메뉴 건너뛰기




Volumn 40, Issue 3, 1997, Pages 278-287

Fluorescence energy transfer-sensitized photobleaching of a fluorescent label as a tool to study donor-acceptor distance distributions and dynamics in protein assemblies: Studies of a complex of biotinylated IgM with streptavidin and aggregates of concanavalin A

Author keywords

Concanavalin A; Fluorescence resonance energy transfer; Fluorescent probes; Photobleaching; Protein assemblies

Indexed keywords

BIOTIN; CONCANAVALIN A; DODECYL SULFATE SODIUM; DYE; FLUORESCENT DYE; IMMUNOGLOBULIN M; PHYCOERYTHRIN; STREPTAVIDIN;

EID: 0030664217     PISSN: 10111344     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1011-1344(97)00070-5     Document Type: Article
Times cited : (23)

References (35)
  • 1
    • 0017795758 scopus 로고
    • Fluorescence energy transfer as a spectroscopic ruler
    • L. Stryer, Fluorescence energy transfer as a spectroscopic ruler, Annu. Rev. Biochem., 47 (1978) 819-846.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 819-846
    • Stryer, L.1
  • 3
    • 0023487834 scopus 로고
    • Fluorescence energy transfer and membrane potential measurements monitor dynamic properties of cell membranes: A critical review
    • J. Szöllösi, S. Damjanovich, S.A. Mulhern, L. Trón, Fluorescence energy transfer and membrane potential measurements monitor dynamic properties of cell membranes: a critical review. Prog. Biophys. Mol. Biol., 48 (1987) 65-87.
    • (1987) Prog. Biophys. Mol. Biol. , vol.48 , pp. 65-87
    • Szöllösi, J.1    Damjanovich, S.2    Mulhern, S.A.3    Trón, L.4
  • 4
    • 0028295796 scopus 로고
    • Resonance energy transfer: Methods and applications
    • P. Wu, L. Brand, Resonance energy transfer: methods and applications, Anal. Biochem., 218 (1994) 1-13.
    • (1994) Anal. Biochem. , vol.218 , pp. 1-13
    • Wu, P.1    Brand, L.2
  • 5
    • 0028913136 scopus 로고
    • Fluorescence resonance energy transfer
    • P.R. Selvin, Fluorescence resonance energy transfer. Methods Enzymol., 246 (1995) 301-334.
    • (1995) Methods Enzymol. , vol.246 , pp. 301-334
    • Selvin, P.R.1
  • 6
    • 0017917406 scopus 로고
    • The use of singlet-singlet energy transfer to study macromolecular assemblies
    • R.H. Fairclough, C.L. Cantor, The use of singlet-singlet energy transfer to study macromolecular assemblies, Methods Enzymol., 48 (1978) 347-379.
    • (1978) Methods Enzymol. , vol.48 , pp. 347-379
    • Fairclough, R.H.1    Cantor, C.L.2
  • 7
    • 0026550033 scopus 로고
    • Fluorescence resonance energy transfer measurements on cell surfaces: A spectroscopic tool for determining protein interactions
    • L. Mátyus, Fluorescence resonance energy transfer measurements on cell surfaces: A spectroscopic tool for determining protein interactions, J. Photochem. Photobiol. B: Biol., 12 (1992) 323-337.
    • (1992) J. Photochem. Photobiol. B: Biol. , vol.12 , pp. 323-337
    • Mátyus, L.1
  • 9
    • 0025894680 scopus 로고
    • Fluorescence resonance energy transfer measurements on single living cells: Application to binding of monovalent haptens to cell-bound immunoglobulin E
    • U. Kubitscheck, M. Kircheis, R. Schweitzer-Stenner, W. Dreybrodt, T.M. Jovin, I. Pecht, Fluorescence resonance energy transfer measurements on single living cells: application to binding of monovalent haptens to cell-bound immunoglobulin E, Biophys. J., 60 (1991) 307-318.
    • (1991) Biophys. J. , vol.60 , pp. 307-318
    • Kubitscheck, U.1    Kircheis, M.2    Schweitzer-Stenner, R.3    Dreybrodt, W.4    Jovin, T.M.5    Pecht, I.6
  • 10
    • 84989751806 scopus 로고
    • A photochemical technique to enhance sensitivity of detection of fluorescence resonance energy transfer
    • V.M. Mekler, A photochemical technique to enhance sensitivity of detection of fluorescence resonance energy transfer, Pholochem. Photobiol., 59 (1994) 615-620.
