메뉴 건너뛰기




Volumn 169, Issue 6, 2005, Pages 1014-1021

Purification and characterization of peroxidases from Withania somnifera (AGB 002) and their ability to oxidize IAA

Author keywords

Ashwagandha; Glycoprotein; IAA (indole 3 acetic acid); Isozymes; Purification; Spectral analysis

Indexed keywords

ACETIC ACID; AMINES; GELS; HYDROPHOBICITY; ION EXCHANGE; PH EFFECTS; PLANTS (BOTANY); POLYACRYLATES; PURIFICATION;

EID: 26444520422     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2005.05.015     Document Type: Article
Times cited : (40)

References (40)
  • 1
    • 0030773115 scopus 로고    scopus 로고
    • From sequence analysis of three novel ascorbate peroxidases from Arabidopsis thaliana to structure, function and evolution of seven types of ascorbate peroxidase
    • H.M. Jespersen, I.V.H.K.J. Aersgard, L. Ostergaard, and K.G. Welinder From sequence analysis of three novel ascorbate peroxidases from Arabidopsis thaliana to structure, function and evolution of seven types of ascorbate peroxidase Biochem. J. 326 1997 305 310
    • (1997) Biochem. J. , vol.326 , pp. 305-310
    • Jespersen, H.M.1    Aersgard, I.V.H.K.J.2    Ostergaard, L.3    Welinder, K.G.4
  • 3
    • 0002565973 scopus 로고
    • Biological roles of plant peroxidases; Known and potential function
    • J. Everse K.E. Everse M.B. Grisham CRC Press Boca Raton
    • A. Campa Biological roles of plant peroxidases; known and potential function J. Everse K.E. Everse M.B. Grisham Peroxidases in Chemistry and Biology vol. 11 1991 CRC Press Boca Raton 25 50
    • (1991) Peroxidases in Chemistry and Biology , vol.11 , pp. 25-50
    • Campa, A.1
  • 4
    • 0000793141 scopus 로고
    • Peroxidase catalysed oxidation of IAA
    • R.L. Hinman, and J. Lang Peroxidase catalysed oxidation of IAA Biochemistry 4 1965 144 158
    • (1965) Biochemistry , vol.4 , pp. 144-158
    • Hinman, R.L.1    Lang, J.2
  • 5
    • 0000215162 scopus 로고
    • The role of peroxidase isoenzyme groups of Nicotiana tabacum in hydrogen peroxide formation
    • M. Mäder, J. Ungemach, and P. Schloss The role of peroxidase isoenzyme groups of Nicotiana tabacum in hydrogen peroxide formation Planta 147 1980 467 470
    • (1980) Planta , vol.147 , pp. 467-470
    • Mäder, M.1    Ungemach, J.2    Schloss, P.3
  • 6
    • 0033002268 scopus 로고    scopus 로고
    • Thiol-dependent degradation of protoporphyrinogen IX by plant peroxidases
    • F.E. Dayan, A.M. Rimando, S.O. Duke, and N.J. Jacobs Thiol-dependent degradation of protoporphyrinogen IX by plant peroxidases FEBS Lett. 444 1999 227 230
    • (1999) FEBS Lett. , vol.444 , pp. 227-230
    • Dayan, F.E.1    Rimando, A.M.2    Duke, S.O.3    Jacobs, N.J.4
  • 7
    • 0030186876 scopus 로고    scopus 로고
    • Tobacco anionic peroxidase overexpressed in transgenic plants: Aerobic oxidation of indole-3-acetic acid
    • I.G. Gazaryan, and M. Lagrimini Tobacco anionic peroxidase overexpressed in transgenic plants: aerobic oxidation of indole-3-acetic acid Phytochemistry 42 1996 1271 1278
    • (1996) Phytochemistry , vol.42 , pp. 1271-1278
    • Gazaryan, I.G.1    Lagrimini, M.2
  • 8
    • 0037123359 scopus 로고    scopus 로고
