메뉴 건너뛰기




Volumn 46, Issue 4, 1998, Pages 1268-1271

Tyrosinase Inhibitors from Anise Oil

Author keywords

Anisaldehyde; Aniseed; L DOPA; Noncompetitive inhibition; Schiff base formation; Tyrosinase inhibitor

Indexed keywords

APIACEAE; BASIDIOMYCOTA; MYRRHIS ODORATA; PIMPINELLA ANISUM;

EID: 0001136721     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf9708958     Document Type: Article
Times cited : (77)

References (26)
  • 1
    • 0001931507 scopus 로고
    • Biochemistry of insect cuticle
    • Andersen, S. O. Biochemistry of insect cuticle. Annu. Rev. Entomol. 1979, 24, 29-61.
    • (1979) Annu. Rev. Entomol. , vol.24 , pp. 29-61
    • Andersen, S.O.1
  • 2
    • 0009160591 scopus 로고
    • A comparison of mushroom tyrosinase dopaquinone and dopachrome assays using diode-array spectrophotometry: Dopachrome formation vs ascorbate-linked dopaquinone reduction
    • Behbahani, I.; Miller, S. A.; O'Keeffe, D. H. A comparison of mushroom tyrosinase dopaquinone and dopachrome assays using diode-array spectrophotometry: Dopachrome formation vs ascorbate-linked dopaquinone reduction. Microchem. J. 1993, 47, 251-260.
    • (1993) Microchem. J. , vol.47 , pp. 251-260
    • Behbahani, I.1    Miller, S.A.2    O'Keeffe, D.H.3
  • 3
    • 85052607115 scopus 로고
    • Spices and Condiments II
    • Maarse, H., Ed.; Dekker: New York
    • Boelens, M. H. Spices and Condiments II. In Volatile Compounds in Foods and Beverages; Maarse, H., Ed.; Dekker: New York, 1991; pp 449-482.
    • (1991) Volatile Compounds in Foods and Beverages , pp. 449-482
    • Boelens, M.H.1
  • 6
    • 0028176278 scopus 로고
    • Inhibitor binding to the binuclear active site of tyrosinase: Temperature, pH, and solvent deuterium isotope effects
    • Conrad, J. S.; Dawso, S. R.; Hubbard, E. R.; Meyers, T. E.; Strothkamp, K. G. Inhibitor binding to the binuclear active site of tyrosinase: Temperature, pH, and solvent deuterium isotope effects. Biochemistry 1994, 33, 5739-5744.
    • (1994) Biochemistry , vol.33 , pp. 5739-5744
    • Conrad, J.S.1    Dawso, S.R.2    Hubbard, E.R.3    Meyers, T.E.4    Strothkamp, K.G.5
  • 7
    • 0014939358 scopus 로고
    • Physicochemical and kinetic properties of mushroom tyrosinase
    • Duckworth, H. W.; Coleman, J. E. Physicochemical and kinetic properties of mushroom tyrosinase. J. Biol. Chem. 1970. 245, 1613-1625.
    • (1970) J. Biol. Chem. , vol.245 , pp. 1613-1625
    • Duckworth, H.W.1    Coleman, J.E.2
  • 8
    • 0000090193 scopus 로고
    • Ultraviolet resonance raman study of oxytyrosinase. Comparison with oxyhemocyanins
    • Eickman, N. C.; Solomon, E. I., Larrabee, J. A.; Spiro, T. G.; Lerch, K. Ultraviolet resonance raman study of oxytyrosinase. Comparison with oxyhemocyanins. J. Am. Chem. Soc. 1978, 100, 6529-6531.
    • (1978) J. Am. Chem. Soc. , vol.100 , pp. 6529-6531
    • Eickman, N.C.1    Solomon, E.I.2    Larrabee, J.A.3    Spiro, T.G.4    Lerch, K.5
  • 9
    • 2842525944 scopus 로고    scopus 로고
    • Food browning and its prevention: An overview
    • Friedman, M. Food browning and its prevention: An overview. J. Agric. Food Chem. 1996, 44, 631-653.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 631-653
    • Friedman, M.1
  • 10
    • 0000427167 scopus 로고
    • Effect of ascorbic acid, sodium bisulfite, and thiol compounds on mushroom polyphenol oxidase
    • Golan-Goldhirsh, A.; Whitaker, J. R. Effect of ascorbic acid, sodium bisulfite, and thiol compounds on mushroom polyphenol oxidase. J. Agric. Food Chem. 1984, 32, 1003-1009.
    • (1984) J. Agric. Food Chem. , vol.32 , pp. 1003-1009
    • Golan-Goldhirsh, A.1    Whitaker, J.R.2
  • 12
    • 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.; LuBien, 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    LuBien, C.D.3    Lerch, K.4    Solomon, E.I.5
  • 13
    • 0000629565 scopus 로고
    • Insect control agents from tropical plants
    • Downum, K. R.; Romeo, J. T.; Stafford, H. A., Eds.; Plenum: New York
    • Kubo, I. Insect control agents from tropical plants. In Recent Advances in Phytochemistry, Phytochemical Potential of Tropical Plants; Downum, K. R.; Romeo, J. T.; Stafford, H. A., Eds.; Plenum: New York, 1993; Vol. 27, pp 133-151.
    • (1993) Recent Advances in Phytochemistry, Phytochemical Potential of Tropical Plants , vol.27 , pp. 133-151
    • Kubo, I.1
  • 14
    • 0347172950 scopus 로고    scopus 로고
    • Tyrosinase inhibitors from plants
    • ACS Symposium Series 658; Hedin, P.; Hollingworth, R.; Masler, E.; Miyamoto, J.; Thompson, D. Eds., American Chemical Society: Washington, DC
