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Volumn 43, Issue 10-11, 2010, Pages 1572-1587

Peroxidase in chemical and biochemical analysis

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EID: 77954838681     PISSN: 00032719     EISSN: 1532236X     Source Type: Journal    
DOI: 10.1080/00032711003653874     Document Type: Article
Times cited : (20)

References (89)
  • 1
    • 77954856974 scopus 로고
    • Enzyme-linked immunoassay with a fluoride ion selective electrode
    • ed. T. T. Ngo, New York: Plenum Press
    • Alexander, P. W. 1987. Enzyme-linked immunoassay with a fluoride ion selective electrode. In Electrochemical Sensors in Immunological Analysis, ed. T. T. Ngo, 203-210. New York: Plenum Press.
    • (1987) Electrochemical Sensors In Immunological Analysis , pp. 203-210
    • Alexander, P.W.1
  • 2
    • 0020015148 scopus 로고
    • Enzyme-linked immunoassay of human immunoglobulin G with fluoride ion-selective electrode
    • Alexander, P. W. and C. Maitra. 1982. Enzyme-linked immunoassay of human immunoglobulin G with fluoride ion-selective electrode. Anal. Chem. 54: 68-71.
    • (1982) Anal. Chem , vol.54 , pp. 68-71
    • Alexander, P.W.1    Maitra, C.2
  • 3
    • 0023947585 scopus 로고
    • Continuous-flow potentiometric determination of horseradish peroxidase with a fluoride-selective electrode
    • Alexander, P. W. and C. Maitra. 1988. Continuous-flow potentiometric determination of horseradish peroxidase with a fluoride-selective electrode. Anal.Chim. Acta. 208: 173-181.
    • (1988) Anal.Chim. Acta , vol.208 , pp. 173-181
    • Alexander, P.W.1    Maitra, C.2
  • 4
    • 0018381691 scopus 로고
    • Purification of peroxidase-conjugated antibody for enzyme immunoassay by affinity chromatography on concanavalin
    • Arend, J. 1979. Purification of peroxidase-conjugated antibody for enzyme immunoassay by affinity chromatography on concanavalin. A. L. Immunol. Methods. 25: 171-175.
    • (1979) A. L. Immunol. Methods , vol.25 , pp. 171-175
    • Arend, J.1
  • 6
    • 0015297282 scopus 로고
    • An improved color reagent for the determination of blood glucose by the oxidase system
    • Barham, D., and P. Trinder. 1972. An improved color reagent for the determination of blood glucose by the oxidase system. Analyst. 97: 142-145.
    • (1972) Analyst , vol.97 , pp. 142-145
    • Barham, D.1    Trinder, P.2
  • 10
    • 0019718969 scopus 로고
    • 3,3,5,5-tetramethylbenzidine as an Ames test negative chromogen for horseradish peroxidase in enzyme immunoassay
    • Bos, E. S., A. A. van der Doelen, N. van Rooy, and A. H W. M. Schuurs. 1981. 3,3,5,5-tetramethylbenzidine as an Ames test negative chromogen for horseradish peroxidase in enzyme immunoassay. J. Immunoassay. 2: 187-204.
    • (1981) J. Immunoassay , vol.2 , pp. 87-204
    • Bos, E.S.1    van der Doelen, A.A.2    van Rooy, N.3    Schuurs, A.H.W.M.4
  • 11
    • 0020374178 scopus 로고
    • Optimizing the o-phenylenediamine assay for horseradish peroxidase: Effect of phosphate and pH, substrate and enzyme concentrations, and stopping reagents
    • Bovaird, J. H., T. T. Ngo, and H. M. Lenhoff. 1982. Optimizing the o-phenylenediamine assay for horseradish peroxidase: Effect of phosphate and pH, substrate and enzyme concentrations, and stopping reagents. Clin. Chem. 28: 2423-2426.
