Thorneley, R.N.F.3
  • 11
    • 17144369127 scopus 로고    scopus 로고
    • Purification and partial characterization of broccoli (Brassica oleracea var. italica) peroxidases
    • Thongsook, T.; Barrett, D. M. Purification and partial characterization of broccoli (Brassica oleracea var. italica) peroxidases. J. Agric. Food Chem. 2005, 53, 3206-3214.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 3206-3214
    • Thongsook, T.1    Barrett, D.M.2
  • 12
    • 0033776052 scopus 로고    scopus 로고
    • Purification and stability of peroxidase of African oil palm Elaies guineensis
    • Sakharov, I. Yu.; Castillo León, J.; Ariza, J. C.; Galaev, I. Yu. Purification and stability of peroxidase of African oil palm Elaies guineensis. Bioseparation 2000, 9, 125-132.
    • (2000) Bioseparation , vol.9 , pp. 125-132
    • Sakharov, I.Y.1    Castillo León, J.2    Ariza, J.C.3    Galaev, I.Y.4
  • 13
    • 0034783572 scopus 로고    scopus 로고
    • Peroxidase from leaves of royal palm tree Roystonea regia: Purification and properties
    • Sakharov, I. Yu.; Vesga Blanco, M. K.; Galaev, I. Yu.; Sakharova, I. V.; Pletjushkina, O. Yu. Peroxidase from leaves of royal palm tree Roystonea regia: purification and properties. Plant Sci. 2001, 161, 853-860.
    • (2001) Plant Sci , vol.161 , pp. 853-860
    • Sakharov, I.Y.1    Vesga Blanco, M.K.2    Galaev, I.Y.3    Sakharova, I.V.4    Pletjushkina, O.Y.5
  • 14
    • 0036847758 scopus 로고    scopus 로고
    • Purification and characterization of soluble peroxidase from oil palm (Elaeis guineensis Jacq.) leaf
    • Deepa, S. S.; Arumughan, C. Purification and characterization of soluble peroxidase from oil palm (Elaeis guineensis Jacq.) leaf. Phytochemistry 2002, 61, 503-511.
    • (2002) Phytochemistry , vol.61 , pp. 503-511
    • Deepa, S.S.1    Arumughan, C.2
  • 15
    • 0346058017 scopus 로고    scopus 로고
    • Purification and characterization of membrane-bound peroxidases from Metroxylon sagu
    • Onsa, G. H.; bin Saari, N.; Selamat, J.; Bakar, J. Purification and characterization of membrane-bound peroxidases from Metroxylon sagu. Food Chem. 2004, 85, 365-376.
    • (2004) Food Chem , vol.85 , pp. 365-376
    • Onsa, G.H.1    bin Saari, N.2    Selamat, J.3    Bakar, J.4
  • 16
    • 0037194336 scopus 로고    scopus 로고
    • Extremely high stability of African oil palm tree peroxidase
    • Sakharov, I. Yu.; Sakharova, I. V. Extremely high stability of African oil palm tree peroxidase. Biochim. Biophys. Acta 2002, 1598, 108-114.
    • (2002) Biochim. Biophys. Acta , vol.1598 , pp. 108-114
    • Sakharov, I.Y.1    Sakharova, I.V.2
  • 21
    • 0033027809 scopus 로고    scopus 로고
    • Sakharov, I. Yu.; Bautista, Ardila, G. Variation of peroxidase activity in cacao beans during their ripering, fermentation and drying. Food Chem. 1999, 65, 51-54.
    • Sakharov, I. Yu.; Bautista, Ardila, G. Variation of peroxidase activity in cacao beans during their ripering, fermentation and drying. Food Chem. 1999, 65, 51-54.
  • 22
    • 84907126001 scopus 로고
    • A method of retaining phloroglucinol proof of lignin
    • Speer, E. O. A method of retaining phloroglucinol proof of lignin. Stain Technol. 1987, 62, 279-280.
    • (1987) Stain Technol , vol.62 , pp. 279-280
    • Speer, E.O.1
  • 23
    • 85044700095 scopus 로고    scopus 로고
    • Autofluorescence of intact Equisetum arvense L. spores during their development
    • Roshchina, V. V.; Melnikova, E. V.; Iashin, V. A.; Karnaukhov, V. N. Autofluorescence of intact Equisetum arvense L. spores during their development. Biofizika (Moscow) 2002, 47, 318-324.
    • (2002) Biofizika (Moscow) , vol.47 , pp. 318-324
    • Roshchina, V.V.1    Melnikova, E.V.2    Iashin, V.A.3    Karnaukhov, V.N.4
  • 25
    • 0002145720 scopus 로고
    • Calcium and peroxidase derived from cultured peanut cells
    • Hu, C.; Lee, D.; Chibbar, R. N.; van Huystee, R. B. Calcium and peroxidase derived from cultured peanut cells. Physiol. Plant 1987, 70, 99-102.