    • Kubo, I. Tyrosinase inhibitors from plants. In Phytochemicals for Pest Control, ACS Symposium Series 658; Hedin, P.; Hollingworth, R.; Masler, E.; Miyamoto, J.; Thompson, D. Eds., American Chemical Society: Washington, DC, 1997; pp 310-326
    • (1997) Phytochemicals for Pest Control , pp. 310-326
    • Kubo, I.1
  • 15
    • 0000256210 scopus 로고
    • Anethole, a synergist of polygodial against filamentous microorganisms
    • Kubo, I.; Himejima, M. Anethole, a synergist of polygodial against filamentous microorganisms. J. Agric. Food Chem. 1991, 39, 2290-2292.
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 2290-2292
    • Kubo, I.1    Himejima, M.2
  • 16
    • 0001064298 scopus 로고
    • Copper monooxygenases: Tyrosinase and dopamine β- Monooxygenase
    • Sigel, H., Ed.; Marcel Dekker: New York
    • Lerch, K. Copper monooxygenases: Tyrosinase and dopamine β-monooxygenase. In Metal Ions in Biological Systems; Sigel, H., Ed.; Marcel Dekker: New York, 1981; pp 143-186.
    • (1981) Metal Ions in Biological Systems , pp. 143-186
    • Lerch, K.1
  • 17
    • 0001185061 scopus 로고
    • In vitro effectiveness of several whitening cosmetic components in human melanocytes
    • Maeda, K.; Fukuda, M. In vitro effectiveness of several whitening cosmetic components in human melanocytes. J. Soc. Cosmet. Chem. 1991, 42, 361-368.
    • (1991) J. Soc. Cosmet. Chem. , vol.42 , pp. 361-368
    • Maeda, K.1    Fukuda, M.2
  • 18
    • 0019225689 scopus 로고
    • Inhibitory effect of Chinese crude drugs on tyrosinase
    • Masamoto, Y.; Iida, S.; Kubo, M. Inhibitory effect of Chinese crude drugs on tyrosinase. Planta Med. 1980, 40, 361-365.
    • (1980) Planta Med. , vol.40 , pp. 361-365
    • Masamoto, Y.1    Iida, S.2    Kubo, M.3
  • 19
    • 0013849210 scopus 로고
    • Melanoproteins I. Reactions between enzyme-generated quinones and amino acids
    • Mason, H. S.; Peterson, E. W. Melanoproteins I. Reactions between enzyme-generated quinones and amino acids. Biochim. Biophys. Acta 1965, 111, 134-146.
    • (1965) Biochim. Biophys. Acta , vol.111 , pp. 134-146
    • Mason, H.S.1    Peterson, E.W.2
  • 20
    • 46149132278 scopus 로고
    • Polyphenol oxidases in plants-Recent progress
    • Mayer, A. M. Polyphenol oxidases in plants-Recent progress. Phytochemistry 1987, 26, 11-20.
    • (1987) Phytochemistry , vol.26 , pp. 11-20
    • Mayer, A.M.1
  • 21
    • 49249153466 scopus 로고
    • Polyphenol oxidases in plants
    • Mayer, A. M.; Harel, E. Polyphenol oxidases in plants. Phytochemistry 1979, 18, 193-215.
    • (1979) Phytochemistry , vol.18 , pp. 193-215
    • Mayer, A.M.1    Harel, E.2
  • 22
    • 0001136083 scopus 로고
    • Vitiligo, etiology, pathogenesis, diagnosis, and treatment
    • Fitzpatrick, T. B.; Eisen, A. Z.; Wolff, K.; Freedberg, I. M.; Austen, K. F., Eds.; McGraw-Hill: New York
    • Mosher, D. B.; Pathak, M. A.; Fitzpatrick, T. B. Vitiligo, etiology, pathogenesis, diagnosis, and treatment. In Update: Dermatology in General Medicine; Fitzpatrick, T. B.; Eisen, A. Z.; Wolff, K.; Freedberg, I. M.; Austen, K. F., Eds.; McGraw-Hill: New York, 1983; pp 205-225.
    • (1983) Update: Dermatology in General Medicine , pp. 205-225
    • Mosher, D.B.1    Pathak, M.A.2    Fitzpatrick, T.B.3
  • 23
    • 0019509874 scopus 로고
    • Molecular basis of substrate and inhibitory specificity of tyrosinase: Phenolic compounds
    • Passi, S.; Nazzaro-Porro, M. Molecular basis of substrate and inhibitory specificity of tyrosinase: Phenolic compounds. Br. J. Dermatol. 1981, 104, 659-665.
    • (1981) Br. J. Dermatol. , vol.104 , pp. 659-665
    • Passi, S.1    Nazzaro-Porro, M.2
  • 24
    • 0027453615 scopus 로고
    • Effect of L-ascorbic acid on the monophenolase activity of tyrosinase
    • Ros, J. R.; Rodríguez-López, J. N.; García-Cánovas, F. Effect of L-ascorbic acid on the monophenolase activity of tyrosinase. Biochem. J. 1993, 295, 309-312.
    • (1993) Biochem. J. , vol.295 , pp. 309-312
    • Ros, J.R.1    Rodríguez-López, J.N.2    García-Cánovas, F.3
  • 25
  • 26
    • 0000387352 scopus 로고
    • Competitive inhibitor binding to the binuclear copper active site in tyrosinase
    • Winkler, M. E.; Lerch, K.; Solomon, E. I. Competitive inhibitor binding to the binuclear copper active site in tyrosinase. J. Am. Chem. Soc. 1981, 103, 7001-7003.
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 7001-7003
    • Winkler, M.E.1    Lerch, K.2    Solomon, E.I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.