메뉴 건너뛰기




Volumn 39, Issue 4, 2006, Pages 399-408

Quenching of the intrinsic fluorescence of human serum albumin by trimethoxyphenylfluorone-Mo(VI) complex

Author keywords

Binding constant; Energy transfer; Fluorescence quenching; Human serum albumin; Trimethoxyphenylfluorone Mo(VI) complex

Indexed keywords


EID: 33747619382     PISSN: 00387010     EISSN: 15322289     Source Type: Journal    
DOI: 10.1080/00387010600806212     Document Type: Article
Times cited : (9)

References (20)
  • 1
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • He, X. M.; Carter, D. C. Atomic structure and chemistry of human serum albumin. Nature 1992, 358, 209-215.
    • (1992) Nature , vol.358 , pp. 209-215
    • He, X.M.1    Carter, D.C.2
  • 2
    • 0037009311 scopus 로고    scopus 로고
    • Interaction of drugs with bovine and human serum albumin
    • Sulkowska, A. Interaction of drugs with bovine and human serum albumin. J. Mol. Struct. 2002, 614, 227-232.
    • (2002) J. Mol. Struct. , vol.614 , pp. 227-232
    • Sulkowska, A.1
  • 3
    • 1042302180 scopus 로고    scopus 로고
    • Complexation of polymethine dyes with human serum albumin: A spectroscopic study
    • Tatikolov, A. S.; Costa, S. M. B. Complexation of polymethine dyes with human serum albumin: a spectroscopic study. Biophys. Chem. 2004, 107, 33-49.
    • (2004) Biophys. Chem. , vol.107 , pp. 33-49
    • Tatikolov, A.S.1    Costa, S.M.B.2
  • 4
    • 0346998044 scopus 로고    scopus 로고
    • Investigation of interaction of cationic surfactant with HSA in the presence of alcohols using PFG-NMR and potentiometric technique
    • Gharibi, H.; Javadian, S.; Hashemianzadeh, M. Investigation of interaction of cationic surfactant with HSA in the presence of alcohols using PFG-NMR and potentiometric technique. Colloids Surf. A 2004, 232, 77-86.
    • (2004) Colloids Surf. A , vol.232 , pp. 77-86
    • Gharibi, H.1    Javadian, S.2    Hashemianzadeh, M.3
  • 5
    • 0032765955 scopus 로고    scopus 로고
    • The interaction between human and bovine serum albumin and zinc studied by a competitive spectrophotometry
    • Ohyoshi, E.; Hamada, Y.; Nakata, K.; Kohata, S. The interaction between human and bovine serum albumin and zinc studied by a competitive spectrophotometry. J. Inorg. Biochem. 1999, 75, 213-218.
    • (1999) J. Inorg. Biochem. , vol.75 , pp. 213-218
    • Ohyoshi, E.1    Hamada, Y.2    Nakata, K.3    Kohata, S.4
  • 6
    • 0034287494 scopus 로고    scopus 로고
    • Spectroscopic studies on the interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants
    • Gelamo, E. L.; Tabak, M. Spectroscopic studies on the interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants. Spectrochim. Acta A 2000, 56, 2255-2271.
    • (2000) Spectrochim. Acta A , vol.56 , pp. 2255-2271
    • Gelamo, E.L.1    Tabak, M.2
  • 7
    • 0033002439 scopus 로고    scopus 로고
    • Chromatographic study of magnesium and calcium binding to immobilized human serum albumin
    • Guillaume, Y. C.; Peyrin, E.; Berthelot, A. Chromatographic study of magnesium and calcium binding to immobilized human serum albumin. J. Chromatogr. B 1999, 728, 167-174.
    • (1999) J. Chromatogr. B , vol.728 , pp. 167-174
    • Guillaume, Y.C.1    Peyrin, E.2    Berthelot, A.3
  • 8
    • 0037117898 scopus 로고    scopus 로고
    • The interaction of human serum albumin with dioctanoylphosphatidyl- choline in aqueous aolutions
    • Martinez-Landeira, P.; Ruso, J. M.; Prieto, G.; Sarmiento, F.; Jones, M. N. The interaction of human serum albumin with dioctanoylphosphatidyl-choline in aqueous aolutions. Langmuir 2002, 18, 3300-3305.
    • (2002) Langmuir , vol.18 , pp. 3300-3305
    • Martinez-Landeira, P.1    Ruso, J.M.2    Prieto, G.3    Sarmiento, F.4    Jones, M.N.5
  • 9
    • 0037739659 scopus 로고    scopus 로고
    • Study of the interaction between daunorubicin and human serum albumin and the determination of daunorubicin in blood serum samples
    • Jiang, C. Q.; Gao, M. X.; Meng, X. Z. Study of the interaction between daunorubicin and human serum albumin and the determination of daunorubicin in blood serum samples. Spectrochim. Acta A 2003, 59, 1605-1610.
    • (2003) Spectrochim. Acta A , vol.59 , pp. 1605-1610
    • Jiang, C.Q.1    Gao, M.X.2    Meng, X.Z.3
  • 10
    • 0037293217 scopus 로고    scopus 로고
    • Binding of bismuth to serum proteins: Implication for targets of Bi(III) in blood plasma
    • Sun, H. Z.; Szeto, K. Y. Binding of bismuth to serum proteins: implication for targets of Bi(III) in blood plasma. J. Inorg. Biochem. 2003, 94, 114-120.
    • (2003) J. Inorg. Biochem. , vol.94 , pp. 114-120
    • Sun, H.Z.1    Szeto, K.Y.2
  • 11
    • 28144453351 scopus 로고    scopus 로고
