메뉴 건너뛰기




Volumn 75, Issue 2, 1998, Pages 1084-1096

Unfolding of acrylodan-labeled human serum albumin probed by steady- state and time-resolved fluorescence methods

Author keywords

[No Author keywords available]

Indexed keywords

SERUM ALBUMIN;

EID: 0031852954     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77598-8     Document Type: Article
Times cited : (179)

References (37)
  • 1
    • 0002761145 scopus 로고
    • Serum albumin: Amino acid sequence
    • V. M. Rosenoer, M. Oratz, and M. A. Rothschild, editors. Pergamon, Oxford
    • Brown, J. R. 1977. Serum albumin: amino acid sequence. In Albumin Structure, Function and Uses. V. M. Rosenoer, M. Oratz, and M. A. Rothschild, editors. Pergamon, Oxford. 27-51.
    • (1977) Albumin Structure, Function and Uses , pp. 27-51
    • Brown, J.R.1
  • 2
    • 0017111139 scopus 로고
    • Displacement of tolbutamide, glibenclamide and chlorpropamide from serum albumin by anionic drugs
    • Brown, K. F., and M. J. Crooks. 1976. Displacement of tolbutamide, glibenclamide and chlorpropamide from serum albumin by anionic drugs. Biochem. Pharmacol. 25:1175-1178.
    • (1976) Biochem. Pharmacol. , vol.25 , pp. 1175-1178
    • Brown, K.F.1    Crooks, M.J.2
  • 4
    • 0028227096 scopus 로고
    • Structure of serum albumin
    • Carter, D. C., and J. X. Ho. 1994. Structure of serum albumin. Adv. Protein Chem. 45:153-203.
    • (1994) Adv. Protein Chem. , vol.45 , pp. 153-203
    • Carter, D.C.1    Ho, J.X.2
  • 5
    • 0019982681 scopus 로고
    • Polarographic investigation of conformational changes of human serum albumin. Part I. Unfolding of human serum albumin by urea
    • Chmelik, J., and V. Kalous. 1982. Polarographic investigation of conformational changes of human serum albumin. Part I. Unfolding of human serum albumin by urea. Bioelectrochem. Bioenerg. 9:7-13.
    • (1982) Bioelectrochem. Bioenerg. , vol.9 , pp. 7-13
    • Chmelik, J.1    Kalous, V.2
  • 6
    • 0023858858 scopus 로고
    • Fluorescence of equine platelet tropomyosin labeled with acrylodan
    • Clark, I. D., and L. D. Burtnick. 1988. Fluorescence of equine platelet tropomyosin labeled with acrylodan. Arch. Biochem. Biophys. 260: 595-600.
    • (1988) Arch. Biochem. Biophys. , vol.260 , pp. 595-600
    • Clark, I.D.1    Burtnick, L.D.2
  • 7
    • 0028388327 scopus 로고
    • Spectroscopic characterization of albumin and myoglobin entrapped in bulk sol-gel glasses
    • Edmiston, P. L., C. L. Wambolt, M. K. Smith, and S. S. Saavedra. 1994. Spectroscopic characterization of albumin and myoglobin entrapped in bulk sol-gel glasses. J. Colloid Interface Sci. 163:395-406.
    • (1994) J. Colloid Interface Sci. , vol.163 , pp. 395-406
    • Edmiston, P.L.1    Wambolt, C.L.2    Smith, M.K.3    Saavedra, S.S.4
  • 8
    • 0027958069 scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • Eftink, M. R. 1994. The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys. J. 66:482-501.
    • (1994) Biophys. J. , vol.66 , pp. 482-501
    • Eftink, M.R.1
  • 9
    • 0017288499 scopus 로고
    • Exposure of tryptophyl residues in proteins. Quantitative determination by fluorescence quenching studies
    • Eftink, M. R., and C. A. Ghiron. 1976. Exposure of tryptophyl residues in proteins. Quantitative determination by fluorescence quenching studies. Biochemistry. 15:672-679.
    • (1976) Biochemistry , vol.15 , pp. 672-679
    • Eftink, M.R.1    Ghiron, C.A.2
  • 10
    • 0030932504 scopus 로고    scopus 로고
    • Destabilization of human serum albumin by polyethylene glycols studied by thermodynamical equilibrium and kinetic approaches
