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Volumn 46, Issue 7, 1998, Pages 2469-2473

Study of Stereospecificity in Pear and Strawberry Polyphenol Oxidases

Author keywords

Enzyme kinetics; MBTH; NMR; Pear; PPO; Stereospecificity; Strawberry

Indexed keywords

FRAGARIA X ANANASSA; PYRUS COMMUNIS;

EID: 0000065531     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf9708406     Document Type: Article
Times cited : (30)

References (38)
  • 1
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of proteins utilizing the principle of protein-dye binding
    • Bradford, M. A rapid and sensitive method for the quantification of microgram quantities of proteins utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-256.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-256
    • Bradford, M.1
  • 3
    • 0028861909 scopus 로고
    • A continuous spectrophotometric method for determining the monophenolase and diphenolase activities of apple polyphenol oxidase
    • Espín, J. C.; Morales, M.; Varón, R.; Tudela, J.; García-Cánovas, F. A continuous spectrophotometric method for determining the monophenolase and diphenolase activities of apple polyphenol oxidase. Anal. Biochem. 1995a, 231, 237-246.
    • (1995) Anal. Biochem. , vol.231 , pp. 237-246
    • Espín, J.C.1    Morales, M.2    Varón, R.3    Tudela, J.4    García-Cánovas, F.5
  • 5
    • 0030444246 scopus 로고    scopus 로고
    • A continuons spectrophotometric method for determining the monophenolase and diphenolase activities of pear polyphenol oxidase
    • Espín, J. C . Morales, M.; Varón, R.; Tudela, J.; García-Cánovas, F. A continuons spectrophotometric method for determining the monophenolase and diphenolase activities of pear polyphenol oxidase. J. Food Sci. 1996, 61, 1177-1182.
    • (1996) J. Food Sci. , vol.61 , pp. 1177-1182
    • Espín, J.C..1    Morales, M.2    Varón, R.3    Tudela, J.4    García-Cánovas, F.5
  • 7
    • 0001003175 scopus 로고    scopus 로고
    • Improvement of a continuous spectro-photometric method for determining the monophenolase and diphenolase activities of mushroom polyphenol oxidase
    • Espín, J C.; Morales, M.; García-Ruiz, P. A., Tudela, J., García-Cánovas, F. Improvement of a continuous spectro-photometric method for determining the monophenolase and diphenolase activities of mushroom polyphenol oxidase. J. Agric. Food Chem. 1997b, 45, 1084-1090.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 1084-1090
    • Espín, J.C.1    Morales, M.2    García-Ruiz, P.A.3    Tudela, J.4    García-Cánovas, F.5
  • 10
  • 11
    • 4244179208 scopus 로고
    • Oxidation of catechols and catecholamines by horseradish peroxidase and lactoperoxidase
    • Ferrari, R. P.; Laurenti, E.; Casella, L.; Poli, S. Oxidation of catechols and catecholamines by horseradish peroxidase and lactoperoxidase. Spectrochim. Acta 1993, 49, 1261-1267.
    • (1993) Spectrochim. Acta , vol.49 , pp. 1261-1267
    • Ferrari, R.P.1    Laurenti, E.2    Casella, L.3    Poli, S.4
  • 13
    • 33847087027 scopus 로고
    • Chemical and spectroscopic studies of the binuclear copper active site of Neurospora tyrosinase: Comparison to hemocyanins
    • Himmelwright, R. S.; Eickman, N. C.; Lu Bien, C. D.; Lerch, K.; Solomon, E. I. Chemical and spectroscopic studies of the binuclear copper active site of Neurospora tyrosinase: comparison to hemocyanins. J. Am. Chem. Soc. 1980, 102, 7339-7344.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 7339-7344