    • (1994) Pholochem. Photobiol. , vol.59 , pp. 615-620
    • Mekler, V.M.1
  • 11
    • 0014045715 scopus 로고
    • Some physical and chemical properties of concanavalin A, the phytohemagglutinin of the Jack Bean
    • M.O.J. Olson, I.E. Liener, Some physical and chemical properties of concanavalin A, the phytohemagglutinin of the Jack Bean, Biochemistry, 6 (1967) 105-111.
    • (1967) Biochemistry , vol.6 , pp. 105-111
    • Olson, M.O.J.1    Liener, I.E.2
  • 15
    • 0042690216 scopus 로고
    • Research Chemicals, Molecular Probes, Inc., Eugene, OR
    • R.P. Haugland, Handbook of Fluorescent Probes, Research Chemicals, Molecular Probes, Inc., Eugene, OR, 1994.
    • (1994) Handbook of Fluorescent Probes
    • Haugland, R.P.1
  • 16
    • 0028930998 scopus 로고
    • Covalent labeling of proteins and nucleic acids with fluorophores
    • A. Waggoner, Covalent labeling of proteins and nucleic acids with fluorophores, Methods Enzymol., 246 (1995) 362-373.
    • (1995) Methods Enzymol. , vol.246 , pp. 362-373
    • Waggoner, A.1
  • 17
    • 0026639433 scopus 로고
    • Fluorescence resonance energy transfer analysis of the structure of the four-way DNA junction
    • R.M. Clegg, A.I.H. Murchie, A. Zechel, C. Carlberg, S. Diekmann, D.M.J. Lilley, Fluorescence resonance energy transfer analysis of the structure of the four-way DNA junction, Biochemistry, 31 (1992) 4846-4856.
    • (1992) Biochemistry , vol.31 , pp. 4846-4856
    • Clegg, R.M.1    Murchie, A.I.H.2    Zechel, A.3    Carlberg, C.4    Diekmann, S.5    Lilley, D.M.J.6
  • 18
    • 0017236539 scopus 로고
    • Measurement of membrane protein lateral diffusion in single cells
    • M. Edidin, Y. Zagyanski, T. Lardner, Measurement of membrane protein lateral diffusion in single cells, Science, 191 (1976) 466-468.
    • (1976) Science , vol.191 , pp. 466-468
    • Edidin, M.1    Zagyanski, Y.2    Lardner, T.3
  • 19
    • 0017192686 scopus 로고
    • Mobility measurement by analysis of fluorescence photobleaching recovery kinetics
    • D. Axelrod, D.E. Koppel, J. Schlessinger, E.L. Elson, W.W. Webb, Mobility measurement by analysis of fluorescence photobleaching recovery kinetics, Biophys. J., 16 (1976) 1055-1069.
    • (1976) Biophys. J. , vol.16 , pp. 1055-1069
    • Axelrod, D.1    Koppel, D.E.2    Schlessinger, J.3    Elson, E.L.4    Webb, W.W.5
  • 20
    • 0016188814 scopus 로고
    • Studies on the mechanism by which cyanine dyes measure membrane potential in red blood cells and phosphatidylcholine vesicles
    • P.J. Sims, A.S. Waggoner, C.H. Wang, J.F. Hoffman, Studies on the mechanism by which cyanine dyes measure membrane potential in red blood cells and phosphatidylcholine vesicles, Biochemistry, 13 (1974) 3315-3330.
    • (1974) Biochemistry , vol.13 , pp. 3315-3330
    • Sims, P.J.1    Waggoner, A.S.2    Wang, C.H.3    Hoffman, J.F.4
  • 21
    • 0342573779 scopus 로고
    • A new sensitive photochemical technique for detection of fluorescence resonance energy transfer
    • J.C. Merlin, S. Turrell, J.P. Huvenne (eds.), Kluver Academic, Amsterdam
    • V.M. Mekler, A new sensitive photochemical technique for detection of fluorescence resonance energy transfer, in: J.C. Merlin, S. Turrell, J.P. Huvenne (eds.), Spectroscopy of Biological Molecules, Kluver Academic, Amsterdam, 1995, pp. 17-18.
    • (1995) Spectroscopy of Biological Molecules , pp. 17-18
    • Mekler, V.M.1
  • 23
    • 0041930769 scopus 로고
    • Organic photochemical imaging systems
    • G.A. Delzenne, Organic photochemical imaging systems, Adv. Photochem., 11 (1979) 1-103.
    • (1979) Adv. Photochem. , vol.11 , pp. 1-103
    • Delzenne, G.A.1
  • 25
    • 0242617623 scopus 로고
    • The properties of streptavidin, a biotin binding protein produced streptomycetes