    • (1982) Clin. Chem , vol.28 , pp. 2423-2426
    • Bovaird, J.H.1    Ngo, T.T.2    Lenhoff, H.M.3
  • 12
    • 0025038084 scopus 로고
    • Comparison of particulate 3,30,5,50-tetramethylbenzidine and 3,30-diaminobenzidine as chromogenic substrates for immunoblot
    • Brand, J. A., V. C. W. Tsang, W. Zhou, and S. B. Shukala. 1990. Comparison of particulate 3,30,5,50-tetramethylbenzidine and 3,30-diaminobenzidine as chromogenic substrates for immunoblot. BioTechniques. 8: 58-60.
    • (1990) BioTechniques , vol.8 , pp. 58-60
    • Brand, J.A.1    Tsang, V.C.W.2    Zhou, W.3    Shukala, S.B.4
  • 14
    • 0028116603 scopus 로고
    • A stable water-soluble tetramethylbenzidine-2-hydroxypropyl-ß-cyclodextrin inclusion complex and its applications in enzyme assays
    • Cattaneo, M. V., and J. H. T. Luong. 1994. A stable water-soluble tetramethylbenzidine-2-hydroxypropyl-ß-cyclodextrin inclusion complex and its applications in enzyme assays. Anal. Biochem. 223: 313-320.
    • (1994) Anal. Biochem , vol.223 , pp. 313-320
    • Cattaneo, M.V.1    Luong, J.H.T.2
  • 15
    • 0019464118 scopus 로고
    • In vitro retrograde neuritic transport of horseradish-peroxidase isoenzymes by sympathetic neurons
    • Chan, K. Y., A. H. Bunt, and R. H. Haschke. 1981. In vitro retrograde neuritic transport of horseradish-peroxidase isoenzymes by sympathetic neurons. Neuroscience. 6: 59-69.
    • (1981) Neuroscience , vol.6 , pp. 59-69
    • Chan, K.Y.1    Bunt, A.H.2    Haschke, R.H.3
  • 16
    • 77954841392 scopus 로고    scopus 로고
    • Biosensors based on "wired" peroxidases
    • ed. V. C. Yang and T. T. Ngo, New York: Kluwer Academic Press/ Plenum
    • Chen, Q., A. Heller, and G. L. Kenausis. 2000. Biosensors based on "wired" peroxidases. In Biosensors and Their Applications, ed. V. C. Yang and T. T. Ngo. 99-112. New York: Kluwer Academic Press/ Plenum.
    • (2000) Biosensors and Their Applications , pp. 99-112
    • Chen, Q.1    Heller, A.2    Kenausis, G.L.3
  • 17
    • 0023610554 scopus 로고
    • Interference in an electrochemical detection system for peroxidase-linked reactions based on a fluoride ion-selective electrode
    • Cowell, D. C., and P. A. E. Ford. 1987. Interference in an electrochemical detection system for peroxidase-linked reactions based on a fluoride ion-selective electrode. Clin. Chem. 33: 1458-1460.
    • (1987) Clin. Chem , vol.33 , pp. 1458-1460
    • Cowell, D.C.1    Ford, P.A.E.2
  • 18
    • 0002154654 scopus 로고
    • Horseradish peroxidase: Structure and kinetic properties
    • ed. J. Everse, K. E. Everse, and M. B. Grisham, Boca Raton, FL: CRC Press
    • Dunford, H. B. 1991. Horseradish peroxidase: Structure and kinetic properties. In Peroxidases in Chemistry and Biology, Vol. II, ed. J. Everse, K. E. Everse, and M. B. Grisham. 1-24. Boca Raton, FL: CRC Press.
    • (1991) Peroxidases In Chemistry and Biology , vol.2 , pp. 1-24
    • Dunford, H.B.1
  • 19
    • 0003514551 scopus 로고    scopus 로고
    • New York, NY: Wiley-VCH
    • Dunford, H. B. 1999. Heme Peroxidase, 33-57. New York, NY: Wiley-VCH.
    • (1999) Heme Peroxidase , pp. 33-57
    • Dunford, H.B.1
  • 20
    • 0000805517 scopus 로고
    • On the function and mechanismof action of peroxidase
    • Dunford, H. B., and J. S. Stillman. 1976. On the function and mechanismof action of peroxidase. Coord. Chem. Rev. 19: 187-251.
