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Volumn 345, Issue 2, 2005, Pages 227-236

Enhanced sensitivity and precision in an enzyme-linked immunosorbent assay with fluorogenic substrates compared with commonly used chromogenic substrates

Author keywords

Affinity constant determination; ELISA; Enzyme substrate; Fluorescence; Fluorogenic substrate; Immuno assay; Level of detection; Level of quantitation; Precision; Sensitivity; Z factor

Indexed keywords

CHROMOGENICS; ENZYMATIC HYDROLYSIS; FLUORESCENCE; SIGNAL TO NOISE RATIO;

EID: 25444513733     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2005.07.026     Document Type: Article
Times cited : (31)

References (29)
  • 1
    • 0025599858 scopus 로고
    • Evaluation of the use of chromogenic and fluorogenic substrates in solid-phase enzyme linked immunosorbent assay (ELISA)
    • J.R. Crowther, L. Angarita, and J. Anderson Evaluation of the use of chromogenic and fluorogenic substrates in solid-phase enzyme linked immunosorbent assay (ELISA) Biologicals 18 1990 331 336
    • (1990) Biologicals , vol.18 , pp. 331-336
    • Crowther, J.R.1    Angarita, L.2    Anderson, J.3
  • 2
    • 0026562350 scopus 로고
    • A sensitive competitive ELISA for 2,4-dinitrophenol using 3,6-fluoresecein diphosphate as a fluorogenic substrate
    • Z. Huang, N.A. Olson, W. You, and R.P. Haugland A sensitive competitive ELISA for 2,4-dinitrophenol using 3,6-fluoresecein diphosphate as a fluorogenic substrate J. Immunol. Methods 149 1992 261 266
    • (1992) J. Immunol. Methods , vol.149 , pp. 261-266
    • Huang, Z.1    Olson, N.A.2    You, W.3    Haugland, R.P.4
  • 3
    • 0026535388 scopus 로고
    • DNA hybridization assay using AttoPhos, a fluorescent substrate for alkaline phosphatase
    • R.J. Cano, M.J. Torres, R.E. Klem, and J.C. Palomares DNA hybridization assay using AttoPhos, a fluorescent substrate for alkaline phosphatase BioTechniques 12 1992 264 268
    • (1992) BioTechniques , vol.12 , pp. 264-268
    • Cano, R.J.1    Torres, M.J.2    Klem, R.E.3    Palomares, J.C.4
  • 4
    • 0025911913 scopus 로고
    • A comparison of the sensitivity and specificity of enzyme immunoassays and time-resolved fluoroimmunoassay
    • I.M. Roberts, S.L. Jones, R.R. Premier, and J.C. Cox A comparison of the sensitivity and specificity of enzyme immunoassays and time-resolved fluoroimmunoassay J. Immunol. Methods 143 1991 49 56
    • (1991) J. Immunol. Methods , vol.143 , pp. 49-56
    • Roberts, I.M.1    Jones, S.L.2    Premier, R.R.3    Cox, J.C.4
  • 5
    • 0032004080 scopus 로고    scopus 로고
    • Optimisation of a heterogeneous non-competitive flow immunoassay comparing fluorescein, peroxidase, and alkaline phosphatase as labels
    • A. Lindgren, J. Emneus, G. Marko-Varga, H. Irth, A. Oosterkamp, and S. Eremin Optimisation of a heterogeneous non-competitive flow immunoassay comparing fluorescein, peroxidase, and alkaline phosphatase as labels J. Immunol. Methods 211 1998 33 42
    • (1998) J. Immunol. Methods , vol.211 , pp. 33-42
    • Lindgren, A.1    Emneus, J.2    Marko-Varga, G.3    Irth, H.4    Oosterkamp, A.5    Eremin, S.6
  • 9
    • 5644236659 scopus 로고    scopus 로고
    • Complexities in horseradish peroxidase-catalyzed oxidation of dihydroxyphenoxazine derivatives: Appropriate ranges for pH values and hydrogen peroxide concentrations in quantitative analysis
    • V. Towne, M. Will, B. Oswald, and Q. Zhao Complexities in horseradish peroxidase-catalyzed oxidation of dihydroxyphenoxazine derivatives: appropriate ranges for pH values and hydrogen peroxide concentrations in quantitative analysis Anal. Biochem. 334 2004 290 296
    • (2004) Anal. Biochem. , vol.334 , pp. 290-296
    • Towne, V.1    Will, M.2    Oswald, B.3    Zhao, Q.4
  • 10
    • 0031573401 scopus 로고    scopus 로고
    • A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: Applications in detecting the activity of phagocyte NADPH oxidase and other oxidases
    • M. Zhou, Z. Diwu, N. Panchuk-Voloshina, and R. Haugland A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: applications in detecting the activity of phagocyte NADPH oxidase and other oxidases Anal. Biochem. 253 1997 162 168
