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Volumn 22, Issue 1, 2008, Pages 43-50

Spectroscopic investigation of the interaction of bovine serum albumin with a novel cardiac agent V-09

Author keywords

Bovine serum albumin; Cardiac agent; Fluorescence spectroscopy; Interaction

Indexed keywords

ENERGY TRANSFER; ENTHALPY; FLUORESCENCE SPECTROSCOPY; HYDROPHOBICITY;

EID: 42149095033     PISSN: 07124813     EISSN: None     Source Type: Journal    
DOI: 10.1155/2008/450257     Document Type: Article
Times cited : (10)

References (20)
  • 1
    • 2342509585 scopus 로고    scopus 로고
    • In vitro study on the binding of anti-coagulant vitamin to bovine serum albumin and the influence of toxic ions and common ions on binding
    • J.Q. Liu, J.N. Tian, W.Y. He et al., In vitro study on the binding of anti-coagulant vitamin to bovine serum albumin and the influence of toxic ions and common ions on binding, J. Pharm. Biomed. Anal. 35 (2004), 671-677.
    • (2004) J. Pharm. Biomed. Anal , vol.35 , pp. 671-677
    • Liu, J.Q.1    Tian, J.N.2    He, W.Y.3
  • 2
    • 0028227096 scopus 로고
    • Structure of serum albumin
    • D.C. Carter and J.X. Ho, Structure of serum albumin, Adv. Protein Chem. 45 (1994), 153-203.
    • (1994) Adv. Protein Chem , vol.45 , pp. 153-203
    • Carter, D.C.1    Ho, J.X.2
  • 4
    • 1842534284 scopus 로고    scopus 로고
    • The interaction of human serum albumin with a novel antidiabetic agent - SU-118
    • W.Y. Zhong, Y.C. Wang, J.S. Yu et al., The interaction of human serum albumin with a novel antidiabetic agent - SU-118, J. Pharm. Sci. 93 (2004), 1039-1046.
    • (2004) J. Pharm. Sci , vol.93 , pp. 1039-1046
    • Zhong, W.Y.1    Wang, Y.C.2    Yu, J.S.3
  • 5
    • 29744456582 scopus 로고    scopus 로고
    • Synthesis and biologic activities on 1-{1-[2-(3,4-dimethoxy)phenylethyl]-5-cyano-6-methyl-uracil-3yl}- 3-substituted amino-2-propanol compounds
    • J.Q. Zhang, L.C. Wang, Z.Z. Jiang and M. Lin, Synthesis and biologic activities on 1-{1-[2-(3,4-dimethoxy)phenylethyl]-5-cyano-6-methyl-uracil-3yl}- 3-substituted amino-2-propanol compounds, J. Chin. Pharm. Univ. 34 (2003), 396-399.
    • (2003) J. Chin. Pharm. Univ , vol.34 , pp. 396-399
    • Zhang, J.Q.1    Wang, L.C.2    Jiang, Z.Z.3    Lin, M.4
  • 7
    • 0015907980 scopus 로고
    • Quenching of fluorescence by oxygen: A probe for structural fluctuations in macromolecules
    • J.R. Lakowica and G. Weber, Quenching of fluorescence by oxygen: A probe for structural fluctuations in macromolecules, Biochemistry 12 (1973), 4161-4170.
    • (1973) Biochemistry , vol.12 , pp. 4161-4170
    • Lakowica, J.R.1    Weber, G.2
  • 8
    • 0019889063 scopus 로고
    • forces contribution to stability
    • Thermodynamics of protein association reaction
    • P.D. Ross and S. Subramanian, Thermodynamics of protein association reaction: forces contribution to stability, Biochemistry 20 (1981), 3096-3102.
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 9
    • 0003468776 scopus 로고    scopus 로고
    • O. Sinanoglu, ed, Academic Press, New York
    • T. Forster, Modern Quantum Chemistry, Vol. 3, O. Sinanoglu, ed., Academic Press, New York, 1996.
    • (1996) Modern Quantum Chemistry , vol.3
    • Forster, T.1
  • 10
    • 27744599888 scopus 로고
    • Transfer mechanisms of electronic excitation
    • T. Forster, Transfer mechanisms of electronic excitation, Discuss Faraday Soc. 27 (1959), 7-10.
    • (1959) Discuss Faraday Soc , vol.27 , pp. 7-10
    • Forster, T.1
  • 11