    • (1976) Coord. Chem. Rev , vol.19 , pp. 187-251
    • Dunford, H.B.1    Stillman, J.S.2
  • 23
    • 0343788608 scopus 로고
    • The Ngo-Lenhoff (MBTH-DMAB) peroxidase assay
    • ed. T. T. Ngo and H. M. Lenhoff, New York: Plenum Press
    • Geoghegan, W. D. 1985. The Ngo-Lenhoff (MBTH-DMAB) peroxidase assay. In Enzyme-Mediated Immunoassay, ed. T. T. Ngo and H. M. Lenhoff. 451-465. New York: Plenum Press.
    • (1985) Enzyme-Mediated Immunoassay , pp. 451-465
    • Geoghegan, W.D.1
  • 24
    • 0020512164 scopus 로고
    • Adaptation of Ngo-Lenhoff peroxidase assay for solid phase ELISA
    • Geoghegan, W. D., F. M. Struve, and R. E. Jordon. 1983. Adaptation of Ngo-Lenhoff peroxidase assay for solid phase ELISA. J. Immunol. Methods 60: 61-68.
    • (1983) J. Immunol. Methods , vol.60 , pp. 61-68
    • Geoghegan, W.D.1    Struve, F.M.2    Jordon, R.E.3
  • 25
    • 17744404633 scopus 로고
    • Use of Enzyme in analytical chemistry
    • Guilbault, G. G. 1968. Use of Enzyme in analytical chemistry. Anal. Chem. 40: 459R-471R.
    • (1968) Anal. Chem , vol.40
    • Guilbault, G.G.1
  • 28
    • 0014310508 scopus 로고
    • New substrates for the fluorometric determination of oxidase enzymes
    • Guilbault, G. G., P. J. Brignac, and M. Juneau. 1968. New substrates for the fluorometric determination of oxidase enzymes. Anal. Chem. 40: 1256-1263.
    • (1968) Anal. Chem , vol.40 , pp. 1256-1263
    • Guilbault, G.G.1    Brignac, P.J.2    Juneau, M.3
  • 29
    • 0014236699 scopus 로고
    • Homovanillic acid as a fluorometric substrate for oxidative enzymes
    • Guilbault, G. G., P. J. Brignac, and M. Zimmer. 1968. Homovanillic acid as a fluorometric substrate for oxidative enzymes. Anal. Chem. 40: 190-196.
    • (1968) Anal. Chem , vol.40 , pp. 190-196
    • Guilbault, G.G.1    Brignac, P.J.2    Zimmer, M.3
  • 30
    • 0017890597 scopus 로고
    • Calcium-related properties if horseradish peroxidase
    • Haschke, R. H., and J. M. Friedhoff. 1978. Calcium-related properties if horseradish peroxidase. Biochem. Biophys. Res. Commun. 80: 1039-1042.
    • (1978) Biochem. Biophys. Res. Commun , vol.80 , pp. 1039-1042
    • Haschke, R.H.1    Friedhoff, J.M.2
  • 31
    • 0024384230 scopus 로고
    • Polyacrylic polyhydrazides as reagents for detection of glycoproteins
    • Heimgartner, U., B. Kozulic, and K. Mosbach. 1989. Polyacrylic polyhydrazides as reagents for detection of glycoproteins. Anal. Biochem. 181: 182-189.
    • (1989) Anal. Biochem , vol.181 , pp. 182-189
    • Heimgartner, U.1    Kozulic, B.2    Mosbach, K.3
  • 32
    • 0025050674 scopus 로고
    • Polyacrylic polyhydrazides as novel reagents for detection of antibodies in immunoblotting assays
    • Heimgartner, U., B. Kozulic, and K. Mosbach. 1990. Polyacrylic polyhydrazides as novel reagents for detection of antibodies in immunoblotting assays. J. Immunol. Methods. 132: 239-245.