    • Himmelwright, R.S.1    Eickman, N.C.2    Lu Bien, C.D.3    Lerch, K.4    Solomon, E.I.5
  • 14
    • 0003700113 scopus 로고
    • Jandel Scientific: Corte Madera, CA
    • Jandel Scientific. Sigma Plot 2.01 for Windows; Jandel Scientific: Corte Madera, CA, 1994.
    • (1994) Sigma Plot 2.01 for Windows
  • 16
    • 49149142913 scopus 로고
    • Monophenolase activity of avocado polyphenol oxidase
    • Khan, V.; Pomerantz, S. H. Monophenolase activity of avocado polyphenol oxidase. Phytochemistry 1980, 19, 379-385.
    • (1980) Phytochemistry , vol.19 , pp. 379-385
    • Khan, V.1    Pomerantz, S.H.2
  • 17
    • 0001064298 scopus 로고
    • Sigel, H., Ed.; Dekker: New York
    • Lerch, K. Metal Ions in Biological Systems; Sigel, H., Ed.; Dekker: New York, 1981; Vol. 13, pp 143-186.
    • (1981) Metal Ions in Biological Systems , vol.13 , pp. 143-186
    • Lerch, K.1
  • 18
    • 0015901114 scopus 로고
    • Reactivity of tyrosinase towards substrates
    • Makino, N.; Mason, H. S. Reactivity of tyrosinase towards substrates. J. Biol. Chem. 1973, 248, 5731-5735.
    • (1973) J. Biol. Chem. , vol.248 , pp. 5731-5735
    • Makino, N.1    Mason, H.S.2
  • 19
    • 0016259645 scopus 로고
    • The oxidation state of copper in resting tyrosinase
    • Makino, N.; McMahill, P.; Mason, H. S.; Moss, T. H. The oxidation state of copper in resting tyrosinase. J. Biol. Chem. 1974, 249, 6062-6066.
    • (1974) J. Biol. Chem. , vol.249 , pp. 6062-6066
    • Makino, N.1    McMahill, P.2    Mason, H.S.3    Moss, T.H.4
  • 20
    • 0000169232 scopus 로고
    • An algorithm for least-squares estimation of nonlinear parameters
    • Marquardt, D. An algorithm for least-squares estimation of nonlinear parameters. J. Sci. Ind. Appl. Math. 1963, 11, 431-444.
    • (1963) J. Sci. Ind. Appl. Math. , vol.11 , pp. 431-444
    • Marquardt, D.1
  • 21
    • 0000034469 scopus 로고
    • The biochemistry and control of enzymatic browning
    • Martínez, M. V.; Whitaker, J. R. The biochemistry and control of enzymatic browning. Trends Food Sci. Technol. 1995, 6, 195-200.
    • (1995) Trends Food Sci. Technol. , vol.6 , pp. 195-200
    • Martínez, M.V.1    Whitaker, J.R.2
  • 22
    • 0001030216 scopus 로고
    • Polyphenoloxidases and their significance in fruits and vegetables
    • Fox, P. F., Ed.; Elsevier: London
    • Mayer, A. M.; Harel, E. Polyphenoloxidases and their significance in fruits and vegetables. In Food Enzymology; Fox, P. F., Ed.; Elsevier: London, 1991; pp 373-379.
    • (1991) Food Enzymology , pp. 373-379
    • Mayer, A.M.1    Harel, E.2
  • 23
    • 0000376546 scopus 로고
    • Tyrosine hydroxylation catalyzed by mammalian tyrosinase-assay
    • Pomerantz, S. H. Tyrosine hydroxylation catalyzed by mammalian tyrosinase-assay. J Biol. Chem. 1963, 238, 2351-2357.
    • (1963) J Biol. Chem. , vol.238 , pp. 2351-2357
    • Pomerantz, S.H.1
  • 24
    • 85053591293 scopus 로고
    • Tyrosinase
    • Lontie, R., Ed.; CRC Press: Boca Raton, FL
    • Robb, D. A. Tyrosinase. In Copper Proteins and Copper-Enzymes; Lontie, R., Ed.; CRC Press: Boca Raton, FL, 1984; pp 207-241.
    • (1984) Copper Proteins and Copper-Enzymes , pp. 207-241
