메뉴 건너뛰기




Volumn 30, Issue 7, 1989, Pages 987-998

Ascorbate peroxidase in tea leaves: Occurrence of two isozymes and the differences in their enzymatic and molecular properties

Author keywords

Ascorbate peroxidase; Chloroplast; Hydrogen peroxide; Isozyme; Scavenger; Tea (Camellia sinensis).

Indexed keywords


EID: 33745314723     PISSN: 00320781     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (665)

References (38)
  • 1
    • 0013769988 scopus 로고
    • Estimation of the molecular weights of proteins by sephadex gel-filtration
    • Andrews, P. (1964) Estimation of the molecular weights of proteins by Sephadex gel-filtration. Biochem. J. 91: 222–233.
    • (1964) Biochem. J , vol.91 , pp. 222-233
    • Andrews, P.1
  • 2
    • 0016378961 scopus 로고
    • Univalent reduction of molecular oxygen by spinach chloroplasts on illumination
    • Asada, K., Kiso, K. and Yoshikawa, K. (1974) Univalent reduction of molecular oxygen by spinach chloroplasts on illumination. J. Biol. Chem. 249: 2175–2181.
    • (1974) J. Biol. Chem , vol.249 , pp. 2175-2181
    • Asada, K.1    Kiso, K.2    Yoshikawa, K.3
  • 3
    • 3543108071 scopus 로고
    • Purification and properties of cytochrome c and two peroxidases from spinach leaves
    • Asada, K. and Takahashi, M. (1971) Purification and properties of cytochrome c and two peroxidases from spinach leaves. Plant Cell Physiol. 12: 361–375.
    • (1971) Plant Cell Physiol , vol.12 , pp. 361-375
    • Asada, K.1    Takahashi, M.2
  • 4
    • 0000682385 scopus 로고
    • Production and scavenging of active oxygen in photosynthesis
    • In, Edited by Kyle, D. J., Osmond, C. B. and Arntzen, C. J, Elsevier, Amsterdam
    • Asada, K. and Takahashi, M. (1987) Production and scavenging of active oxygen in photosynthesis. In Photoinhibition. Edited by Kyle, D. J., Osmond, C. B. and Arntzen, C. J. pp. 227–287. Elsevier, Amsterdam.
    • (1987) Photoinhibition , pp. 227-287
    • Asada, K.1    Takahashi, M.2
  • 5
    • 0015882208 scopus 로고
    • Subcellular location of superoxide dismutase in spinach leaves and preparation and properties of crystalline spinach superoxidedismutase
    • Asada, K., Urano, M. and Takahashi, M. (1973) Subcellular location of superoxide dismutase in spinach leaves and preparation and properties of crystalline spinach superoxidedismutase. Eur. J. Biochem. 36: 257–266.
    • (1973) Eur. J. Biochem , vol.36 , pp. 257-266
    • Asada, K.1    Urano, M.2    Takahashi, M.3
  • 6
    • 0013893929 scopus 로고
    • Heme proteins. Vi. crystalline pineapple peroxidase b
    • Beaudreau, C. and Yasunobu, K. T. (1966) Heme proteins. VI. Crystalline pineapple peroxidase B. Biochemistry 5: 1405–1412
    • (1966) Biochemistry , vol.5 , pp. 1405-1412
    • Beaudreau, C.1    Yasunobu, K.T.2
  • 7
    • 0024289432 scopus 로고
    • Identification of the fifth axial heme ligand of chloroperoxidase
    • Blanke, S. R. and Hager, L. P. (1988) Identification of the fifth axial heme ligand of chloroperoxidase. J. Biol. Chem. 263: 18739–18743.
    • (1988) J. Biol. Chem , vol.263 , pp. 18739-18743
    • Blanke, S.R.1    Hager, L.P.2
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248–254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 0000019955 scopus 로고
    • Purification, properties, and distribution of ascorbate peroxidase in legume root nodules
