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Volumn 17, Issue 1, 1997, Pages 97-105

Isolation and Characterization of a Peroxidase from the Airway

Author keywords

[No Author keywords available]

Indexed keywords

OVIS; OVIS ARIES;

EID: 0031180867     PISSN: 10441549     EISSN: None     Source Type: Journal    
DOI: 10.1165/ajrcmb.17.1.2719     Document Type: Article
Times cited : (50)

References (42)
  • 1
    • 0026600739 scopus 로고
    • Inflammatory mediators and the generation and release of reactive oxygen species by airway epithelium in vitro
    • Adler, K. B., V. L. Kinnule, N. Akley, J. Lee, L. A. Conn, and J. D. Crapo. 1992. Inflammatory mediators and the generation and release of reactive oxygen species by airway epithelium in vitro. Chest 101:53S-54S.
    • (1992) Chest , vol.101
    • Adler, K.B.1    Kinnule, V.L.2    Akley, N.3    Lee, J.4    Conn, L.A.5    Crapo, J.D.6
  • 2
    • 0028225941 scopus 로고
    • Polymorphonuclear leukocyte-generated oxygen metabolites decrease beat frequency of human respiratory cilia
    • Kantar, A., N. Oggiano, P. L. Giorgi, P. C. Braga, and R. Fiorini. 1994. Polymorphonuclear leukocyte-generated oxygen metabolites decrease beat frequency of human respiratory cilia. Lung 172:215-222.
    • (1994) Lung , vol.172 , pp. 215-222
    • Kantar, A.1    Oggiano, N.2    Giorgi, P.L.3    Braga, P.C.4    Fiorini, R.5
  • 5
    • 0025970976 scopus 로고
    • Mechanisms of hydroperoxide-induced broncho- and vasoconstriction in isolated and perfused rat lung
    • Olafsdottir, K., L. Atzori, A. Ryrfeldt, M. Berggren, M. Kumlin, and P. Moldeus. 1991. Mechanisms of hydroperoxide-induced broncho- and vasoconstriction in isolated and perfused rat lung. Pharmacol. Toxitol. 68:181-186.
    • (1991) Pharmacol. Toxitol. , vol.68 , pp. 181-186
    • Olafsdottir, K.1    Atzori, L.2    Ryrfeldt, A.3    Berggren, M.4    Kumlin, M.5    Moldeus, P.6
  • 6
    • 0027271829 scopus 로고
    • Hydrogen peroxide-induced broncho- and vasoconstriction in the isolated perfused and ventilated guinea pig lung
    • Bannenberg, G., M. Kimland, A. Ryrfeldt, and P. Moldeus. 1993. Hydrogen peroxide-induced broncho- and vasoconstriction in the isolated perfused and ventilated guinea pig lung. Pharmacol. Toxicol. 72:314-320.
    • (1993) Pharmacol. Toxicol. , vol.72 , pp. 314-320
    • Bannenberg, G.1    Kimland, M.2    Ryrfeldt, A.3    Moldeus, P.4
  • 8
    • 0028934956 scopus 로고
    • Morphometric estimation of superoxide generation in allergen-induced airway hyperresponsiveness
    • Liberman, H., A. T. Mariassy, D. Sorace, S. Suster, and W. M. Abraham. 1995. Morphometric estimation of superoxide generation in allergen-induced airway hyperresponsiveness. Lab. Invest. 72:348-354.
    • (1995) Lab. Invest. , vol.72 , pp. 348-354
    • Liberman, H.1    Mariassy, A.T.2    Sorace, D.3    Suster, S.4    Abraham, W.M.5
  • 9
    • 0026720136 scopus 로고
    • Release of reactive oxygen species by guinea pig tracheal epithelial cells in vitro
    • Kinnula, V. L., K. B. Adler, N. J. Ackley, and J. D. Crapo. 1992. Release of reactive oxygen species by guinea pig tracheal epithelial cells in vitro. Am. J. Physiol. 262:L708-L712.
    • (1992) Am. J. Physiol. , vol.262
    • Kinnula, V.L.1    Adler, K.B.2    Ackley, N.J.3    Crapo, J.D.4
  • 10
    • 0024998101 scopus 로고
