메뉴 건너뛰기




Volumn 39, Issue 4, 2010, Pages 482-494

In vitro study of the binding of taxifolin to bovine serum albumin and the influence of common ions on the binding

Author keywords

Bovine serum albumin; Common ions; Interaction; Quenching of fluorescence; Taxifolin

Indexed keywords


EID: 77952093188     PISSN: 00959782     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10953-010-9516-y     Document Type: Article
Times cited : (13)

References (31)
  • 3
    • 37549055478 scopus 로고    scopus 로고
    • Mechanistic study on the enzymatic oxidation of flavonols
    • 10.1016/j.tetlet.2007.11.147 1:CAS:528:DC%2BD1cXis1aisw%3D%3D
    • S. Ghidouche N.F. Es-Safi P.H. Ducrot 2008 Mechanistic study on the enzymatic oxidation of flavonols Tetrahedron Lett. 49 619 623 10.1016/j.tetlet.2007.11.147 1:CAS:528:DC%2BD1cXis1aisw%3D%3D
    • (2008) Tetrahedron Lett. , vol.49 , pp. 619-623
    • Ghidouche, S.1    Es-Safi, N.F.2    Ducrot, P.H.3
  • 4
    • 0034522961 scopus 로고    scopus 로고
    • Modulation of hepatic lipoprotein synthesis and secretion by taxifolin, a plant flavonoid
    • 1:CAS:528:DC%2BD3MXhsVOkuw%3D%3D
    • A. Theriault Q. Wang S.C. Van Iderstine B. Chen A.A. Franke K. Adeli 2000 Modulation of hepatic lipoprotein synthesis and secretion by taxifolin, a plant flavonoid J. Lipid Res. 41 1969 1979 1:CAS:528:DC%2BD3MXhsVOkuw%3D%3D
    • (2000) J. Lipid Res. , vol.41 , pp. 1969-1979
    • Theriault, A.1    Wang, Q.2    Van Iderstine, S.C.3    Chen, B.4    Franke, A.A.5    Adeli, K.6
  • 5
    • 52649114815 scopus 로고    scopus 로고
    • Flavonoids, taxifolin and luteolin attenuate cellular melanogenesis despite increasing tyrosinase protein levels
    • 10.1002/ptr.2435 1:CAS:528:DC%2BD1cXht1aqtrrK
    • S.M. An H.J. Kim J.E. Kim Y.C. Boo 2008 Flavonoids, taxifolin and luteolin attenuate cellular melanogenesis despite increasing tyrosinase protein levels Phytother. Res. 22 1200 1207 10.1002/ptr.2435 1:CAS:528: DC%2BD1cXht1aqtrrK
    • (2008) Phytother. Res. , vol.22 , pp. 1200-1207
    • An, S.M.1    Kim, H.J.2    Kim, J.E.3    Boo, Y.C.4
  • 6
    • 0019524375 scopus 로고
    • The location of drug binding sites in human serum albumin
    • DOI 10.1016/0006-2952(81)90151-9
    • K.J. Fehske W.E. Müller U. Wollert 1981 The location of drug binding sites in human serum albumin Biochem. Pharmacol. 30 687 692 10.1016/0006-2952(81)90151-9 1:CAS:528:DyaL3MXksFKnsrY%3D (Pubitemid 11146814)
    • (1981) Biochemical Pharmacology , vol.30 , Issue.7 , pp. 687-692
    • Fehske, K.J.1    Mueller, W.E.2    Wollert, U.3
  • 7
    • 0028227096 scopus 로고
    • Structure of serum albumin
    • 10.1016/S0065-3233(08)60640-3 1:CAS:528:DyaK2cXltVajtLk%3D
    • D.C. Carter J.X. Ho 1994 Structure of serum albumin Adv. Protein Chem. 45 153 203 10.1016/S0065-3233(08)60640-3 1:CAS:528:DyaK2cXltVajtLk%3D
    • (1994) Adv. Protein Chem. , vol.45 , pp. 153-203
    • Carter, D.C.1    Ho, J.X.2
  • 8
    • 0021782306 scopus 로고
    • Serum albumin
    • 10.1016/S0065-3233(08)60065-0 1:CAS:528:DyaL2MXmtV2js70%3D
    • T. Peters 1985 Serum albumin Adv. Protein Chem. 37 161 236 10.1016/S0065-3233(08)60065-0 1:CAS:528:DyaL2MXmtV2js70%3D
    • (1985) Adv. Protein Chem. , vol.37 , pp. 161-236
    • Peters, T.1
  • 9