    • Analysis and expression of class 111 peroxidase large gene family in Arabidopsis thaliana
    • M. Tognolli, C. Penel, H. Greppin, and P. Simon Analysis and expression of class 111 peroxidase large gene family in Arabidopsis thaliana Gene 288 2002 129 138
    • (2002) Gene , vol.288 , pp. 129-138
    • Tognolli, M.1    Penel, C.2    Greppin, H.3    Simon, P.4
  • 10
    • 0032973059 scopus 로고    scopus 로고
    • Clinical and preclinical modulation of chemotherapy-induced toxicity in patients with cancer
    • H. Klaas, J.F. Van der Vijgh Wim, and B.J. Vermorken Clinical and preclinical modulation of chemotherapy-induced toxicity in patients with cancer Drugs 57 1999 133 155
    • (1999) Drugs , vol.57 , pp. 133-155
    • Klaas, H.1    Van Der Vijgh Wim, J.F.2    Vermorken, B.J.3
  • 12
    • 0000809327 scopus 로고
    • Pharmocology of Withania somnifera (Linn Dunal): A review
    • R. Asthana, and M.K. Raina Pharmocology of Withania somnifera (Linn Dunal): a review Indian Drugs 26 1989 199 205
    • (1989) Indian Drugs , vol.26 , pp. 199-205
    • Asthana, R.1    Raina, M.K.2
  • 13
    • 0032756875 scopus 로고    scopus 로고
    • Effect of Withania somnifera on cytokine production in normal and cyclophosphamide treated mice
    • L. Davis, and G. Kuttan Effect of Withania somnifera on cytokine production in normal and cyclophosphamide treated mice Immunopharmacol. Immunotoxicol. 21 1999 695 703
    • (1999) Immunopharmacol. Immunotoxicol. , vol.21 , pp. 695-703
    • Davis, L.1    Kuttan, G.2
  • 14
    • 0029819884 scopus 로고    scopus 로고
    • Withania somnifera Dunal (Ashwagandha): Potential plant source of a promising drug for cancer chemotherapy and radiosensitization
    • P. Uma Devi Withania somnifera Dunal (Ashwagandha): potential plant source of a promising drug for cancer chemotherapy and radiosensitization Indian J. Exp. Biol. 34 1996 927 932
    • (1996) Indian J. Exp. Biol. , vol.34 , pp. 927-932
    • Uma Devi, P.1
  • 16
    • 0347753599 scopus 로고    scopus 로고
    • Immunoprotection by botanical drugs in cancer chemotherapy
    • S. Diwanay, D. Chitre, and B. Patwardhan Immunoprotection by botanical drugs in cancer chemotherapy J. Ethnopharmacol. 90 2004 49 55
    • (2004) J. Ethnopharmacol. , vol.90 , pp. 49-55
    • Diwanay, S.1    Chitre, D.2    Patwardhan, B.3
  • 17
    • 77957006400 scopus 로고
    • S.P. Colowick N.O. Kaplan Academic Press New York
    • B. Chance, and M. Maehly S.P. Colowick N.O. Kaplan Methods in Enzymology vol. 2 1955 Academic Press New York 764
    • (1955) Methods in Enzymology , vol.2 , pp. 764
    • Chance, B.1    Maehly, M.2
  • 19
    • 84963172223 scopus 로고
    • Properties of IAA oxidase from ripening tomatoes
    • A.E. Huang, and N.F. Haard Properties of IAA oxidase from ripening tomatoes J. Food Biochem. 1 1977 93 110
    • (1977) J. Food Biochem. , vol.1 , pp. 93-110
    • Huang, A.E.1    Haard, N.F.2
  • 20
    • 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
  • 21
  • 22
    • 0001218618 scopus 로고
    • Progress and prospects in the use of peroxidase to study cell development
    • R.B. van Huystee, and W.L. Carins Progress and prospects in the use of peroxidase to study cell development Phytochemistry 21 1982 1843 1847