    • (1990) J. Immunol. Methods , vol.132 , pp. 239-245
    • Heimgartner, U.1    Kozulic, B.2    Mosbach, K.3
  • 33
    • 0022371526 scopus 로고
    • Enhanced ultrastructural visualization of the horseradish peroxidase-tetramethybenzidine reaction product
    • Henry, M. A., L. E. Westrum, and L. R. Johnson. 1985. Enhanced ultrastructural visualization of the horseradish peroxidase-tetramethybenzidine reaction product. J. Histochem. Cytochem. 33: 1256-1259.
    • (1985) J. Histochem. Cytochem , vol.33 , pp. 1256-1259
    • Henry, M.A.1    Westrum, L.E.2    Johnson, L.R.3
  • 34
    • 0003648956 scopus 로고    scopus 로고
    • Bioconjugation Techniques
    • CA: Academic Press
    • Hermanson, G. T. 1996. Bioconjugation Techniques. San Diego, CA: Academic Press.
    • (1996) San Diego
    • Hermanson, G.T.1
  • 35
    • 77954859692 scopus 로고
    • Enzyme labeling with N,N'-ophenylenedimaleimide
    • ed. E. Ishikawa, T. Kawai, and K. Miyai, Tokyo: Igaku-Shoin
    • Ishikawa, E., Y. Hamaguchi, and S. Yoshitake. 1981. Enzyme labeling with N,N'-ophenylenedimaleimide. In Enzyme Immunoassay, ed. E. Ishikawa, T. Kawai, and K. Miyai. 67-80. Tokyo: Igaku-Shoin.
    • (1981) In Enzyme Immunoassay , pp. 67-80
    • Ishikawa, E.1    Hamaguchi, Y.2    Yoshitake, S.3
  • 36
    • 0345367565 scopus 로고
    • Method for enzyme-labeling of antigens, antibodies and their fragments
    • ed. T. T. Ngo. New York: Plenum
    • Ishikawa, E., S. Hashida, T. Kohno, and K. Tanaka. 1988. Method for enzyme-labeling of antigens, antibodies and their fragments. In Nonisotopic Immunoassay, ed. T. T. Ngo. New York: Plenum.
    • (1988) Nonisotopic Immunoassay
    • Ishikawa, E.1    Hashida, S.2    Kohno, T.3    Tanaka, K.4
  • 37
    • 0020565866 scopus 로고
    • Enzyme-labeling of antibodies and their fragments for enzyme immunoassay and immuno histochemical staining
    • Ishikawa, E., M. Imagawa, S. Hashida, S. Yoshitake, Y. Hamaguchi, and T. Ueno. 1983. Enzyme-labeling of antibodies and their fragments for enzyme immunoassay and immuno histochemical staining. J. Immun. 4: 209-327.
    • (1983) J. Immun , vol.4 , pp. 209-327
    • Ishikawa, E.1    Imagawa, M.2    Hashida, S.3    Yoshitake, S.4    Hamaguchi, Y.5    Ueno, T.6
  • 39
    • 0012893529 scopus 로고
    • A more stable maleimide, N-(4-Carboxycyclohexylmethyl)maleimide, for enzyme labeling
    • ed. E. Ishikawa, T. Kawai, and K. Miyai, Tokyo: Igaku-Shoin
    • Ishikawa, E., Y. Yamada, S. Yashitake, and H. Kawaguchi. 1981. A more stable maleimide, N-(4-Carboxycyclohexylmethyl)maleimide, for enzyme labeling. In Enzyme Immunoassay, ed. E. Ishikawa, T. Kawai, and K. Miyai. 90-105. Tokyo: Igaku-Shoin.
    • (1981) Enzyme Immunoassay , pp. 90-105
    • Ishikawa, E.1    Yamada, Y.2    Yashitake, S.3    Kawaguchi, H.4
  • 40
    • 0141657568 scopus 로고
    • Antibodies
    • ed. E. Ishikawa, T. Kawai, and K. Miyai, Tokyo: Igaku-Shoin
    • Ishikawa, E., and S. Yoshitake. 1981. Antibodies. In Enzyme Immunoassay, ed. E. Ishikawa, T. Kawai, and K. Miyai. 263-272. Tokyo: Igaku-Shoin.