    • 0015340490 scopus 로고
    • Proximity relationships in rhodopsin
    • C.W. Wu and L. Stryer, Proximity relationships in rhodopsin, Proc. Natl. Acad. Sci. USA 69 (1972), 1104-1108.
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 1104-1108
    • Wu, C.W.1    Stryer, L.2
  • 13
    • 0017130253 scopus 로고
    • Statistical interpretation of fluorescence energy transfer measurements in macromolecular systems
    • Z. Hillel and C.W. Wu, Statistical interpretation of fluorescence energy transfer measurements in macromolecular systems, Biochemistry 15 (1976), 2105-2113.
    • (1976) Biochemistry , vol.15 , pp. 2105-2113
    • Hillel, Z.1    Wu, C.W.2
  • 14
    • 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
  • 15
    • 0023235043 scopus 로고
    • Fluorescence energy transfer study of the relationship between the lone tryptophan residue and drug binding sites in human serum albumin
    • S. Kasai, T. Horie, T. Mizuma and S. Awazu, Fluorescence energy transfer study of the relationship between the lone tryptophan residue and drug binding sites in human serum albumin, J. Pharm. Sci. 76 (1987), 387-392.
    • (1987) J. Pharm. Sci , vol.76 , pp. 387-392
    • Kasai, S.1    Horie, T.2    Mizuma, T.3    Awazu, S.4
  • 16
    • 0018413926 scopus 로고
    • Spectroscopic studies of binding and proximity relationships for fatty acids and bilirubin
    • E.B. Charies and B.S. Hudson, Spectroscopic studies of binding and proximity relationships for fatty acids and bilirubin, J. Biol. Chem. 254 (1979), 391-400.
    • (1979) J. Biol. Chem , vol.254 , pp. 391-400
    • Charies, E.B.1    Hudson, B.S.2
  • 17
    • 0013471242 scopus 로고
    • How to illustrate ligand-protein binding in a class experiment: An elementary fluorescent assay
    • W. Marty, M. Boiret and M. Deumin, How to illustrate ligand-protein binding in a class experiment: An elementary fluorescent assay, J. Chem. Educ. 63 (1986), 365-366.
    • (1986) J. Chem. Educ , vol.63 , pp. 365-366
    • Marty, W.1    Boiret, M.2    Deumin, M.3
  • 18
    • 0018903487 scopus 로고
    • Study of reactivity of tryptophan residues in serum albumins and lysozyme by N-bromosuccinamide fluorescence quenching
    • B.F. Peterman and K.J. Laidler, Study of reactivity of tryptophan residues in serum albumins and lysozyme by N-bromosuccinamide fluorescence quenching, Arch. Biochem. Biophys. 199 (1980), 158-164.
    • (1980) Arch. Biochem. Biophys , vol.199 , pp. 158-164
    • Peterman, B.F.1    Laidler, K.J.2
  • 19
    • 0034518920 scopus 로고    scopus 로고
    • Native fluorescence and mag-indo-1-protein interaction as tools for probing unfolding and refolding sequences of the bovine serum albumin subdomain in the presence of guanidine hydrochloride
    • M.V. Pierre, V.D. Tuan, A.C. Ribou, V. Jean and J.M. Salmon, Native fluorescence and mag-indo-1-protein interaction as tools for probing unfolding and refolding sequences of the bovine serum albumin subdomain in the presence of guanidine hydrochloride, J. Protein Chem. 19 (2000), 431-439.
    • (2000) J. Protein Chem , vol.19 , pp. 431-439
    • Pierre, M.V.1    Tuan, V.D.2    Ribou, A.C.3    Jean, V.4    Salmon, J.M.5
  • 20
    • 0005885530 scopus 로고
    • Recent advances in molecular luminescence analysis
    • J.N. Miller, Recent advances in molecular luminescence analysis, Proc. Anal. Div. Chem. Soc. 16 (1979), 203-208.
    • (1979) Proc. Anal. Div. Chem. Soc , vol.16 , pp. 203-208
    • Miller, J.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.