    • (1982) Phytochemistry , vol.21 , pp. 1843-1847
    • Van Huystee, R.B.1    Carins, W.L.2
  • 24
    • 0003320513 scopus 로고
    • Some molecular aspects of plant peroxidase biosynthetic studies
    • R.B. van Huystee Some molecular aspects of plant peroxidase biosynthetic studies Ann. Rev. Plant Physiol. 38 1987 205 219
    • (1987) Ann. Rev. Plant Physiol. , vol.38 , pp. 205-219
    • Van Huystee, R.B.1
  • 25
    • 0027162273 scopus 로고
    • A study on glycosylation of cationic peanut peroxidase
    • L. Wan, and R.B. van Huystee A study on glycosylation of cationic peanut peroxidase Biochem. Biophys. Res. Commun. 194 1993 1398 1405
    • (1993) Biochem. Biophys. Res. Commun. , vol.194 , pp. 1398-1405
    • Wan, L.1    Van Huystee, R.B.2
  • 27
    • 0002154654 scopus 로고
    • J. Everse K.E. Everse M.B. Grisham CRC Press Boca Raton, FL
    • H.B. Dunford J. Everse K.E. Everse M.B. Grisham Peroxidases in Chemistry and Biology vol. 2 1991 CRC Press Boca Raton, FL 1 24
    • (1991) Peroxidases in Chemistry and Biology , vol.2 , pp. 1-24
    • Dunford, H.B.1
  • 28
    • 0034088553 scopus 로고    scopus 로고
    • Functional expression of horseradish peroxidase in Saccharomyces cerevisiae and Pichia pastoris
    • B. Morawski, Z. Lin, P. Cirino, H. Joo, G. Bandara, and F.H. Arnold Functional expression of horseradish peroxidase in Saccharomyces cerevisiae and Pichia pastoris Protein Eng. 13 2000 377 384
    • (2000) Protein Eng. , vol.13 , pp. 377-384
    • Morawski, B.1    Lin, Z.2    Cirino, P.3    Joo, H.4    Bandara, G.5    Arnold, F.H.6
  • 29
    • 26444497523 scopus 로고
    • A comparison between 3,5-diiodo-4-hydroxybenzoic acid and 2,3,5-triiodobenzoic acid. 1. Effects on growth and development of maize roots
    • R. Beffa, H.V. Maetin, and P.-E. Pilet A comparison between 3,5-diiodo-4-hydroxybenzoic acid and 2,3,5-triiodobenzoic acid. 1. Effects on growth and development of maize roots Physiol. Plant 71 1987 30 36
    • (1987) Physiol. Plant , vol.71 , pp. 30-36
    • Beffa, R.1    Maetin, H.V.2    Pilet, P.-E.3
  • 30
    • 0026810618 scopus 로고
    • Characterization of two forms of cationic peroxidase from cultured peanut cells
    • J.P. O'Donnell, L. Wan, and R.B. van Huystee Characterization of two forms of cationic peroxidase from cultured peanut cells Biochem. Cell Biol. 70 1992 166 169
    • (1992) Biochem. Cell Biol. , vol.70 , pp. 166-169
    • O'Donnell, J.P.1    Wan, L.2    Van Huystee, R.B.3
  • 31
    • 0019741905 scopus 로고
    • Polyphenol oxidase and peroxidase in fruits and vegetables
    • L. Vamos-Vigyazo Polyphenol oxidase and peroxidase in fruits and vegetables CRC Crit. Rev. Food Sci. Nutr. 15 1981 49 127
    • (1981) CRC Crit. Rev. Food Sci. Nutr. , vol.15 , pp. 49-127
    • Vamos-Vigyazo, L.1
  • 32
    • 0036230003 scopus 로고    scopus 로고
    • Oil palm fruit peroxidase: Purification and characterization
    • S.S. Deepa, and C. Arumughan Oil palm fruit peroxidase: purification and characterization J. Food Sci. Technol. 39 2002 8 13
    • (2002) J. Food Sci. Technol. , vol.39 , pp. 8-13
    • Deepa, S.S.1    Arumughan, C.2
  • 33
    • 33750092016 scopus 로고
    • Coconut peroxidase isoenzymes: Isolation, partial purification and physicochemical properties
