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Volumn 48, Issue 9, 2010, Pages 758-763

Purification and kinetic characterization of the liverwort Pallavicinia lyelli (Hook.) S. Gray. cytosolic ascorbate peroxidase

Author keywords

Ascorbate peroxidase; Characterization; Hydrogen peroxide; Kinetics; Pallavicinia lyelli; Purification

Indexed keywords

PALLAVICINIA;

EID: 77955660230     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2010.06.004     Document Type: Article
Times cited : (14)

References (22)
  • 1
    • 0001844190 scopus 로고
    • Copper enzymes in the isolated chloroplasts, polyphenol oxidase in Beta vulgaris
    • Arnon D.I. Copper enzymes in the isolated chloroplasts, polyphenol oxidase in Beta vulgaris. Plant Physiol. 1949, 24:1-15.
    • (1949) Plant Physiol. , vol.24 , pp. 1-15
    • Arnon, D.I.1
  • 2
    • 0031906754 scopus 로고    scopus 로고
    • Identification of two cytosolic ascorbate peroxidase cDNAs from soybean leaves and characterization of their products by functional expression in E. coli
    • Caldwell C.R., Turano F.J., McMahon M.B. Identification of two cytosolic ascorbate peroxidase cDNAs from soybean leaves and characterization of their products by functional expression in E. coli. Planta 1998, 204:120-126.
    • (1998) Planta , vol.204 , pp. 120-126
    • Caldwell, C.R.1    Turano, F.J.2    McMahon, M.B.3
  • 3
    • 33745314723 scopus 로고
    • Ascorbate peroxidase in tea leaves: occurrence of two isozymes and the differences in their enzymatic and molecular properties
    • Chen G.X., Asada K. Ascorbate peroxidase in tea leaves: occurrence of two isozymes and the differences in their enzymatic and molecular properties. Plant Cell Physiol. 1989, 30:987-998.
    • (1989) Plant Cell Physiol. , vol.30 , pp. 987-998
    • Chen, G.X.1    Asada, K.2
  • 4
    • 0000019955 scopus 로고
    • Purification, properties, and distribution of ascorbate peroxidase in legume root nodules
    • Dalton D.A., Hanus F.J., Russell S.A., Evans H.J. Purification, properties, and distribution of ascorbate peroxidase in legume root nodules. Plant Physiol. 1987, 83:789-794.
    • (1987) Plant Physiol. , vol.83 , pp. 789-794
    • Dalton, D.A.1    Hanus, F.J.2    Russell, S.A.3    Evans, H.J.4
  • 5
    • 0000412725 scopus 로고
    • Chloroplast superoxide and hydrogen peroxide scavenging systems from pea leaves: seasonal variation
    • Gillham D.J., Dodge A.D. Chloroplast superoxide and hydrogen peroxide scavenging systems from pea leaves: seasonal variation. Plant Sci. 1987, 50:105-109.
    • (1987) Plant Sci. , vol.50 , pp. 105-109
    • Gillham, D.J.1    Dodge, A.D.2
  • 6
    • 0000918942 scopus 로고
    • Monodehydroascorbate reductase in spinach chloroplasts and its participation in regeneration of ascorbate for scavenging hydrogen peroxide
    • Hossain M.A., Nakano Y., Asada K. Monodehydroascorbate reductase in spinach chloroplasts and its participation in regeneration of ascorbate for scavenging hydrogen peroxide. Plant Cell Physiol. 1984, 25:385-395.
    • (1984) Plant Cell Physiol. , vol.25 , pp. 385-395
    • Hossain, M.A.1    Nakano, Y.2    Asada, K.3
  • 7
    • 0029895579 scopus 로고    scopus 로고
    • Molecular characterization of Euglena ascorbate peroxidase using monoclonal antibody
    • Ishikawa T., Takeda T., Kohno H., Shigeoka S. Molecular characterization of Euglena ascorbate peroxidase using monoclonal antibody. Biochim. Biophys. Acta 1996, 1290:69-75.
    • (1996) Biochim. Biophys. Acta , vol.1290 , pp. 69-75
    • Ishikawa, T.1    Takeda, T.2    Kohno, H.3    Shigeoka, S.4
  • 8
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 9
    • 0034623448 scopus 로고    scopus 로고
    • Chilling stress-induced changes of antioxidant enzymes in the leaves of cucumber: in gel enzyme activity assays
    • Lee D.H., Lee C.B. Chilling stress-induced changes of antioxidant enzymes in the leaves of cucumber: in gel enzyme activity assays. Plant Sci. 2000, 159:75-85.
    • (2000) Plant Sci. , vol.159 , pp. 75-85
    • Lee, D.H.1    Lee, C.B.2
  • 10
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constant
    • Lineweaver H., Burk D. The determination of enzyme dissociation constant. J. Am. Chem. Soc. 1934, 56:658-661.
    • (1934) J. Am. Chem. Soc. , vol.56 , pp. 658-661
    • Lineweaver, H.1    Burk, D.2
  • 11
    • 0025975577 scopus 로고
    • Oxidative stress responses and shock proteins in the unicellular cyanobacterium Synechococcus R2 (PCC-7942)