    • (1981) Enzyme Immunoassay , pp. 263-272
    • Ishikawa, E.1    Yoshitake, S.2
  • 41
    • 0028838209 scopus 로고
    • Stable and general-purpose chemiluminescent detection system for peroxidase employing thiazole compound enhancer and some additives
    • Iwata, R., H. Ito, T. Hayashi, Y. Sekine, N. Koyama, and M. Yamaki. 1995. Stable and general-purpose chemiluminescent detection system for peroxidase employing thiazole compound enhancer and some additives. Anal. Biochem. 231: 170-174.
    • (1995) Anal. Biochem , vol.231 , pp. 170-174
    • Iwata, R.1    Ito, H.2    Hayashi, T.3    Sekine, Y.4    Koyama, N.5    Yamaki, M.6
  • 46
    • 0017381491 scopus 로고
    • Visualization of peroxidase isozymes with eugenol, a noncarcinogenic substrate
    • Liu, E. H., and D. M. Gibson. 1977. Visualization of peroxidase isozymes with eugenol, a noncarcinogenic substrate. Anal. Biochem. 79: 597-601.
    • (1977) Anal. Biochem , vol.79 , pp. 597-601
    • Liu, E.H.1    Gibson, D.M.2
  • 48
    • 0017853307 scopus 로고
    • Tetramethylbenzidine for horseradish peroxidase neurohistochemistry: A non-carcinogenic blue reaction-product with superior sensitivity for visualizing neural afferents and efferents
    • Mesulam, M. -M. 1978. Tetramethylbenzidine for horseradish peroxidase neurohistochemistry: A non-carcinogenic blue reaction-product with superior sensitivity for visualizing neural afferents and efferents. J. Histochem. Cytochem. 26: 106-117.
    • (1978) J. Histochem. Cytochem , vol.26 , pp. 106-117
    • Mesulam M., -M.1
  • 49
    • 0004251667 scopus 로고
    • Fluorimetic measurements in enzyme immunoassays
    • ed. T. T. Ngo and H. M. Lenhoff, New York: Plenum Press
    • Milby, K. H. 1985. Fluorimetic measurements in enzyme immunoassays. In Enzyme-Mediated Immunoassay, ed. T. T. Ngo and H. M. Lenhoff. 325-341. New York: Plenum Press.
    • (1985) Enzyme-Mediated Immunoassay , pp. 325-341
    • Milby, K.H.1
  • 51
    • 0019509897 scopus 로고
    • Comparison of horseradish peroxidase visualization methods
    • Morrell, J. I., L. M. Greenberger, and D. W. Pfaff. 1981. Comparison of horseradish peroxidase visualization methods. J. Histochem. Cytochem. 29: 903-916.
    • (1981) J. Histochem. Cytochem , vol.29 , pp. 903-916
    • Morrell, J.I.1    Greenberger, L.M.2    Pfaff, D.W.3
  • 52
    • 0033867054 scopus 로고    scopus 로고
    • Quantitation of monosodium glutamate using immobilized glutamate oxidase/peroxidase and flow injection analysis
    • Munkasingh, U., D. Narinesingh, and T. T. Ngo. 2000. Quantitation of monosodium glutamate using immobilized glutamate oxidase/peroxidase and flow injection analysis. Anal. Lett. 33: 2407-2423.
    • (2000) Anal. Lett , vol.33 , pp. 2407-2423
    • Munkasingh, U.1    Narinesingh, D.2    Ngo, T.T.3
  • 53
    • 39049174255 scopus 로고
    • Enzyme-labeled antibodies preparation and application for the localization of antigens
    • Nakane, P., and G. R. Pierce. 1967. Enzyme-labeled antibodies preparation and application for the localization of antigens. J. Histochem. Cytochem. 12: 929-931.
    • (1967) J. Histochem. Cytochem , vol.12 , pp. 929-931
    • Nakane, P.1    Pierce, G.R.2
  • 54
    • 51249174236 scopus 로고
    • Ultrasensitive chromogen system for horseradish peroxidase using 3-methyl-2-benzothiazolinone hydrazone and N-phenyldiethanolamine
    • Ngo, T. T. 1985. Ultrasensitive chromogen system for horseradish peroxidase using 3-methyl-2-benzothiazolinone hydrazone and N-phenyldiethanolamine. Appl. Biochem. Biotechnol. 11: 257-268.