    • 20444423659 scopus 로고    scopus 로고
    • Effect of metal ions on the interaction between bovine serum albumin and berberine chloride extracted from a traditional Chinese Herb coptis chinensis franch
    • DOI 10.1016/j.jinorgbio.2005.02.025, PII S0162013405000589
    • X.F. Liu Y.M. Xia Y. Fang 2005 Effect of metal ions on the interaction between bovine serum albumin and berberine chloride extracted from a traditional Chinese herb Coptis chinensis franch J. Inorg. Biochem. 99 1449 1457 10.1016/j.jinorgbio.2005.02.025 1:CAS:528:DC%2BD2MXltFartb8%3D (Pubitemid 40804954)
    • (2005) Journal of Inorganic Biochemistry , vol.99 , Issue.7 , pp. 1449-1457
    • Liu, X.-F.1    Xia, Y.-M.2    Fang, Y.3
  • 10
    • 16644381647 scopus 로고    scopus 로고
    • Studies on dihydroflavonol glycosides from rhizome of Smilax glabra
    • 1:CAS:528:DC%2BD2MXhtlClurnK
    • J.Z. Yuan D.Q. Dou Y.J. Chen W. Li K. Kazuo N. Tamotsu X.S. Yao 2004 Studies on dihydroflavonol glycosides from rhizome of Smilax glabra J. Chin. Med. Mater. 29 867 870 1:CAS:528:DC%2BD2MXhtlClurnK
    • (2004) J. Chin. Med. Mater. , vol.29 , pp. 867-870
    • Yuan, J.Z.1    Dou, D.Q.2    Chen, Y.J.3    Li, W.4    Kazuo, K.5    Tamotsu, N.6    Yao, X.S.7
  • 11
    • 36348976813 scopus 로고    scopus 로고
    • Spectroscopic investigation of inner filter effect by magnolol solutions
    • DOI 10.1016/j.saa.2007.02.002, PII S1386142507000790
    • H.M. Li Y.Z. Hu 2007 Spectroscopic investigation of inner filter effect by magnolol solutions Spectrochim. Acta. A 68 1263 1268 10.1016/j.saa.2007.02. 002 (Pubitemid 350161397)
    • (2007) Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy , vol.68 , Issue.5 , pp. 1263-1268
    • Li, H.M.1    Hu, Y.Z.2
  • 13
    • 0001917250 scopus 로고
    • Fluorescence quenching: Theory and applications
    • J.R. Lakowicz (eds). Plenum Press New York
    • Eftink, M.R.: Fluorescence Quenching: Theory and Applications. In: Lakowicz, J.R. (ed.) Topics in Fluorescence Spectroscopy. Principles, vol. 2, p. 55. Plenum Press, New York (1991)
    • (1991) Topics in Fluorescence Spectroscopy , vol.2 , pp. 55
    • Eftink, M.R.1
  • 14
    • 0015907980 scopus 로고
    • Quenching of fluorescence by oxygen. A probe for structural fluctuations in macromolecules
    • 1:CAS:528:DyaE3sXlsVeks78%3D
    • R.J. Lakowicz G. Webber 1973 Quenching of fluorescence by oxygen. A probe for structural fluctuations in macromolecules Bio. Chem. 12 4161 4170 1:CAS:528:DyaE3sXlsVeks78%3D
    • (1973) Bio. Chem. , vol.12 , pp. 4161-4170
    • Lakowicz, R.J.1    Webber, G.2
  • 15
    • 3042793205 scopus 로고    scopus 로고
    • Study on the interaction of colchicine and bovine serum albumins by fluorescence method
    • Y.M. Liu G.Z. Li X.F. Sun 2004 Study on the interaction of colchicine and bovine serum albumins by fluorescence method Chin. J. Anal. Chem. 32 615 618
    • (2004) Chin. J. Anal. Chem. , vol.32 , pp. 615-618
    • Liu, Y.M.1    Li, G.Z.2    Sun, X.F.3
  • 16
    • 0037060027 scopus 로고    scopus 로고
    • Study of the interaction between terazosin and serum albumin -Synchronous fluorescence determination of terazosin
    • DOI 10.1016/S0003-2670(01)01453-2, PII S0003267001014532