    • (1997) Anal. Biochem. , vol.253 , pp. 162-168
    • Zhou, M.1    Diwu, Z.2    Panchuk-Voloshina, N.3    Haugland, R.4
  • 12
    • 0019297315 scopus 로고
    • New fluorogenic substrates for horseradish peroxidase: Rapid and sensitive assays for hydrogen peroxide and the peroxidase
    • K. Zaitsu, and Y. Ohkura New fluorogenic substrates for horseradish peroxidase: rapid and sensitive assays for hydrogen peroxide and the peroxidase Anal. Biochem. 109 1980 109 113
    • (1980) Anal. Biochem. , vol.109 , pp. 109-113
    • Zaitsu, K.1    Ohkura, Y.2
  • 13
    • 0030003076 scopus 로고    scopus 로고
    • Studies on single alkaline phosphatase molecules: Reaction rate and activation energy of a reaction catalyzed by a single molecule and the effect of thermal denaturation-the death of an enzyme
    • D.B. Craig, E.A. Arriaga, J.C.Y. Wong, H. Lu, and N.J. Dovichi Studies on single alkaline phosphatase molecules: reaction rate and activation energy of a reaction catalyzed by a single molecule and the effect of thermal denaturation-the death of an enzyme J. Am. Chem. Soc. 118 1996 5245
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 5245
    • Craig, D.B.1    Arriaga, E.A.2    Wong, J.C.Y.3    Lu, H.4    Dovichi, N.J.5
  • 14
    • 0000222399 scopus 로고    scopus 로고
    • Detection of attomolar concentrations of alkaline phosphatase by capillary electrophoresis using laser-induced fluorescence detection
    • D.B. Craig, J.C.Y. Wong, and N.J. Dovichi Detection of attomolar concentrations of alkaline phosphatase by capillary electrophoresis using laser-induced fluorescence detection Anal. Chem. 68 1996 697 700
    • (1996) Anal. Chem. , vol.68 , pp. 697-700
    • Craig, D.B.1    Wong, J.C.Y.2    Dovichi, N.J.3
  • 15
    • 0033003760 scopus 로고    scopus 로고
    • A simple statistical parameter for use in evaluation and validation of high throughput screening assays
    • J.H. Zhang, T.D.Y. Chung, and K.R. Oldenburg A simple statistical parameter for use in evaluation and validation of high throughput screening assays J. Biomol. Screen. 4 1999 67 73
    • (1999) J. Biomol. Screen. , vol.4 , pp. 67-73
    • Zhang, J.H.1    Chung, T.D.Y.2    Oldenburg, K.R.3
  • 17
    • 0001200298 scopus 로고
    • Statistical analysis of radioimmunoassay and immunoradiometric (labeled antibody) assays: A generalized weighted, iterative, least squares method for logistic curve fitting
    • International Atomic Energy Agency, Vienna, Austria
    • D. Rodbard, D.M. Hutt, Statistical analysis of radioimmunoassay and immunoradiometric (labeled antibody) assays: a generalized weighted, iterative, least squares method for logistic curve fitting, in: Radioimmunoassay and Related Procedures in Medicine, International Atomic Energy Agency, Vienna, Austria, 1974, pp. 165-190.
    • (1974) Radioimmunoassay and Related Procedures in Medicine , pp. 165-190
    • Rodbard, D.1    Hutt, D.M.2
  • 18
    • 0038156417 scopus 로고    scopus 로고
    • Novel fluorescence based receptor binding assay method for receptors lacking ligand conjugates with preserved affinity: Study on estrogen receptor alpha
    • S. Christoph, and F.J. Meyer-Almes Novel fluorescence based receptor binding assay method for receptors lacking ligand conjugates with preserved affinity: study on estrogen receptor alpha Biopolymers 72 2003 256 263
    • (2003) Biopolymers , vol.72 , pp. 256-263
    • Christoph, S.1    Meyer-Almes, F.J.2
  • 19
    • 2442501720 scopus 로고    scopus 로고
    • Determining appropriate substrate conversion for enzymatic assays in high-throughput screening
    • G. Wu, Y. Yuan, and C.N. Hodge Determining appropriate substrate conversion for enzymatic assays in high-throughput screening J. Biomol. Screen. 8 2003 694 700
    • (2003) J. Biomol. Screen. , vol.8 , pp. 694-700
    • Wu, G.1    Yuan, Y.2    Hodge, C.N.3
  • 20
    • 0036570950 scopus 로고    scopus 로고
    • Development of a homogeneous, fluorescence resonance energy transfer-based in vitro recruitment assay for peroxisome proliferator-activated receptor delta via selection of active LXXLL coactivator peptides