    • Reactive oxygen species and airway inflammation
    • Barnes, P. J. 1990. Reactive oxygen species and airway inflammation. Free Radic. Biol. Med. 9:235-243.
    • (1990) Free Radic. Biol. Med. , vol.9 , pp. 235-243
    • Barnes, P.J.1
  • 11
    • 0021272862 scopus 로고
    • Antioxidant protection: A function of tracheobronchial and gastrointestinal mucus
    • Cross, C. E., B. Halliwell, and A. Allen. 1984. Antioxidant protection: a function of tracheobronchial and gastrointestinal mucus. Lancet 1:1328-1330.
    • (1984) Lancet , vol.1 , pp. 1328-1330
    • Cross, C.E.1    Halliwell, B.2    Allen, A.3
  • 13
    • 0019353003 scopus 로고
    • Ultrastructural localization of endogenous peroxidase in the lower respiratory tract of the guinea pig
    • Christensen, T. G., G. C. Blanchard, G. Nolley, and J. A. Haves. 1981. Ultrastructural localization of endogenous peroxidase in the lower respiratory tract of the guinea pig. Cell Tissue Res. 214:407-415.
    • (1981) Cell Tissue Res. , vol.214 , pp. 407-415
    • Christensen, T.G.1    Blanchard, G.C.2    Nolley, G.3    Haves, J.A.4
  • 14
    • 0020042304 scopus 로고
    • Endogenous peroxidase in the conducting airways of hamsters: Morphologic evidence of synthesis and secretion
    • Christensen, T. G., and J. A. Hayes. 1982. Endogenous peroxidase in the conducting airways of hamsters: morphologic evidence of synthesis and secretion. Am. Rev. Respir. Dis. 125:341-346.
    • (1982) Am. Rev. Respir. Dis. , vol.125 , pp. 341-346
    • Christensen, T.G.1    Hayes, J.A.2
  • 15
    • 0026562826 scopus 로고
    • Expression of peroxidase activity in rat tracheal epithelial cells associated with Mycoplasma pulmonis
    • Kinbara, M., T. Ueda, and K. Hirai. 1992. Expression of peroxidase activity in rat tracheal epithelial cells associated with Mycoplasma pulmonis. Am. J. Physiol. 262(1:L92-L99.)
    • (1992) Am. J. Physiol. , vol.262 , Issue.1
    • Kinbara, M.1    Ueda, T.2    Hirai, K.3
  • 16
    • 0025807982 scopus 로고
    • Airway blood flow modifies allergic airway smooth muscle contraction
    • Csete, M. E., A. D. Chediak, W. M. Abraham, and A. Wanner. 1991. Airway blood flow modifies allergic airway smooth muscle contraction. Am. Rev. Respir. Dis. 144:59-63.
    • (1991) Am. Rev. Respir. Dis. , vol.144 , pp. 59-63
    • Csete, M.E.1    Chediak, A.D.2    Abraham, W.M.3    Wanner, A.4
  • 17
    • 0014957790 scopus 로고
    • Catalysis of iodination by lactoperoxidase
    • Morrison, M., and G. S. Bayse. 1970. Catalysis of iodination by lactoperoxidase. Biochemistry 9:2995-3000.
    • (1970) Biochemistry , vol.9 , pp. 2995-3000
    • Morrison, M.1    Bayse, G.S.2
  • 18
    • 0020064097 scopus 로고
    • Isolation and characterization of a proteinaceous subnuclear fraction composed of nuclear matrix, peripheral lamina, and nuclear pore complexes from embryos of Drosophila melanogaster
    • Fisher, P. A., M. Berrios, and G. Blobel. 1982. Isolation and characterization of a proteinaceous subnuclear fraction composed of nuclear matrix, peripheral lamina, and nuclear pore complexes from embryos of Drosophila melanogaster. J. Cell Biol. 92:674-686.
    • (1982) J. Cell Biol. , vol.92 , pp. 674-686
    • Fisher, P.A.1    Berrios, M.2    Blobel, G.3
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0022726911 scopus 로고