    • (1985) Appl. Biochem. Biotechnol , vol.11 , pp. 257-268
    • Ngo, T.T.1
  • 56
    • 85202762934 scopus 로고
    • Enzyme systems and enzyme conjugates for solid-phase ELISA
    • ed. J. E. Butler, Boca Raton: CRC Press
    • Ngo, T. T. 1991. Enzyme systems and enzyme conjugates for solid-phase ELISA. In Immunochemistry of Solid-Phase Immunoassayed, ed. J. E. Butler. 85-102. Boca Raton: CRC Press.
    • (1991) Immunochemistry of Solid-Phase Immunoassayed , pp. 85-102
    • Ngo, T.T.1
  • 57
    • 0034428566 scopus 로고    scopus 로고
    • Development in immunoassay technology
    • San Diego: Academic Press
    • Ngo, T. T. 2000. Development in immunoassay technology. In METHODS, volume 22, No. 1. San Diego: Academic Press.
    • (2000) METHODS , vol.22 , Issue.1
    • Ngo, T.T.1
  • 58
    • 49149140663 scopus 로고
    • A sensitive and versatile chromogenic assay for peroxidase and peroxidase coupled reactions
    • Ngo, T. T., and H. M. Lenhoff. 1980. A sensitive and versatile chromogenic assay for peroxidase and peroxidase coupled reactions. Anal. Biochem. 105: 389-397.
    • (1980) Anal. Biochem , vol.105 , pp. 389-397
    • Ngo, T.T.1    Lenhoff, H.M.2
  • 60
    • 0019450984 scopus 로고
    • A technique for preparing defined conjugates of horseradish peroxidase and immunoglobulin
    • Nilsson, P., N. R. Bergquist, and M. S. Grundy. 1981. A technique for preparing defined conjugates of horseradish peroxidase and immunoglobulin. J. Immunol. Methods. 41: 81-93.
    • (1981) J. Immunol. Methods , vol.41 , pp. 81-93
    • Nilsson, P.1    Bergquist, N.R.2    Grundy, M.S.3
  • 61
    • 0018802741 scopus 로고
    • Calcium binding by horseradish peroxidase C and the heme environmental structure
    • Ogawa, S., Y. Shiro, and I. Marishima. 1979. Calcium binding by horseradish peroxidase C and the heme environmental structure. Biochem. Biophys. Res. Commun. 90: 674-678.
    • (1979) Biochem. Biophys. Res. Commun , vol.90 , pp. 674-678
    • Ogawa, S.1    Shiro, Y.2    Marishima, I.3
  • 62
    • 0001598453 scopus 로고
    • Electrocatalytic reduction of hydrogen peroxide via direct electric transfer from pyrolytic graphite electrodes to irreversibly adsorbed cytochrome c peroxidase
    • Paddock, R. M., and E. F. Bowden. 1989. Electrocatalytic reduction of hydrogen peroxide via direct electric transfer from pyrolytic graphite electrodes to irreversibly adsorbed cytochrome c peroxidase. J. Electroanal. Interf. Electrochem. 260: 487-494.
    • (1989) J. Electroanal. Interf. Electrochem , vol.260 , pp. 487-494
    • Paddock, R.M.1    Bowden, E.F.2
  • 66
    • 0002784336 scopus 로고
    • Chromogenic substrate for enzyme immunoassay
    • ed. T. T. Ngo, New York: Plenum Press
    • Porstman, P., and T. Porstman. 1988. Chromogenic substrate for enzyme immunoassay. In Nonisotopic Immunoassay, ed. T. T. Ngo. 57-84. New York: Plenum Press.