    • Dalton, D.A., Hanus, F. J., Russell, S. A. and Evans, H. J. (1987) Purification, properties, and distribution of ascorbate peroxidase in legume root nodules. Plant Physiol. 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
  • 10
    • 0000746853 scopus 로고
    • Enzymatic reactions of ascorbate and glutathione that prevent peroxide damage in soybean root nodules
    • Dalton, D. A., Russell, S. A., Hanus, F. J., Pascoe, G. A. and Evans, H. J. (1986) Enzymatic reactions of ascorbate and glutathione that prevent peroxide damage in soybean root nodules. Proc. Natl. Acad. Sci. USA 83: 3811–3815.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 3811-3815
    • Dalton, D.A.1    Russell, S.A.2    Hanus, F.J.3    Pascoe, G.A.4    Evans, H.J.5
  • 11
    • 78651153791 scopus 로고
    • Disc electrophoresis ii. Method and application to human serum proteins
    • Davis, B. J. (1964) Disc electrophoresis II. Method and application to human serum proteins. Ann. N. Y. Acad. Sci. 121: 404–427.
    • (1964) Ann. N. Y. Acad. Sci , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 13
    • 84938038242 scopus 로고
    • Isolation of immunoglobulins, antibodies, and their subunits
    • In, Edited by Garvey, J. S., Cremer, N. E. and Sussdorf, D. H, The Benjamin/Cummings Publ., Reading, Mass
    • Garvey, J. S., Cremer, N. E. and Sussdorf, D. H. (1977) Isolation of immunoglobulins, antibodies, and their subunits. In Methods in Immunology. Edited by Garvey, J. S., Cremer, N. E. and Sussdorf, D. H. pp. 215–219. The Benjamin/Cummings Publ., Reading, Mass.
    • (1977) Methods in Immunology , pp. 215-219
    • Garvey, J.S.1    Cremer, N.E.2    Sussdorf, D.H.3
  • 14
    • 0001773373 scopus 로고
    • Partial purification and properties of soluble ascorbate peroxidases from pea leaves
    • Gerbling, K. P., Kelly, G. J., Fisher, K. H. and Latzko, E. (1984) Partial purification and properties of soluble ascorbate peroxidases from pea leaves. J. Plant Physiol. 115: 59–67.
    • (1984) J. Plant Physiol , vol.115 , pp. 59-67
    • Gerbling, K.P.1    Kelly, G.J.2    Fisher, K.H.3    Latzko, E.4
  • 15
    • 34250131767 scopus 로고
    • Hydrogen-peroxide-scavenging systems within pea chloroplasts
    • Gillham, D. J. and Dodge, A. D. (1986) Hydrogen-peroxide-scavenging systems within pea chloroplasts. Planta 167: 246–251.
    • (1986) Planta , vol.167 , pp. 246-251
    • Gillham, D.J.1    Dodge, A.D.2
  • 16
    • 0020074305 scopus 로고
    • A dot-immuno-binding assay for monoclonal and other antibodies
    • Hawkes, R., Niday, E. and Gorden, J. (1982) A dot-immuno-binding assay for monoclonal and other antibodies. Anal. Biochem. 119: 142–147.
    • (1982) Anal. Biochem , vol.119 , pp. 142-147
    • Hawkes, R.1    Niday, E.2    Gorden, J.3
  • 17
    • 0000949449 scopus 로고
    • Inactivation of ascorbate peroxidase in spinach chloroplasts on dark addition of hydrogen peroxide: Its protection by ascorbate
    • Hossain, M. A. and Asada, K. (1984) Inactivation of ascorbate peroxidase in spinach chloroplasts on dark addition of hydrogen peroxide: its protection by ascorbate. Plant Cell Physiol. 25: 1285–1295.
    • (1984) Plant Cell Physiol , vol.25 , pp. 1285-1295
    • Hossain, M.A.1    Asada, K.2
  • 20
    • 0018570272 scopus 로고
    • Soluble ascorbate peroxidase
    • Kelly, G. J. and Latzko, E. (1980) Soluble ascorbate peroxidase. Naturwissenschaften 66: 617–618.
    • (1980) Naturwissenschaften , vol.66 , pp. 617-618