    • C.Q. Jiang M.X. Gao J.X. He 2002 Study of the interaction between terazosin and serum albumin synchronous fluorescence determination of terazosin Anal. Chim. Acta 452 185 189 10.1016/S0003-2670(01)01453-2 1:CAS:528: DC%2BD38Xmtlaguw%3D%3D (Pubitemid 34135977)
    • (2002) Analytica Chimica Acta , vol.452 , Issue.2 , pp. 185-189
    • Jiang, C.-Q.1    Gao, M.-X.2    He, J.-X.3
  • 17
    • 33645292880 scopus 로고    scopus 로고
    • Study of the Interaction of carbamazepine with bovine serum albumin by fluorescence quenching method
    • 10.2116/analsci.22.435 1:CAS:528:DC%2BD28XjvFars78%3D
    • C. Wang Q.H. Wu Z. Wang J. Zhao 2006 Study of the Interaction of carbamazepine with bovine serum albumin by fluorescence quenching method Anal. Sci. 22 435 438 10.2116/analsci.22.435 1:CAS:528:DC%2BD28XjvFars78%3D
    • (2006) Anal. Sci. , vol.22 , pp. 435-438
    • Wang, C.1    Wu, Q.H.2    Wang, Z.3    Zhao, J.4
  • 18
    • 1842426864 scopus 로고
    • Oxygen quenching of fluorescence in solution: An experimental study of the diffusion process
    • 10.1021/j100809a020
    • W.R. Ware 1962 Oxygen quenching of fluorescence in solution: an experimental study of the diffusion process J. Phys. Chem. 66 445 458 10.1021/j100809a020
    • (1962) J. Phys. Chem. , vol.66 , pp. 445-458
    • Ware, W.R.1
  • 19
    • 0034661298 scopus 로고    scopus 로고
    • Quantitative determination of PEG-hirudin in human plasma using a competitive enzyme-linked immunosorbent assay
    • DOI 10.1016/S0049-3848(00)00246-2, PII S0049384800002462
    • X.H. Song G. Huhle L.C. Wang J. Harenberg 2000 Quantitative determination of PEG-hirudin in human plasma using a competitive enzyme-linked immunosorbent assay Thromb. Res. 99 195 202 10.1016/S0049-3848(00)00246-2 1:CAS:528: DC%2BD3cXls1Clsbc%3D (Pubitemid 30628493)
    • (2000) Thrombosis Research , vol.99 , Issue.2 , pp. 195-202
    • Song, X.H.1    Huhle, G.2    Wang, L.C.3    Harenberg, J.4
  • 20
    • 0035808405 scopus 로고    scopus 로고
    • Flow-injection analysis chemiluminescence detection combined with microdialysis sampling for studying protein binding of drug
    • DOI 10.1016/S0039-9140(00)00569-5, PII S0039914000005695
    • Y.M. Huang Z.J. Zhang D.J. Zhang J.G. Lv 2001 Flow-injection analysis chemiluminescence detection combined with microdialysis sampling for studying protein binding of drug Talanta 53 835 841 10.1016/S0039-9140(00)00569-5 1:CAS:528:DC%2BD3MXntFOquw%3D%3D (Pubitemid 32064763)
    • (2001) Talanta , vol.53 , Issue.4 , pp. 835-841
    • Huang, Y.1    Zhang, Z.2    Zhang, D.3    Lv, J.4
  • 21
    • 1842782322 scopus 로고    scopus 로고
    • Thermodynamics studies on the reaction characteristics between piroxican and bovine serum albumin
    • 1:CAS:528:DC%2BD2cXjsVCmsbw%3D
    • C.N. Yan Y.F. Shangguan Z.T. Pang Y. Liu S.S. Qu 2004 Thermodynamics studies on the reaction characteristics between piroxican and bovine serum albumin Chin. J. Anal. Chem. 32 317 319 1:CAS:528:DC%2BD2cXjsVCmsbw%3D
    • (2004) Chin. J. Anal. Chem. , vol.32 , pp. 317-319
    • Yan, C.N.1    Shangguan, Y.F.2    Pang, Z.T.3    Liu, Y.4    Qu, S.S.5
  • 23
    • 33947553005 scopus 로고
    • The structure of water and hydrophobic binding in proteins
    • 10.1021/j100816a004