    • (1988) Nonisotopic Immunoassay , pp. 57-84
    • Porstman, P.1    Porstman, T.2
  • 67
    • 0019370306 scopus 로고
    • Temperature dependence rise in activity of horseradish peroxidase caused by non-ionic detergents and its use in enzyme-immunoassay
    • Porstman, P., T. Porstman, D. Gaede, E. Nugel, and E. Egger. 1981. Temperature dependence rise in activity of horseradish peroxidase caused by non-ionic detergents and its use in enzyme-immunoassay. Clin. Chim. Acta. 109: 175-181.
    • (1981) Clin. Chim. Acta , vol.109 , pp. 175-181
    • Porstman, P.1    Porstman, T.2    Gaede, D.3    Nugel, E.4    Egger, E.5
  • 68
    • 0030578871 scopus 로고    scopus 로고
    • Peroxidase-modified electrode: Fundamentals and application
    • Ruzgas, T., E. Csoregi, and J. Emneus. 1996. Peroxidase-modified electrode: Fundamentals and application. Anal. Chim. Acta. 330: 123-138.
    • (1996) Anal. Chim. Acta , vol.330 , pp. 123-138
    • Ruzgas, T.1    Csoregi, E.2    Emneus, J.3
  • 70
    • 0022976015 scopus 로고
    • Presence of endogenous calcium ion and its functional and structural regulation in horseradish peroxidase
    • Shiro, Y., M. Kuromo, and I. Morishima. 1986. Presence of endogenous calcium ion and its functional and structural regulation in horseradish peroxidase. J. Biol. Chem. 261: 9382-9390.
    • (1986) J. Biol. Chem , vol.261 , pp. 9382-9390
    • Shiro, Y.1    Kuromo, M.2    Morishima, I.3
  • 71
    • 0019989517 scopus 로고
    • An electrochemical assay system for peroxidase and peroxidase-coupled reactions on a fluoride ion-selective electrode
    • Siddiqi, I. W. 1982. An electrochemical assay system for peroxidase and peroxidase-coupled reactions on a fluoride ion-selective electrode. Clin. Chem. 28: 1962.
    • (1982) Clin. Chem , vol.28 , pp. 1962
    • Siddiqi, I.W.1
  • 74
    • 0003072603 scopus 로고
    • Determination of glucose in blood using glucose oxidase with an alternative oxygen acceptor
    • Trinder, P. 1969. Determination of glucose in blood using glucose oxidase with an alternative oxygen acceptor. Ann. Clin. Biochem. 6: 24-27.
    • (1969) Ann. Clin. Biochem , vol.6 , pp. 24-27
    • Trinder, P.1
  • 75
    • 0018937882 scopus 로고
    • On the mutagenic action of some enzyme immunoassay substrates
    • Voogd, C. E., J. J. van der Stel, and J. J. J. A. A. Jacob. 1980. On the mutagenic action of some enzyme immunoassay substrates. J. Immunol. Methods. 36: 55-61.
    • (1980) J. Immunol. Methods , vol.36 , pp. 55-61
    • Voogd, C.E.1    van der Stel, J.J.2    Jacob, J.J.J.A.A.3
  • 76
    • 0000436609 scopus 로고
    • Hydrogen peroxide and beta-nicotinamide adenine dinucleotide sensing amperometric electrodes based on electric connection of horseradish peroxidase redox centers to electrodes through a three-dimensional electron relaying polymer network
    • Vreeke, M., R. Maidan, and A. Heller. 1992. Hydrogen peroxide and beta-nicotinamide adenine dinucleotide sensing amperometric electrodes based on electric connection of horseradish peroxidase redox centers to electrodes through a three-dimensional electron relaying polymer network. Anal. Chem. 64: 3084-3090.
    • (1992) Anal. Chem , vol.64 , pp. 3084-3090
    • Vreeke, M.1    Maidan, R.2    Heller, A.3
  • 77
    • 0001371680 scopus 로고
    • A thermostable hydrogen peroxide sensor based on "wiring" of soybean peroxidase
    • Vreeke, M., K. Yong, and A. Heller. 1995. A thermostable hydrogen peroxide sensor based on "wiring" of soybean peroxidase. Anal.Chem. 67: 4247-4349.