    • Kelly, G.J.1    Latzko, E.2
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage t4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0000155139 scopus 로고
    • Molecular cloning of complementary dna encoding the lignin-forming peroxidase from tobacco: Molecular analysis and tissue-specific expression
    • Lagrimini, L. M., Burkhart, W., Moyer, M. and Rothstein, S. (1987) Molecular cloning of complementary DNA encoding the lignin-forming peroxidase from tobacco: molecular analysis and tissue-specific expression. Proc. Natl. Acad. Sci. USA 84: 7542–7546.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7542-7546
    • Lagrimini, L.M.1    Burkhart, W.2    Moyer, M.3    Rothstein, S.4
  • 23
    • 0001435023 scopus 로고
    • Relatedness among proteins: A new method of estimation and its application to immunoglobulins
    • Marchalonis, J. J. and Weltman, J. K. (1971) Relatedness among proteins: a new method of estimation and its application to immunoglobulins. Comp. Biochem. Physiol. 38B: 609–625.
    • (1971) Comp. Biochem. Physiol , vol.38B , pp. 609-625
    • Marchalonis, J.J.1    Weltman, J.K.2
  • 24
    • 0019035007 scopus 로고
    • Covalent structure of turnip peroxidase 7
    • Mazza, G. and Welinder, K. G. (1980) Covalent structure of turnip peroxidase 7. Eur. J. Biochem. 108: 481–489.
    • (1980) Eur. J. Biochem , vol.108 , pp. 481-489
    • Mazza, G.1    Welinder, K.G.2
  • 25
    • 0023937734 scopus 로고
    • Purification, crystallization, and characterization of peroxidase from coprinus cinereus
    • Morita, Y., Yamashita, H., Mikami, B., Iwamoto, H., Aibara, S., Terada, M. and Minami, J. (1988) Purification, crystallization, and characterization of peroxidase from Coprinus cinereus. J. Biochem. 103: 693–699.
    • (1988) J. Biochem , vol.103 , pp. 693-699
    • Morita, Y.1    Yamashita, H.2    Mikami, B.3    Iwamoto, H.4    Aibara, S.5    Terada, M.6    Minami, J.7
  • 26
    • 0001330378 scopus 로고
    • Spinach chloroplasts scavenge hydrogen peroxide on illumination
    • Nakano, Y. and Asada, K. (1980) Spinach chloroplasts scavenge hydrogen peroxide on illumination. Plant Cell Physiol. 21: 1295–1307.
    • (1980) Plant Cell Physiol , vol.21 , pp. 1295-1307
    • Nakano, Y.1    Asada, K.2
  • 27
    • 0010282460 scopus 로고
    • Hydrogen peroxide is scavenged by ascorbate-specific peroxidase in spinach chloroplasts
    • Nakano, Y. and Asada, K. (1981) Hydrogen peroxide is scavenged by ascorbate-specific peroxidase in spinach chloroplasts. Plant Cell Physiol. 22: 867–880.
    • (1981) Plant Cell Physiol , vol.22 , pp. 867-880
    • Nakano, Y.1    Asada, K.2
  • 28
    • 77957183372 scopus 로고
    • Purification of ascorbate peroxidase in spinach chloroplasts; its inactivation in ascorbate-depleted medium and reactivation by monodehydro-ascorbate radical
    • Nakano, Y. and Asada, K. (1987) Purification of ascorbate peroxidase in spinach chloroplasts; its inactivation in ascorbate-depleted medium and reactivation by monodehydro-ascorbate radical. Plant Cell Physiol. 28: 131–140.
    • (1987) Plant Cell Physiol , vol.28 , pp. 131-140
    • Nakano, Y.1    Asada, K.2
  • 29
    • 0342811084 scopus 로고
    • Hill reaction, hydrogen peroxide scavenging, and ascorbate peroxidase activity of mesophyll and bundle sheath chloroplasts of nadp-malic enzyme type c4 species
    • 4 species. Plant Physiol. 85: 294–298.