    • Robb, D.A.1
  • 26
    • 0028140296 scopus 로고
    • A continuous spectrophotometric method for the determination of monophenolase activity of tyrosinase using 3-methyl-2-benzothiazolinone hydrazone
    • Rodríguez-López, J. N.; Escribano, J.; García-Cánovas, F. A continuous spectrophotometric method for the determination of monophenolase activity of tyrosinase using 3-methyl-2-benzothiazolinone hydrazone. Anal. Biochem. 1994, 216, 205-212.
    • (1994) Anal. Biochem. , vol.216 , pp. 205-212
    • Rodríguez-López, J.N.1    Escribano, J.2    García-Cánovas, F.3
  • 29
    • 0015609087 scopus 로고
    • Magnetic dipole-dipole coupled Cu(II) pairs in nitric oxide-treated tyrosinase: A structural relationship between the active sites of tyrosinase and hemocyanin
    • Schoot-Uiterkamp, A. J.; Mason, H. S. Magnetic dipole-dipole coupled Cu(II) pairs in nitric oxide-treated tyrosinase: a structural relationship between the active sites of tyrosinase and hemocyanin. Proc. Natl. Acad. Sci. U.S.A. 1973, 70, 993-996.
    • (1973) Proc. Natl. Acad. Sci. U.S.A. , vol.70 , pp. 993-996
    • Schoot-Uiterkamp, A.J.1    Mason, H.S.2
  • 30
    • 0017183229 scopus 로고
    • Absorption and circular dichroism spectra of different forms of mushroom tyrosinase
    • Schoot-Uiterkamp, A. J. M.; Evans, L. H.; Jolley, R. L.; Mason, H. S. Absorption and circular dichroism spectra of different forms of mushroom tyrosinase. Biochim. Biophys. Acta 1976, 453, 200-204.
    • (1976) Biochim. Biophys. Acta , vol.453 , pp. 200-204
    • Schoot-Uiterkamp, A.J.M.1    Evans, L.H.2    Jolley, R.L.3    Mason, H.S.4
  • 31
    • 0002954387 scopus 로고
    • Spiro, T. G., Ed.; Wiley-Interscience: New York
    • Solomon, E. I. In Copper Proteins and Copper Enzymes; Spiro, T. G., Ed.; Wiley-Interscience: New York, 1981; Vol. III, pp 41-108.
    • (1981) Copper Proteins and Copper Enzymes , vol.3 , pp. 41-108
    • Solomon, E.I.1
  • 32
    • 0027914978 scopus 로고
    • Electronic structure contributions to function in bioinorganic chemistry
    • Solomon, E. I.; Lowery, M. D. Electronic structure contributions to function in bioinorganic chemistry. Science 1993, 259, 1575-1581
    • (1993) Science , vol.259 , pp. 1575-1581
    • Solomon, E.I.1    Lowery, M.D.2
  • 35
  • 36
    • 0005499841 scopus 로고
    • Statistical estimations in enzyme kinetics
    • Wilkinson, G. N. Statistical estimations in enzyme kinetics. Biochem. J. 1961, 80, 324-332.
    • (1961) Biochem. J. , vol.80 , pp. 324-332
    • Wilkinson, G.N.1
  • 37
    • 0025910929 scopus 로고
    • New assays for the tyrosine hydroxylase and dopa oxidase activities of tyrosinase
    • Winder, A. J.; Harris, H. New assays for the tyrosine hydroxylase and dopa oxidase activities of tyrosinase. Eur. J. Biochem. 1991, 198, 317-326.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 317-326
    • Winder, A.J.1    Harris, H.2
  • 38
    • 0016381387 scopus 로고
    • Production of 3,4-dihydroxyphenyl-L-alanine (L-dopa) by Pseudomonas melanogenum
    • Yoshida, H.; Tanaka, Y.; Nakayama, K. Production of 3,4-dihydroxyphenyl-L-alanine (L-dopa) by Pseudomonas melanogenum. Agric. Biol. Chem. 1974, 38, 627-632.
    • (1974) Agric. Biol. Chem. , vol.38 , pp. 627-632
    • Yoshida, H.1    Tanaka, Y.2    Nakayama, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.