    • (1987) Physiol. Plant , vol.70 , pp. 99-102
    • Hu, C.1    Lee, D.2    Chibbar, R.N.3    van Huystee, R.B.4
  • 26
    • 33846559458 scopus 로고    scopus 로고
    • Smulevich, G. A comparative analysis of the structures of various peroxidases as defined by resonance Raman and electronic absorption spectroscopies. In Plant Peroxidases. Biochemistry and Physiology; Obinger, C., Burner, U., Ebermann, R., Penel, C., Greppin, H., Eds.; University of Agriculture of Vienna and University of Geneva: Geneva, Switzerland, and Vienna, Austria, 1996; pp 13-19.
    • Smulevich, G. A comparative analysis of the structures of various peroxidases as defined by resonance Raman and electronic absorption spectroscopies. In Plant Peroxidases. Biochemistry and Physiology; Obinger, C., Burner, U., Ebermann, R., Penel, C., Greppin, H., Eds.; University of Agriculture of Vienna and University of Geneva: Geneva, Switzerland, and Vienna, Austria, 1996; pp 13-19.
  • 27
    • 23944527027 scopus 로고    scopus 로고
    • Structural determinants of plant peroxidase function
    • Veith, N. C. Structural determinants of plant peroxidase function. Phytochem. Rev. 2004, 3, 3-18.
    • (2004) Phytochem. Rev , vol.3 , pp. 3-18
    • Veith, N.C.1
  • 30
    • 0028447617 scopus 로고
    • The abscisic acid induction of a novel peroxidase is antagonized by cytokinin in Spirodela polyrrhiza L
    • Chaloupkova, K.; Smart, C. C. The abscisic acid induction of a novel peroxidase is antagonized by cytokinin in Spirodela polyrrhiza L. Plant Physiol. 1994, 105, 497-507.
    • (1994) Plant Physiol , vol.105 , pp. 497-507
    • Chaloupkova, K.1    Smart, C.C.2
  • 31
    • 33846549680 scopus 로고
    • Cloning and sequencing flax (Linum usitatissimum) peroxidases
    • Tyson, H. Cloning and sequencing flax (Linum usitatissimum) peroxidases. Plant Peroxidase Newsl. 1993, 14-18.
    • (1993) Plant Peroxidase Newsl , pp. 14-18
    • Tyson, H.1
  • 32
    • 0030966273 scopus 로고    scopus 로고
    • Molecular cloning and characterization of cDNAs for anionic and neutral peroxidases from suspension cultured-cells of sweet potato and their differential expression in response to stress
    • Huh, G.-H.; Lee, S. J.; Bae, Y.-S.; Liu, J. R.; Kwak, S.-S. Molecular cloning and characterization of cDNAs for anionic and neutral peroxidases from suspension cultured-cells of sweet potato and their differential expression in response to stress. Mol. Gen. Genet. 1997, 255, 382-391.
    • (1997) Mol. Gen. Genet , vol.255 , pp. 382-391
    • Huh, G.-H.1    Lee, S.J.2    Bae, Y.-S.3    Liu, J.R.4    Kwak, S.-S.5
  • 33
    • 0002154654 scopus 로고
    • Horseradish peroxidase: Structure and kinetic properties
    • Everse, J, Everse, K. E, Grisham, M. B, Eds, CRC Press: Boca Raton, FL
    • Dunford, H. B. Horseradish peroxidase: structure and kinetic properties. In Peroxidase in Chemistry and Biology; Everse, J., Everse, K. E., Grisham, M. B., Eds.; CRC Press: Boca Raton, FL, 1991; pp 1-24.
    • (1991) Peroxidase in Chemistry and Biology , pp. 1-24
    • Dunford, H.B.1
  • 34
    • 0026093912 scopus 로고
    • A comparative study of peroxidases from horseradish and Arthromyces ramonus as labels in luminol-mediated chemiluminescent assays
    • Kim, B. B.; Pisarev, V. V.; Egorov, A. M. A comparative study of peroxidases from horseradish and Arthromyces ramonus as labels in luminol-mediated chemiluminescent assays. Anal. Biochem. 1991, 199, 1-6.
    • (1991) Anal. Biochem , vol.199 , pp. 1-6
    • Kim, B.B.1    Pisarev, V.V.2    Egorov, A.M.3
  • 35
    • 22544476518 scopus 로고    scopus 로고
    • Soybean peroxidase-catalyzed oxidation of luminol by hydrogen peroxide
    • Alpeeva, I. S.; Sakharov, I. Yu. Soybean peroxidase-catalyzed oxidation of luminol by hydrogen peroxide. J. Agric. Food Chem. 2005, 53, 5784-5788.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 5784-5788
    • Alpeeva, I.S.1    Sakharov, I.Y.2
  • 36
  • 37
    • 34247880239 scopus 로고    scopus 로고
    • Luminol-hydrogen peroxide chemiluminescence produced by sweet potato peroxidase
    • press available by internet doi: 10.1002/bio.931
    • Alpeeva, I. S.; Sakharov, I. Yu. Luminol-hydrogen peroxide chemiluminescence produced by sweet potato peroxidase. Luminescence 2006, in press (available by internet doi: 10.1002/bio.931).
    • (2006) Luminescence
    • Alpeeva, I.S.1    Sakharov, I.Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.