    • K.A. Drake, J.H. Zhang, R.K. Harrison, and G.M. McGeehan Development of a homogeneous, fluorescence resonance energy transfer-based in vitro recruitment assay for peroxisome proliferator-activated receptor delta via selection of active LXXLL coactivator peptides Anal. Biochem. 304 2002 63 69
    • (2002) Anal. Biochem. , vol.304 , pp. 63-69
    • Drake, K.A.1    Zhang, J.H.2    Harrison, R.K.3    McGeehan, G.M.4
  • 21
    • 0036047826 scopus 로고    scopus 로고
    • A colorimetric and fluorometric microplate assay for the detection of microcystin-LR in drinking water without preconcentration
    • N. Bouaicha, I. Maatouk, G. Vincent, and Y. Levi A colorimetric and fluorometric microplate assay for the detection of microcystin-LR in drinking water without preconcentration Food Chem. Toxicol. 40 2002 1677 1683
    • (2002) Food Chem. Toxicol. , vol.40 , pp. 1677-1683
    • Bouaicha, N.1    Maatouk, I.2    Vincent, G.3    Levi, Y.4
  • 22
    • 0034093667 scopus 로고    scopus 로고
    • Phosphatase activities of endolithic communities in rocks of the Antarctic dry valleys
    • M. Banerjee, B.A. Whitton, and D.D. Wynn-Williams Phosphatase activities of endolithic communities in rocks of the Antarctic dry valleys Microb. Ecol. 39 2000 80 91
    • (2000) Microb. Ecol. , vol.39 , pp. 80-91
    • Banerjee, M.1    Whitton, B.A.2    Wynn-Williams, D.D.3
  • 23
    • 0030729758 scopus 로고    scopus 로고
    • Quantification of gene expression with a secreted alkaline phosphatase reporter system
    • T.T. Yang, P. Sinai, P.A. Kitts, and S.R. Kain Quantification of gene expression with a secreted alkaline phosphatase reporter system BioTechniques 23 1997 1110 1114
    • (1997) BioTechniques , vol.23 , pp. 1110-1114
    • Yang, T.T.1    Sinai, P.2    Kitts, P.A.3    Kain, S.R.4
  • 24
    • 3442881347 scopus 로고    scopus 로고
    • Measurement of enzyme kinetics using microscale steady-state kinetic analysis
    • N.J. Gleason, and J.D. Carbeck Measurement of enzyme kinetics using microscale steady-state kinetic analysis Langmuir 20 2004 6374 6381
    • (2004) Langmuir , vol.20 , pp. 6374-6381
    • Gleason, N.J.1    Carbeck, J.D.2
  • 25
    • 0142227215 scopus 로고    scopus 로고
    • The first fluorogenic assay for detecting a Baeyer-Villigerase activity in microbial cells
    • M.C. Gutierrez, A. Sleegers, H.D. Simpson, V. Alphand, and R. Furstoss The first fluorogenic assay for detecting a Baeyer-Villigerase activity in microbial cells Org. Biomol. Chem. 1 2003 3500 3506
    • (2003) Org. Biomol. Chem. , vol.1 , pp. 3500-3506
    • Gutierrez, M.C.1    Sleegers, A.2    Simpson, H.D.3    Alphand, V.4    Furstoss, R.5
  • 27
    • 0030573412 scopus 로고    scopus 로고
    • Fast determination of low-level cytochrome P-450 1A1 activity by high-performance liquid chromatography with fluorescence or visible absorbance detection
    • I. Leclercq, J.P. Desager, C. Vandenplas, and Y. Horsmans Fast determination of low-level cytochrome P-450 1A1 activity by high-performance liquid chromatography with fluorescence or visible absorbance detection J. Chromatogr. B Biomed. Appl. 681 1996 227 232
    • (1996) J. Chromatogr. B Biomed. Appl. , vol.681 , pp. 227-232
    • Leclercq, I.1    Desager, J.P.2    Vandenplas, C.3    Horsmans, Y.4
  • 28
    • 0035424461 scopus 로고    scopus 로고
    • Surface phosphophilicity of aluminum-containing adjuvants probed by their efficiency for catalyzing the P-O bond cleavage with chromogenic and fluorogenic substrates
    • Q. Zhao, and R. Sitrin Surface phosphophilicity of aluminum-containing adjuvants probed by their efficiency for catalyzing the P-O bond cleavage with chromogenic and fluorogenic substrates Anal. Biochem. 295 2001 76 81
    • (2001) Anal. Biochem. , vol.295 , pp. 76-81
    • Zhao, Q.1    Sitrin, R.2
  • 29
    • 0021964141 scopus 로고
    • Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay
    • B. Friguet, A.F. Chaffotte, L. Djavadi-Ohaniance, and M.E. Goldberg Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay J. Immunol. Methods 77 1985 305 319
    • (1985) J. Immunol. Methods , vol.77 , pp. 305-319
    • Friguet, B.1    Chaffotte, A.F.2    Djavadi-Ohaniance, L.3    Goldberg, M.E.4


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