    • Rapid and highly sensitive method for protein determination in biological samples with m-nitrophenylfluorone-Mo(VI) complex as a spectral probe
    • Du, B.; Wu, D.; Wei, Q.; Duan, C. H.; Li, Y. Rapid and highly sensitive method for protein determination in biological samples with m- nitrophenylfluorone-Mo(VI) complex as a spectral probe. Instrum Sci. Technol. 2005, 33, 1-11.
    • (2005) Instrum Sci. Technol. , vol.33 , pp. 1-11
    • Du, B.1    Wu, D.2    Wei, Q.3    Duan, C.H.4    Li, Y.5
  • 12
    • 26444570827 scopus 로고    scopus 로고
    • Fast determination of ultra trace amounts of residual proteins in penicillin based on the enhancement in Rayleigh light scattering spectra of phenylfluorone-Mo(VI) complex
    • Du, B.; Wu, D.; Zhang, H.; Li, Y.; Wei, Q.; Li, Z. J. Fast determination of ultra trace amounts of residual proteins in penicillin based on the enhancement in Rayleigh light scattering spectra of phenylfluorone-Mo(VI) complex. Chem. Anal. (Warsaw) 2005, 50, 795-806.
    • (2005) Chem. Anal. (Warsaw) , vol.50 , pp. 795-806
    • Du, B.1    Wu, D.2    Zhang, H.3    Li, Y.4    Wei, Q.5    Li, Z.J.6
  • 13
    • 29244442326 scopus 로고    scopus 로고
    • A spectrophotometric method for determination of total proteins in cow milk powder samples using the o-nitrophenylfluorone/Mo(VI) complex
    • Wei, Q.; Wu, D.; Du, B.; Li, Z.; Huo, Y. Q. A spectrophotometric method for determination of total proteins in cow milk powder samples using the o-nitrophenylfluorone/Mo(VI) complex. J. Food Compos. Anal. 2006, 19, 76-82.
    • (2006) J. Food Compos. Anal. , vol.19 , pp. 76-82
    • Wei, Q.1    Wu, D.2    Du, B.3    Li, Z.4    Huo, Y.Q.5
  • 14
    • 19544384433 scopus 로고    scopus 로고
    • Rapid determination of ultra trace amounts of residual protein in penicillin based on its enhancement effects of Rayleigh light scattering on trimethoxyphenlyfluorone (TM-PF)-Mo(VI) complex
    • Wei, Q.; Li, Y.; Zhang, H.; Ding, Y. L.; Du, B. Rapid determination of ultra trace amounts of residual protein in penicillin based on its enhancement effects of Rayleigh light scattering on trimethoxyphenlyfluorone (TM-PF)-Mo(VI) complex. J. Pharm. Biomed. Anal. 2005, 38, 232-238.
    • (2005) J. Pharm. Biomed. Anal. , vol.38 , pp. 232-238
    • Wei, Q.1    Li, Y.2    Zhang, H.3    Ding, Y.L.4    Du, B.5
  • 15
    • 0015794613 scopus 로고
    • Fluorescence and the location of tryptophan residues in protein molecules
    • Burstein, E. A.; Vedenkina, N. S.; Ivkova, M. N. Fluorescence and the location of tryptophan residues in protein molecules. Photochem. Photobiol. 1973, 18, 263-279.
    • (1973) Photochem. Photobiol. , vol.18 , pp. 263-279
    • Burstein, E.A.1    Vedenkina, N.S.2    Ivkova, M.N.3
  • 16
    • 0642316329 scopus 로고    scopus 로고
    • Interaction of magnolol with bovine serum albumin: A fluorescence- quenching study
    • Liu, J. Q.; Tian, J. N.; Zhang, J. Y.; Hu, Z. D.; Chen, X. G. Interaction of magnolol with bovine serum albumin: a fluorescence-quenching study. Anal. Bioanal. Chem. 2003, 376, 864-867.
    • (2003) Anal. Bioanal. Chem. , vol.376 , pp. 864-867
    • Liu, J.Q.1    Tian, J.N.2    Zhang, J.Y.3    Hu, Z.D.4    Chen, X.G.5
  • 17
    • 0037060027 scopus 로고    scopus 로고
    • Study of the interaction between terazosin and serum Albumin: Synchronous fluorescence determination of terazosin
    • Jiang, C. Q.; Gao, M. X.; He, J. X. Study of the interaction between terazosin and serum Albumin: synchronous fluorescence determination of terazosin. Anal. Chim. Acta 2002, 452, 185-189.
    • (2002) Anal. Chim. Acta , vol.452 , pp. 185-189
    • Jiang, C.Q.1    Gao, M.X.2    He, J.X.3
  • 18
    • 0028924992 scopus 로고
    • Fluorescence resonance energy transfer
    • Clegg, R. M. Fluorescence resonance energy transfer. Curr. Opin. Biotech. 1995, 6, 103-110.
    • (1995) Curr. Opin. Biotech. , vol.6 , pp. 103-110
    • Clegg, R.M.1
  • 19
    • 0028884014 scopus 로고
    • Fluorescence resonance energy transfer spectroscopy is a reliable "ruler" for measuring structural changes in proteins: Dispelling the problem of the unknown orientation factor
    • Cristobal, G.; Dos, R.; Pierre, D. J. M. Fluorescence resonance energy transfer spectroscopy is a reliable "ruler" for measuring structural changes in proteins: dispelling the problem of the unknown orientation factor. J. Struct. Biol. 1995, 115, 175-185.
    • (1995) J. Struct. Biol. , vol.115 , pp. 175-185
    • Cristobal, G.1    Dos, R.2    Pierre, D.J.M.3
  • 20
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: Forces contributing to stability
    • Ross, P. D.; Subramanian, S. Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 1981, 20, 3096-3102.
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.