    • (1995) Anal.Chem , vol.67 , pp. 4247-4349
    • Vreeke, M.1    Yong, K.2    Heller, A.3
  • 79
    • 0025952763 scopus 로고
    • Amperometric biosensing of organic peroxide with peroxidase-modified electrodes
    • Wang, J., B. Frieha, and N. Naser. 1991. Amperometric biosensing of organic peroxide with peroxidase-modified electrodes. Anal. Chim. Acta. 254: 81-88.
    • (1991) Anal. Chim. Acta , vol.254 , pp. 81-88
    • Wang, J.1    Frieha, B.2    Naser, N.3
  • 80
    • 0017041348 scopus 로고
    • Covalent structure of glycoprotein horseradish peroxidase (EC 1.11.1.7)
    • Welinder, K. G. 1976. Covalent structure of glycoprotein horseradish peroxidase (EC 1.11.1.7). FEBS Lett. 72: 19-23.
    • (1976) FEBS Lett , vol.72 , pp. 19-23
    • Welinder, K.G.1
  • 81
    • 0018488111 scopus 로고
    • Amino acid sequence studies of horseradish peroxidase. Amino and carboxyl termini, cyanogen bromide and tryptic fragments, a complete sequence, and some structural characteristics of horseradish peroxidase c
    • Welinder, K. G. 1979. Amino acid sequence studies of horseradish peroxidase. Amino and carboxyl termini, cyanogen bromide and tryptic fragments, a complete sequence, and some structural characteristics of horseradish peroxidase c. Eur. L. Biochem. 96: 483-502.
    • (1979) Eur. L. Biochem , vol.96 , pp. 483-502
    • Welinder, K.G.1
  • 82
    • 0022427616 scopus 로고
    • Plant preoxidases. Their primary, secondary and tertiary structures, and relation to cytochrome c peroxidase
    • Welinder, K. G. 1985. Plant preoxidases. Their primary, secondary and tertiary structures, and relation to cytochrome c peroxidase. Eur. J. Biochem. 151: 497-504.
    • (1985) Eur. J. Biochem , vol.151 , pp. 497-504
    • Welinder, K.G.1
  • 83
    • 0001778765 scopus 로고
    • Plant peroxidases: Structure-Function Relationship
    • ed. C. Penel, Th. Gaspar, and H. Greppin, Switzerland: University of Geneva
    • Welinder, K. G. 1992. Plant peroxidases: Structure-Function Relationship. In Plant Peroxidases 1980-1990, ed. C. Penel, Th. Gaspar, and H. Greppin. 1-24. Switzerland: University of Geneva.
    • (1992) Plant Peroxidases 1980-1990 , pp. 1-24
    • Welinder, K.G.1
  • 84
    • 0015252106 scopus 로고
    • Amino acid sequence studies of horseradish peroxidase
    • Welinder, K. G., and L. B. Smillie. 1972. Amino acid sequence studies of horseradish peroxidase. II. Thermolytic Peptides. 50: 63-90.
    • (1972) II. Thermolytic Peptides , vol.50 , pp. 63-90
    • Welinder, K.G.1    Smillie, L.B.2
  • 86
    • 0023876319 scopus 로고
    • The avidin-biotin complex in bioanalytical applications
    • Wilchek, M., and E. A. Bayer. 1988. The avidin-biotin complex in bioanalytical applications. Anal. Biochem. 171: 1-32.
    • (1988) Anal. Biochem , vol.171 , pp. 1-32
    • Wilchek, M.1    Bayer, E.A.2
  • 88
    • 0347089960 scopus 로고
    • Formation of blue chromophore from oxidative coupling of aminoantipyrine with chromotropic acid in the presence of peroxide and horseradish peroxidase
    • Wong, R. C., T. T. Ngo, and H. M. Lenhoff. 1981. Formation of blue chromophore from oxidative coupling of aminoantipyrine with chromotropic acid in the presence of peroxide and horseradish peroxidase. Intl. J. Biochem. 13: 159-163.
    • (1981) Intl. J. Biochem , vol.13 , pp. 159-163
    • Wong, R.C.1    Ngo, T.T.2    Lenhoff, H.M.3


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