    • Farruggia, B., G. Gabriela, C. D'Angelo, and G. Pico. 1997. Destabilization of human serum albumin by polyethylene glycols studied by thermodynamical equilibrium and kinetic approaches. Int. J. Macromol. 20:43-51.
    • (1997) Int. J. Macromol. , vol.20 , pp. 43-51
    • Farruggia, B.1    Gabriela, G.2    D'Angelo, C.3    Pico, G.4
  • 11
    • 0021099449 scopus 로고
    • Resonance energy transfer between cysteine-34, tryptophan-214, and tyrosine-411 of human serum albumin
    • Hagag, N., E. R. Birnbaum, and D. W. Darnall. 1983. Resonance energy transfer between cysteine-34, tryptophan-214, and tyrosine-411 of human serum albumin. Biochemistry. 22:2420-2427.
    • (1983) Biochemistry , vol.22 , pp. 2420-2427
    • Hagag, N.1    Birnbaum, E.R.2    Darnall, D.W.3
  • 12
    • 0030926943 scopus 로고    scopus 로고
    • Time-resolved fluorescence studies on site-directed mutants of human serum albumin
    • Helms, M. K., C. E. Petersen, N. V. Bhagavan, and D. M. Jameson. 1997. Time-resolved fluorescence studies on site-directed mutants of human serum albumin. FEBS Lett. 408:67-70.
    • (1997) FEBS Lett. , vol.408 , pp. 67-70
    • Helms, M.K.1    Petersen, C.E.2    Bhagavan, N.V.3    Jameson, D.M.4
  • 13
    • 0016813415 scopus 로고
    • Interaction between salicylic acid and indometacin in binding to human serum albumin
    • Hultmark, D., K. Borg, R. Elofsson, and L. Palmer. 1975. Interaction between salicylic acid and indometacin in binding to human serum albumin. Acta Pharm. Suec. 12:259-276.
    • (1975) Acta Pharm. Suec. , vol.12 , pp. 259-276
    • Hultmark, D.1    Borg, K.2    Elofsson, R.3    Palmer, L.4
  • 14
    • 0000470477 scopus 로고
    • Singlet adiabatic states of solvated prodan: A semi-empirical molecular orbital study
    • Ilich, P., and F. G. Prendergast. 1989. Singlet adiabatic states of solvated prodan: a semi-empirical molecular orbital study. J. Phys. Chem. 93: 4441-4447.
    • (1989) J. Phys. Chem. , vol.93 , pp. 4441-4447
    • Ilich, P.1    Prendergast, F.G.2
  • 15
    • 0030587038 scopus 로고    scopus 로고
    • Accessibility of the fluorescent reporter group in native, silica-adsorbed, and covalently attached acrylodan-labeled serum albumins
    • Ingersoll, C. M., J. D. Jordon, and F. V. Bright. 1996. Accessibility of the fluorescent reporter group in native, silica-adsorbed, and covalently attached acrylodan-labeled serum albumins. Anal. Chem. 68: 3194-3198.
    • (1996) Anal. Chem. , vol.68 , pp. 3194-3198
    • Ingersoll, C.M.1    Jordon, J.D.2    Bright, F.V.3
  • 16
    • 0029645142 scopus 로고
    • Dynamics of acrylodan-labeled bovine and human serum albumin entrapped in a sol-gel-derived biogel
    • Jordon, J. D., R. A. Dunbar, and F. V. Bright. 1995. Dynamics of acrylodan-labeled bovine and human serum albumin entrapped in a sol-gel-derived biogel. Anal. Chem. 67:2436-2443.
    • (1995) Anal. Chem. , vol.67 , pp. 2436-2443
    • Jordon, J.D.1    Dunbar, R.A.2    Bright, F.V.3
  • 17
    • 0015371639 scopus 로고
    • Comparison of equilibrium dialysis and frontal analysis chromatography in the study of salicylate binding
    • Kerestes-Nagy, S., R. F. Mais, Y. T. Dester, and J. F. Zaroslinski. 1972. Comparison of equilibrium dialysis and frontal analysis chromatography in the study of salicylate binding. Anal. Biochem. 48:80-89.
    • (1972) Anal. Biochem. , vol.48 , pp. 80-89
    • Kerestes-Nagy, S.1    Mais, R.F.2    Dester, Y.T.3    Zaroslinski, J.F.4
  • 18
    • 0015907980 scopus 로고