    • Mittler R., Tel-Or E. Oxidative stress responses and shock proteins in the unicellular cyanobacterium Synechococcus R2 (PCC-7942). Arch. Microbiol. 1991, 155:125-131.
    • (1991) Arch. Microbiol. , vol.155 , pp. 125-131
    • Mittler, R.1    Tel-Or, E.2
  • 12
    • 0000121196 scopus 로고
    • Purification and characterization of pea cytosolic ascorbate peroxidase
    • Mittler R., Zilinskas B.A. Purification and characterization of pea cytosolic ascorbate peroxidase. Plant Physiol. 1991, 97:962-968.
    • (1991) Plant Physiol. , vol.97 , pp. 962-968
    • Mittler, R.1    Zilinskas, B.A.2
  • 13
    • 0000121196 scopus 로고
    • Regulation of pea cytosolic ascorbate peroxidase and other anioxidant enzymes during the progression of drought stress and following recovery from drought
    • Mittler R., Zilinskas B.A. Regulation of pea cytosolic ascorbate peroxidase and other anioxidant enzymes during the progression of drought stress and following recovery from drought. Plant Physiol. 1991, 97:962-968.
    • (1991) Plant Physiol. , vol.97 , pp. 962-968
    • Mittler, R.1    Zilinskas, B.A.2
  • 14
    • 0001073890 scopus 로고
    • Purification and molecular properties of the thylakoid-bound ascorbate peroxidase in spinach chloroplasts
    • Miyake C., Cao W.H., Asada K. Purification and molecular properties of the thylakoid-bound ascorbate peroxidase in spinach chloroplasts. Plant Cell Physiol. 1993, 34:881-889.
    • (1993) Plant Cell Physiol. , vol.34 , pp. 881-889
    • Miyake, C.1    Cao, W.H.2    Asada, K.3
  • 15
    • 77957183372 scopus 로고
    • Purification of ascorbate peroxidase in spinach chloroplasts; its inactivation in ascorbate-depleted medium and reactivation by monodehydroascorbate radical
    • Nakano Y., Asada K. Purification of ascorbate peroxidase in spinach chloroplasts; its inactivation in ascorbate-depleted medium and reactivation by monodehydroascorbate radical. Plant Cell Physiol. 1987, 28:131-140.
    • (1987) Plant Cell Physiol. , vol.28 , pp. 131-140
    • Nakano, Y.1    Asada, K.2
  • 16
    • 0037311726 scopus 로고    scopus 로고
    • Two APX from broccoli: identification, expression and characterization of their recombinant proteins
    • Nishikawa F., Kato M., Wang R., Hyodo H., Ikoma Y., Sugiura M., Yano M. Two APX from broccoli: identification, expression and characterization of their recombinant proteins. Postharvest Biol. Technol. 2003, 27:147-156.
    • (2003) Postharvest Biol. Technol. , vol.27 , pp. 147-156
    • Nishikawa, F.1    Kato, M.2    Wang, R.3    Hyodo, H.4    Ikoma, Y.5    Sugiura, M.6    Yano, M.7
  • 19
    • 0019325168 scopus 로고
    • Purification and some properties of L-ascorbic acid-specific peroxidase in Euglena gracilis
    • Shigeoka S., Nakano Y., Kitaoka S. Purification and some properties of L-ascorbic acid-specific peroxidase in Euglena gracilis. Arch. Biochem. Biophys. 1980, 201:121-127.
    • (1980) Arch. Biochem. Biophys. , vol.201 , pp. 121-127
    • Shigeoka, S.1    Nakano, Y.2    Kitaoka, S.3
  • 20
    • 0023142291 scopus 로고
    • Properties of monodchydroascorbate rcductase and dehydroascorbate reductase and their participation in the regeneration of ascorbate in Euglena gracilis
    • Shigeoka S., Yasumoto R., Onishi T., Nakano Y., Kitaoka S. Properties of monodchydroascorbate rcductase and dehydroascorbate reductase and their participation in the regeneration of ascorbate in Euglena gracilis. J. Gen. Microbiol. 1987, 133:227-232.
    • (1987) J. Gen. Microbiol. , vol.133 , pp. 227-232
    • Shigeoka, S.1    Yasumoto, R.2    Onishi, T.3    Nakano, Y.4    Kitaoka, S.5
  • 21
    • 0001362389 scopus 로고
    • The presence of enzymes related to glutathione metabolism and oxygen metabolism in Chlamydomonas reinhardtii
    • Takeda T., Shigeoka S., Hirayama O., Mitsnnaga T. The presence of enzymes related to glutathione metabolism and oxygen metabolism in Chlamydomonas reinhardtii. Biosci. Biotechnol. Biochem. 1992, 56:1662-1663.
    • (1992) Biosci. Biotechnol. Biochem. , vol.56 , pp. 1662-1663
    • Takeda, T.1    Shigeoka, S.2    Hirayama, O.3    Mitsnnaga, T.4
  • 22
    • 12944305786 scopus 로고
    • Superfamily of plant, fungal and bacterial peroxidases
    • Welinder K.G. Superfamily of plant, fungal and bacterial peroxidases. Curr. Opin. Struct. Biol. 1992, 2:388-393.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 388-393
    • Welinder, K.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.