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Volumn 57, Issue 5, 2004, Pages

Kinetics of intraconversion of redox intermediates of lactoperoxidase, eosinophil peroxidase and myeloperoxidase

Author keywords

[No Author keywords available]

Indexed keywords

CATALASE; EOSINOPHIL PEROXIDASE; HEME; LACTOPEROXIDASE; MYELOPEROXIDASE; OXIDOREDUCTASE; PEROXIDASE; PORPHYRIN;

EID: 9144234136     PISSN: 13446304     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Conference Paper
Times cited : (41)

References (10)
  • 1
    • 12944305786 scopus 로고
    • Superfamily of plant, fungal and bacterial peroxidases
    • Welinder, K. (1992): Superfamily of plant, fungal and bacteria] peroxidases. Curr. Opin. Struct. Biol., 2, 388-393.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 388-393
    • Welinder, K.1
  • 2
    • 0023888377 scopus 로고
    • Human myeloperoxidase and thyroid peroxidase, two enzymes with separate and distinct physiological functions, are evolutionary related members of the same gene family
    • Kimura, S. and Ikeda-Saito, M. (1988): Human myeloperoxidase and thyroid peroxidase, two enzymes with separate and distinct physiological functions, are evolutionary related members of the same gene family. Proteins Struct. Funct. Genet., 3, 113-120.
    • (1988) Proteins Struct. Funct. Genet. , vol.3 , pp. 113-120
    • Kimura, S.1    Ikeda-Saito, M.2
  • 3
    • 0034697020 scopus 로고    scopus 로고
    • X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 Å resolution
    • Fiedler, T. J., Davey, C. A. and Fernna, R. E. (2000): X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 Å resolution. J. Biol. Chem., 275, 11964-11971.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11964-11971
    • Fiedler, T.J.1    Davey, C.A.2    Fernna, R.E.3
  • 4
    • 0032558979 scopus 로고    scopus 로고
    • Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate
    • Furtmüller, P. G., Burner, U. and Obinger, C. (1998): Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate. Biochemistry, 37, 17923-17930.
    • (1998) Biochemistry , vol.37 , pp. 17923-17930
    • Furtmüller, P.G.1    Burner, U.2    Obinger, C.3
  • 5
    • 0034687654 scopus 로고    scopus 로고
    • Spectral and kinetic studies on the formation of eosinophil peroxidase compound I and its reaction with halides and thiocyanate
    • Furtmüller, P. G., Burner, U., Regelsberger, G. and Obinger, C. (2000): Spectral and kinetic studies on the formation of eosinophil peroxidase compound I and its reaction with halides and thiocyanate. Biochemistry, 39, 15578-15584.
    • (2000) Biochemistry , vol.39 , pp. 15578-15584
    • Furtmüller, P.G.1    Burner, U.2    Regelsberger, G.3    Obinger, C.4
  • 7
    • 0034792757 scopus 로고    scopus 로고
    • Redox properties of the couple compound I/native enzyme of myeloperoxidase and eosinophil peroxidase
    • Arnhold, J., Furtmüller, P. G., Regelsberger, G. and Obinger, C. (2001): Redox properties of the couple compound I/native enzyme of myeloperoxidase and eosinophil peroxidase. Eur. J. Biochem., 268, 5142-5148.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5142-5148
    • Arnhold, J.1    Furtmüller, P.G.2    Regelsberger, G.3    Obinger, C.4
  • 8
    • 0036478818 scopus 로고    scopus 로고
    • Redox intermediates of plant and mammalian peroxidases: A comparative transient-kinetic study of their reactivity toward indole derivatives
    • Jantschko, W., Furtmüller, P. G., Allegra, M., Livrea, M. A., Jakopitsch, C., Regelsberger, G. and Obinger, C. (2002): Redox intermediates of plant and mammalian peroxidases: a comparative transient-kinetic study of their reactivity toward indole derivatives. Arch. Biochem. Biophys., 398, 12-22.
    • (2002) Arch. Biochem. Biophys. , vol.398 , pp. 12-22
    • Jantschko, W.1    Furtmüller, P.G.2    Allegra, M.3    Livrea, M.A.4    Jakopitsch, C.5    Regelsberger, G.6    Obinger, C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.