    • C.V. Mujer, E.M.T. Menzdoza, and D.A. Ramirez Coconut peroxidase isoenzymes: isolation, partial purification and physicochemical properties Phytochemistry 22 1983 1335 1340
    • (1983) Phytochemistry , vol.22 , pp. 1335-1340
    • Mujer, C.V.1    Menzdoza, E.M.T.2    Ramirez, D.A.3
  • 34
    • 84907421681 scopus 로고
    • Peroxidase from strawberry fruit: Partial purification and determination of some properties
    • P.M. Civello, G.A. Martinez, A.R. Chaves, and M.C. Anon Peroxidase from strawberry fruit: partial purification and determination of some properties J. Agric. Food Chem. 43 1995 2596 2601
    • (1995) J. Agric. Food Chem. , vol.43 , pp. 2596-2601
    • Civello, P.M.1    Martinez, G.A.2    Chaves, A.R.3    Anon, M.C.4
  • 35
    • 38249015817 scopus 로고
    • Purification and characterization of anionic peroxidase from cotton
    • B.A. Triplett, and J.E. Melton Purification and characterization of anionic peroxidase from cotton Plant Sci. 81 1992 147 154
    • (1992) Plant Sci. , vol.81 , pp. 147-154
    • Triplett, B.A.1    Melton, J.E.2
  • 36
    • 34250144281 scopus 로고
    • The relationship between oxidase activity, peroxidase activity, hydrogen peroxide and phenolic compounds in the degradation of IAA in vitro
    • H.J. Grambow, and B. Langenbeck-Schwich The relationship between oxidase activity, peroxidase activity, hydrogen peroxide and phenolic compounds in the degradation of IAA in vitro Planta 157 1983 131 137
    • (1983) Planta , vol.157 , pp. 131-137
    • Grambow, H.J.1    Langenbeck-Schwich, B.2
  • 37
    • 0000956054 scopus 로고
    • Hydrogen peroxide-mediated oxidation of IAA by tomato peroxidase and molecular oxygen
    • D.M. Kokkinakis, and J.L. Brooks Hydrogen peroxide-mediated oxidation of IAA by tomato peroxidase and molecular oxygen Plant Physiol. 64 1979 220 223
    • (1979) Plant Physiol. , vol.64 , pp. 220-223
    • Kokkinakis, D.M.1    Brooks, J.L.2
  • 38
    • 0000449737 scopus 로고
    • Isolation and characterization of wheat peroxidase isoenzymes B1
    • Z. Zmrhal, and I. Machackova Isolation and characterization of wheat peroxidase isoenzymes B1 Phytochemistry 17 1978 1517 1520
    • (1978) Phytochemistry , vol.17 , pp. 1517-1520
    • Zmrhal, Z.1    MacHackova, I.2
  • 39
    • 0002532436 scopus 로고
    • Compartmentation of peroxidase isozymes in plant cells
    • C. Penel Th. Gasper H. Greppin University of Geneva
    • M. Mäder Compartmentation of peroxidase isozymes in plant cells C. Penel Th. Gasper H. Greppin Plant Peroxidases 1980-1990 1992 University of Geneva 37 46
    • (1992) Plant Peroxidases 1980-1990 , pp. 37-46
    • Mäder, M.1
  • 40
    • 84986533755 scopus 로고
    • Oxidation of indole-3-acetic acid by an apparently homogeneous peroxidase from the flavedo of Washington avel oranges (Citrus sinensis)
    • J. Chamarro, and I. Monila Oxidation of indole-3-acetic acid by an apparently homogeneous peroxidase from the flavedo of Washington avel oranges (Citrus sinensis) J. Food Biochem. 13 1989 361 375
    • (1989) J. Food Biochem. , vol.13 , pp. 361-375
    • Chamarro, J.1    Monila, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.