    • Quenching of fluorescence by oxygen. A probe for structural fluctuations in macromolecules
    • Lakowicz, J. R., and G. Weber. 1973. Quenching of fluorescence by oxygen. A probe for structural fluctuations in macromolecules. Biochemistry. 12:4161-4170.
    • (1973) Biochemistry , vol.12 , pp. 4161-4170
    • Lakowicz, J.R.1    Weber, G.2
  • 19
    • 0026773387 scopus 로고
    • Partially folded state of the disulfide-reduced form of human serum albumin as an intermediate for reversible denaturation
    • Lee, J. Y., and M. Hirose. 1992. Partially folded state of the disulfide-reduced form of human serum albumin as an intermediate for reversible denaturation. J. Biol. Chem. 267:14753-14758.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14753-14758
    • Lee, J.Y.1    Hirose, M.2
  • 20
    • 0028793738 scopus 로고
    • Dynamics of acrylodan-labeled bovine and human serum albumin sequestered with aerosol-OT reverse micelles
    • Lundgren, J. S., M. P. Heitz, and F. V. Bright. 1995. Dynamics of acrylodan-labeled bovine and human serum albumin sequestered with aerosol-OT reverse micelles. Anal. Chem. 67:3775-3781.
    • (1995) Anal. Chem. , vol.67 , pp. 3775-3781
    • Lundgren, J.S.1    Heitz, M.P.2    Bright, F.V.3
  • 21
    • 0031006443 scopus 로고    scopus 로고
    • Probing the cysteine 34 residue in human serum albumin using fluorescence techniques
    • Narazaki, R., T. Maruyama, and M. Otagiri. 1997. Probing the cysteine 34 residue in human serum albumin using fluorescence techniques. Biochim. Biophys. Acta. 1338:275-281.
    • (1997) Biochim. Biophys. Acta. , vol.1338 , pp. 275-281
    • Narazaki, R.1    Maruyama, T.2    Otagiri, M.3
  • 23
    • 0029556501 scopus 로고
    • Thermodynamic aspects of the thermal stability of human serum albumin
    • Pico, G. A. 1995. Thermodynamic aspects of the thermal stability of human serum albumin. Biochem. Mol. Biol. Int. 36:1017-1023.
    • (1995) Biochem. Mol. Biol. Int. , vol.36 , pp. 1017-1023
    • Pico, G.A.1
  • 24
    • 0029849761 scopus 로고    scopus 로고
    • Thermal stability of human serum albumin by sodium halide salts
    • Pico, G. A. 1996. Thermal stability of human serum albumin by sodium halide salts. Biochem. Mol. Biol. Int. 38:1-6.
    • (1996) Biochem. Mol. Biol. Int. , vol.38 , pp. 1-6
    • Pico, G.A.1
  • 25
    • 0030976566 scopus 로고    scopus 로고
    • Thermodynamic features of the thermal unfolding of human serum albumin
    • Pico, G. A. 1997. Thermodynamic features of the thermal unfolding of human serum albumin. Int. J. Biol. Macromol. 20:63-73.
    • (1997) Int. J. Biol. Macromol. , vol.20 , pp. 63-73
    • Pico, G.A.1
  • 26
    • 0021112116 scopus 로고
    • Synthesis, spectral properties, and use of 6-acryloyl-2-dimethylamino-naphthalene (acrylodan)
    • Prendergast, F. G., M. Meyer, G. L. Carlson, S. Iida, and J. D. Potter. 1983. Synthesis, spectral properties, and use of 6-acryloyl-2-dimethylamino-naphthalene (acrylodan). J. Biol. Chem. 258:7541-7544.
    • (1983) J. Biol. Chem. , vol.258 , pp. 7541-7544
    • Prendergast, F.G.1    Meyer, M.2    Carlson, G.L.3    Iida, S.4    Potter, J.D.5
  • 27
    • 0001417340 scopus 로고
    • Characterization of chloride ion binding to human serum albumin using CI-NMR null point spectral analysis
    • Price, W. S., N.-H. Ge, L.-Z. Hong, and L.-P. Hwang. 1993. Characterization of chloride ion binding to human serum albumin using CI-NMR null point spectral analysis. J. Am. Chem. Soc. 115:1095-1105.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 1095-1105