    • Enzymatic detection of native and derivatized horseradish peroxidase in sodium dodecyl sulfate polyacrylamide gels
    • Schmidt, M. L., and J. O. Trojanowski. 1986. Enzymatic detection of native and derivatized horseradish peroxidase in sodium dodecyl sulfate polyacrylamide gels. Anal. Biochem. 155:371-375.
    • (1986) Anal. Biochem. , vol.155 , pp. 371-375
    • Schmidt, M.L.1    Trojanowski, J.O.2
  • 22
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira, P. 1987. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262: 100135-10038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 100135-110038
    • Matsudaira, P.1
  • 23
    • 0019740344 scopus 로고
    • Glutathione peroxidase
    • Wendel, A. 1981. Glutathione peroxidase. Methods Enzymol. 77:325-333.
    • (1981) Methods Enzymol. , vol.77 , pp. 325-333
    • Wendel, A.1
  • 24
    • 0011836244 scopus 로고
    • Glutathione peroxidase: The two selenium enzymes
    • J. Everse, K. E. Everse, and M. B. Grisham, editors. CRC Press, Boca Raton, FL
    • Spallholz, J. E., and L. M. Boylan. 1991. Glutathione peroxidase: the two selenium enzymes. In Peroxidases in Chemistry and Biology. J. Everse, K. E. Everse, and M. B. Grisham, editors. CRC Press, Boca Raton, FL. 259-291.
    • (1991) Peroxidases in Chemistry and Biology , pp. 259-291
    • Spallholz, J.E.1    Boylan, L.M.2
  • 25
    • 0000974742 scopus 로고
    • Lactoperoxidase: Structure and catalytic properties
    • J. Everse, K. E. Everse, and M. B. Grisham, editors. CRC Press, Boca Raton, FL
    • Thomas, E. L., P. M. Bozeman, and D. B. Learn. 1991. Lactoperoxidase: structure and catalytic properties. In Peroxidases in Chemistry and Biology. J. Everse, K. E. Everse, and M. B. Grisham, editors. CRC Press, Boca Raton, FL. 123-142.
    • (1991) Peroxidases in Chemistry and Biology , pp. 123-142
    • Thomas, E.L.1    Bozeman, P.M.2    Learn, D.B.3
  • 26
    • 0002083802 scopus 로고
    • Myeloperoxidase: Active site structure and catalytic mechanism
    • J. Everse, K. E. Everse, and M. B. Grisham, editors. CRC Press, Boca Raton, FL
    • Hurst, J. K. 1991. Myeloperoxidase: active site structure and catalytic mechanism. In Peroxidases in Chemistry and Biology. Vol. 1. J. Everse, K. E. Everse, and M. B. Grisham, editors. CRC Press, Boca Raton, FL. 37-62.
    • (1991) Peroxidases in Chemistry and Biology , vol.1 , pp. 37-62
    • Hurst, J.K.1
  • 27
    • 0025012904 scopus 로고
    • Assay of the human leukocyte enzymes myeloperoxidase and eosinophil peroxidase
    • Bozeman, P. M., D. B. Learn, and E. L. Thomas. 1990. Assay of the human leukocyte enzymes myeloperoxidase and eosinophil peroxidase. J. Immunol. Methods 126:125-133.
    • (1990) J. Immunol. Methods , vol.126 , pp. 125-133
    • Bozeman, P.M.1    Learn, D.B.2    Thomas, E.L.3
  • 29
    • 0000480359 scopus 로고
    • Lactoperoxidase: Biological function
    • J. Everse, K. E. Everse, and M. B. Grisham, editors. CRC Press, Boca Raton, FL
    • Reiter, N., and J. P. Perraudin. 1991. Lactoperoxidase: biological function. In Peroxidases in Chemistry and Biology, Vol. I. J. Everse, K. E. Everse, and M. B. Grisham, editors. CRC Press, Boca Raton, FL. 143-180.
    • (1991) Peroxidases in Chemistry and Biology , vol.1 , pp. 143-180
    • Reiter, N.1    Perraudin, J.P.2
  • 30
    • 0017375208 scopus 로고
    • The subunit structure of crystalline canine myeloperoxidase