    • L. Chaiet, R.F. Wolf, The properties of streptavidin, a biotin binding protein produced Streptomycetes, Arch. Biochem. Biophys., 106 (1964) 1-5.
    • (1964) Arch. Biochem. Biophys. , vol.106 , pp. 1-5
    • Chaiet, L.1    Wolf, R.F.2
  • 26
    • 0041446796 scopus 로고
    • Structure and functions of immunoglobulins
    • L.E. Glynn, M.W. Steward (eds.), Wiley, New York
    • M.W. Turner, Structure and functions of immunoglobulins, in L.E. Glynn, M.W. Steward (eds.), Structure and Functions of Antibodies, Wiley, New York, 1981, pp. 8-65.
    • (1981) Structure and Functions of Antibodies , pp. 8-65
    • Turner, M.W.1
  • 28
    • 0014425864 scopus 로고
    • Molecular weight of concanavalin A
    • A.J. Kalb, A. Lustig, Molecular weight of concanavalin A. Biochem. Biophys. Acta, 168 (1968) 366-367.
    • (1968) Biochem. Biophys. Acta , vol.168 , pp. 366-367
    • Kalb, A.J.1    Lustig, A.2
  • 29
    • 0016502735 scopus 로고
    • Distribution of end-to-end distances of oligopeptides in solution as estimated by energy transfer
    • E. Haas, M. Wilchek, E. Katchalski-Katzir, I.Z. Steinberg, Distribution of end-to-end distances of oligopeptides in solution as estimated by energy transfer. Proc. Natl. Acad. USA. 72 (1975) 1807-1811.
    • (1975) Proc. Natl. Acad. USA , vol.72 , pp. 1807-1811
    • Haas, E.1    Wilchek, M.2    Katchalski-Katzir, E.3    Steinberg, I.Z.4
  • 30
    • 0023943009 scopus 로고
    • Distance distribution in native and random-coil troponin I from frequency-domain measurements of fluorescence energy transfer
    • J.R. Lakowicz, I. Gryczynski, W. Wiczk, G. Laczko, F.C. Prendergast, M.L. Jounson, Distance distribution in native and random-coil troponin I from frequency-domain measurements of fluorescence energy transfer, Biopolymers, 27 (1990) 821-830.
    • (1990) Biopolymers , vol.27 , pp. 821-830
    • Lakowicz, J.R.1    Gryczynski, I.2    Wiczk, W.3    Laczko, G.4    Prendergast, F.C.5    Jounson, M.L.6
  • 31
    • 0026052393 scopus 로고
    • Differential flexibilities in three branches of an N-linked triantennary glycopeptide
    • P.G. Wu, K.G. Rice, L. Brand, Y.C. Lee, Differential flexibilities in three branches of an N-linked triantennary glycopeptide, Proc. Natl. Acad. USA, 88 (1991) 9355-9359.
    • (1991) Proc. Natl. Acad. USA , vol.88 , pp. 9355-9359
    • Wu, P.G.1    Rice, K.G.2    Brand, L.3    Lee, Y.C.4
  • 32
    • 0028861599 scopus 로고
    • Metal-ligand complexes as a new class of long-lived fluorophores for protein hydrodynamics
    • E. Terpetschnig, H. Szmacinski, H. Malak, J.R. Lakowicz, Metal-ligand complexes as a new class of long-lived fluorophores for protein hydrodynamics. Biophys. J., 68 (1995) 342-350.
    • (1995) Biophys. J. , vol.68 , pp. 342-350
    • Terpetschnig, E.1    Szmacinski, H.2    Malak, H.3    Lakowicz, J.R.4
  • 33
    • 0019442257 scopus 로고
    • Detection of actin assembly by fluorescence energy transfer
    • D.L. Taylor, J. Readler, J.A. Spudich, L. Stryer, Detection of actin assembly by fluorescence energy transfer, J. Cell. Biol., 89 (1981) 362-367.
    • (1981) J. Cell. Biol. , vol.89 , pp. 362-367
    • Taylor, D.L.1    Readler, J.2    Spudich, J.A.3    Stryer, L.4
  • 34
    • 0028934105 scopus 로고
    • Kinetic studies by fluorescence resonance energy transfer employing a double-labeled oligonucleotide: Hybridization to the oligonucleotide complement and to single-stranded DNA
    • K.M. Parkhurst, L.J. Parkhurst, Kinetic studies by fluorescence resonance energy transfer employing a double-labeled oligonucleotide: hybridization to the oligonucleotide complement and to single-stranded DNA, Biochemistry, 34 (1995) 285-292.
    • (1995) Biochemistry , vol.34 , pp. 285-292
    • Parkhurst, K.M.1    Parkhurst, L.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.