    • Price, W.S.1    Ge, N.-H.2    Hong, L.-Z.3    Hwang, L.-P.4
  • 28
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenyl-methanesulfonyl α-chymotrypsin using different denaturants
    • Santoro, M. M., and D. W. Bolen. 1988. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenyl-methanesulfonyl α-chymotrypsin using different denaturants. Biochemistry. 27:8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 29
    • 0017174391 scopus 로고
    • Further characterization of specific drug binding sites on human serum albumin
    • Sudlow, G., D. J. Birkett, and D. N. Wade. 1976. Further characterization of specific drug binding sites on human serum albumin. Mol. Pharmacol. 12:1052-1061.
    • (1976) Mol. Pharmacol. , vol.12 , pp. 1052-1061
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 30
    • 0021099448 scopus 로고
    • Resonance energy transfer between cysteine-34 and tryptophan-214 in human serum albumin. Distance measurements as a function of pH
    • Suzukida, M., H. P. Le, F. Shahid, R. A. McPherson, E. R. Birnbaum, and D. W. Darnall. 1983. Resonance energy transfer between cysteine-34 and tryptophan-214 in human serum albumin. Distance measurements as a function of pH. Biochemistry. 22:2415-2420.
    • (1983) Biochemistry , vol.22 , pp. 2415-2420
    • Suzukida, M.1    Le, H.P.2    Shahid, F.3    McPherson, R.A.4    Birnbaum, E.R.5    Darnall, D.W.6
  • 31
    • 58149363707 scopus 로고
    • Experimental determination of the free energy of unfolding of proteins
    • Tayyab, S., M. U. Siddiqui, and N. Ahmad. 1995. Experimental determination of the free energy of unfolding of proteins. Biochem. Ed. 23: 162-164.
    • (1995) Biochem. Ed. , vol.23 , pp. 162-164
    • Tayyab, S.1    Siddiqui, M.U.2    Ahmad, N.3
  • 32
    • 0015935434 scopus 로고
    • Reversible denaturation of human serum albumin by pH, temperature, and guanidine hydrochloride followed by optical rotation
    • Wallevick, K. 1973. Reversible denaturation of human serum albumin by pH, temperature, and guanidine hydrochloride followed by optical rotation. J. Biol. Chem. 248:2650-2655.
    • (1973) J. Biol. Chem. , vol.248 , pp. 2650-2655
    • Wallevick, K.1
  • 33
    • 0000437706 scopus 로고
    • Rotational reorientation kinetics of dansylated bovine serum albumin
    • Wang, R., and F. V. Bright. 1993. Rotational reorientation kinetics of dansylated bovine serum albumin. J. Phys. Chem. 97:4231-4238.
    • (1993) J. Phys. Chem. , vol.97 , pp. 4231-4238
    • Wang, R.1    Bright, F.V.2
  • 34
    • 0029059110 scopus 로고    scopus 로고
    • Dynamics surrounding Cys-34 in native, chemically denatured, and silica-adsorbed bovine serum albumin
    • Wang, R., S. Sun, E. J. Bekos, and F. V. Bright. 1996. Dynamics surrounding Cys-34 in native, chemically denatured, and silica-adsorbed bovine serum albumin. Anal. Chem. 67:149-159.
    • (1996) Anal. Chem. , vol.67 , pp. 149-159
    • Wang, R.1    Sun, S.2    Bekos, E.J.3    Bright, F.V.4
  • 37
    • 1542786312 scopus 로고    scopus 로고
    • Measurement of fluorescence from tryptophan to probe the environment and reaction kinetics within protein-doped sol-gel-derived glass monoliths
    • Zheng, L., W. R. Reid, and J. D. Brennan. 1997. Measurement of fluorescence from tryptophan to probe the environment and reaction kinetics within protein-doped sol-gel-derived glass monoliths. Anal. Chem. 69: 3940-3949.
    • (1997) Anal. Chem. , vol.69 , pp. 3940-3949
    • Zheng, L.1    Reid, W.R.2    Brennan, J.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.