    • Harrison, J. E., S. Pabalan, and J. Schultz. 1977. The subunit structure of crystalline canine myeloperoxidase. Biochim. Biophys. Acta 493:247-259.
    • (1977) Biochim. Biophys. Acta , vol.493 , pp. 247-259
    • Harrison, J.E.1    Pabalan, S.2    Schultz, J.3
  • 32
    • 0021942070 scopus 로고
    • Human eosinophil peroxidase: Purification and characterization
    • Carlson, M. G., C. G. Peterson, and P. Venge. 1985. Human eosinophil peroxidase: purification and characterization. J. Immunol. 134:1875-1879.
    • (1985) J. Immunol. , vol.134 , pp. 1875-1879
    • Carlson, M.G.1    Peterson, C.G.2    Venge, P.3
  • 33
    • 0025051915 scopus 로고
    • Control of pH of airway surface liquid of the ferret trachea in vitro
    • Kyle, H., J. P. Ward, and J. G. Widdicombe. 1990. Control of pH of airway surface liquid of the ferret trachea in vitro. J. Appl. Physiol. 68:135-140.
    • (1990) J. Appl. Physiol. , vol.68 , pp. 135-140
    • Kyle, H.1    Ward, J.P.2    Widdicombe, J.G.3
  • 37
    • 0028105362 scopus 로고
    • Human placenta makes extracellular glutathione peroxidase and secretes it into maternal circulation
    • Avissar, N., C. Eisenmann, J. G. Breen, S. Horowitz, R. K. Miller, and H. J. Cohen. 1994. Human placenta makes extracellular glutathione peroxidase and secretes it into maternal circulation. Am. J. Physiol. 267:E68-E76.
    • (1994) Am. J. Physiol. , vol.267
    • Avissar, N.1    Eisenmann, C.2    Breen, J.G.3    Horowitz, S.4    Miller, R.K.5    Cohen, H.J.6
  • 38
    • 0017226339 scopus 로고
    • Intracellular distinction between peroxidase and catalase in exocrine cells of rat lacrimal gland: A biochemical and cytochemical study
    • Herzog, V., and H. D. Fahimi. 1976. Intracellular distinction between peroxidase and catalase in exocrine cells of rat lacrimal gland: a biochemical and cytochemical study. Histochemistry 46:273-286.
    • (1976) Histochemistry , vol.46 , pp. 273-286
    • Herzog, V.1    Fahimi, H.D.2
  • 39
    • 0021338419 scopus 로고
    • A quantitative study of peroxidase activity in unfixed tissue sections of the guinea-pig thyroid gland
    • Ealey, P. A., B. Henderson, and N. Loveridge. 1984. A quantitative study of peroxidase activity in unfixed tissue sections of the guinea-pig thyroid gland. Histochem. J. 16:111-122.
    • (1984) Histochem. J. , vol.16 , pp. 111-122
    • Ealey, P.A.1    Henderson, B.2    Loveridge, N.3
  • 40
    • 0018670584 scopus 로고
    • An assessment of the DAB methods for cytochemical detection of catalase and peroxidase
    • Fahimi, H. D. 1979. An assessment of the DAB methods for cytochemical detection of catalase and peroxidase. J. Histochem. Cytochem. 27:1365-1366.
    • (1979) J. Histochem. Cytochem. , vol.27 , pp. 1365-1366
    • Fahimi, H.D.1
  • 41
    • 0026077397 scopus 로고
    • Endothelial superoxide production in the isolated rat heart during early reperfusion after ischemia. A histochemical study
    • Babbs, C. F., M. D. Cregor, J. J. Turek, and S. F. Badylak. 1991. Endothelial superoxide production in the isolated rat heart during early reperfusion after ischemia. A histochemical study. Am. J. Pathol. 139:1069-1080.
    • (1991) Am. J. Pathol. , vol.139 , pp. 1069-1080
    • Babbs, C.F.1    Cregor, M.D.2    Turek, J.J.3    Badylak, S.F.4


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