    • (1987) Plant Physiol , vol.85 , pp. 294-298
    • Nakano, Y.1    Edwards, G.E.2
  • 30
    • 0010481117 scopus 로고
    • Distribution and structure of plant microbodies (Peroxisomes)
    • In, Edited by Hatch, M. D., Osmond, C. B. and Slatyer, R. O, Wiley-Interscience, New York
    • Newcomb, E. H. and Fredrick, S. E. (1971) Distribution and structure of plant microbodies (peroxisomes). In Photosynthesis and Photorespiration. Edited by Hatch, M. D., Osmond, C. B. and Slatyer, R. O. pp. 442–457. Wiley-Interscience, New York.
    • (1971) Photosynthesis and Photorespiration , pp. 442-457
    • Newcomb, E.H.1    Fredrick, S.E.2
  • 31
    • 0000756628 scopus 로고
    • The molar light absorption of pyridine ferroprotoporphyrin (Pyridine haemochromogen)
    • Paul, K. G., Theorell, H. and Akeson, A. (1953) The molar light absorption of pyridine ferroprotoporphyrin (pyridine haemochromogen). Acta Chem. Scand. 7: 1284–1287.
    • (1953) Acta Chem. Scand , vol.7 , pp. 1284-1287
    • Paul, K.G.1    Theorell, H.2    Akeson, A.3
  • 32
    • 0018640551 scopus 로고
    • Glycoprotein detected in polyacrylamide gel with thymol and sulfuric acid
    • Racusen, C. (1979) Glycoprotein detected in polyacrylamide gel with thymol and sulfuric acid. Anal. Biochem. 99: 474–476.
    • (1979) Anal. Biochem , vol.99 , pp. 474-476
    • Racusen, C.1
  • 34
    • 0019324583 scopus 로고
    • Metabolism of hydrogen peroxide in euglena gracilis z by l-ascorbic acid peroxidase
    • Shigeoka, S., Nakano, Y. and Kitaoka, S. (1980a) Metabolism of hydrogen peroxide in Euglena gracilis z by L-ascorbic acid peroxidase. Biochem. J. 186: 377–380.
    • (1980) Biochem. J , vol.186 , pp. 377-380
    • Shigeoka, S.1    Nakano, Y.2    Kitaoka, S.3
  • 35
    • 0019325168 scopus 로고
    • Purification and some properties of l-ascorbic acid-specific peroxidase in euglena gracilis z
    • Shigeoka, S., Nakano, Y. and Kitaoka, S. (1980b) Purification and some properties of L-ascorbic acid-specific peroxidase in Euglena gracilis z. Arch. Biochem. Biophys. 201: 121–127.
    • (1980) Arch. Biochem. Biophys , vol.201 , pp. 121-127
    • Shigeoka, S.1    Nakano, Y.2    Kitaoka, S.3
  • 36
    • 0018398183 scopus 로고
    • Phylogenetic distribution of glutathione peroxidase
    • Smith, J. and Shrift, A. (1979) Phylogenetic distribution of glutathione peroxidase. Comp. Biochem. Physiol. 63B: 39–44.
    • (1979) Comp. Biochem. Physiol , vol.63B , pp. 39-44
    • Smith, J.1    Shrift, A.2
  • 37
    • 0013906320 scopus 로고
    • Pharmaceutical studies on ascorbic acid derivatives. I. syntheses of esters of ascorbic acid and their physicochemical properties
    • Tanaka, H. and Yamamoto, R. (1966) Pharmaceutical studies on ascorbic acid derivatives. I. Syntheses of esters of ascorbic acid and their physicochemical properties. Yakugaku Zasshi. 86: 376–383.
    • (1966) Yakugaku Zasshi , vol.86 , pp. 376-383
    • Tanaka, H.1    Yamamoto, R.2
  • 38
    • 0015152970 scopus 로고
    • An improved procedure using ferricyanide for detecting catalase isozymes
    • Woodbury, W., Spencer, A. K. and Stahmann, M. A. (1971) An improved procedure using ferricyanide for detecting catalase isozymes. Anal. Biochem. 44: 301–305.
    • (1971) Anal. Biochem , vol.44 , pp. 301-305
    • Woodbury, W.1    Spencer, A.K.2    Stahmann, M.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.