    • G. Némethy A.S. Harold 1962 The structure of water and hydrophobic binding in proteins J. Phys. Chem. 66 1773 1789 10.1021/j100816a004
    • (1962) J. Phys. Chem. , vol.66 , pp. 1773-1789
    • Némethy, G.1    Harold, A.S.2
  • 24
    • 0024805333 scopus 로고
    • Thermodynamics of the binding of phenothiazines to human plasma, human serum albumin and alpha 1-acid glycoprotein: A calorimetric study
    • 1:CAS:528:DyaK3cXhsF2iuw%3D%3D
    • H. Aki H. Yamamoto 1989 Thermodynamics of the binding of phenothiazines to human plasma, human serum albumin and alpha 1-acid glycoprotein: a calorimetric study J. Pharm. Pharmacol. 41 674 679 1:CAS:528: DyaK3cXhsF2iuw%3D%3D
    • (1989) J. Pharm. Pharmacol. , vol.41 , pp. 674-679
    • Aki, H.1    Yamamoto, H.2
  • 25
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: Forces contributing to stability
    • 10.1021/bi00514a017 1:CAS:528:DyaL3MXktF2qsb0%3D
    • P.D. Ross S. Subrimanian 1981 Thermodynamics of protein association reactions: forces contributing to stability Biochemistry 20 3096 3102 10.1021/bi00514a017 1:CAS:528:DyaL3MXktF2qsb0%3D
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subrimanian, S.2
  • 26
    • 0017661379 scopus 로고    scopus 로고
    • Conjugated polyene fatty acids as fluorescent probes: Binding to bovine serum albumin
    • 10.1021/bi00642a024
    • L.A. Skalar B.S. Hudson R.D. Simoni 1997 Conjugated polyene fatty acids as fluorescent probes: binding to bovine serum albumin Biochemistry 16 5100 5108 10.1021/bi00642a024
    • (1997) Biochemistry , vol.16 , pp. 5100-5108
    • Skalar, L.A.1    Hudson, B.S.2    Simoni, R.D.3
  • 27
    • 0000056380 scopus 로고
    • Resonance energy transfer
    • J.R. Lakowicz (eds). Plenum Press New York
    • Herber, C.C.: Resonance energy transfer. In: Lakowicz, J.R. (ed.) Topics in Fluorescence Spectroscopy. Principles, vol. 2, pp. 127-130. Plenum Press, New York (1991)
    • (1991) Topics in Fluorescence Spectroscopy , vol.2 , pp. 127-130
    • Herber, C.C.1
  • 28
    • 85044700016 scopus 로고    scopus 로고
    • Separation of the tyrosine and tryptophan components of fluorescence using synchronous scanning method
    • 1:CAS:528:DyaK2sXkvVWhtrg%3D
    • N.L. Vekshin 1996 Separation of the tyrosine and tryptophan components of fluorescence using synchronous scanning method Biofizika 41 1176 1179 1:CAS:528:DyaK2sXkvVWhtrg%3D
    • (1996) Biofizika , vol.41 , pp. 1176-1179
    • Vekshin, N.L.1
  • 29
    • 0017943943 scopus 로고
    • Multicomponent analysis by synchronous luminescence spectrometry
    • 10.1021/ac50025a010
    • T. Vo-Dinh 1978 Multicomponent analysis by synchronous luminescence spectrometry Anal. Chem. 50 396 401 10.1021/ac50025a010
    • (1978) Anal. Chem. , vol.50 , pp. 396-401
    • Vo-Dinh, T.1
  • 30
    • 0036148318 scopus 로고    scopus 로고
    • Fluorescence studies on PAMAM dendrimers interactions with bovine serum albumin
    • DOI 10.1016/S1567-5394(01)00170-0, PII S1567539401001700
    • B. Klajnert M. Bryszewska 2002 Fluorescence studies on PAMAM dendrimers interactions with bovine serum albumin Bioelectrochemistry 55 33 35 10.1016/S1567-5394(01)00170-0 1:CAS:528:DC%2BD38Xls1eguw%3D%3D (Pubitemid 34084746)
    • (2002) Bioelectrochemistry , vol.55 , Issue.1-2 , pp. 33-35
    • Klajnert, B.1    Bryszewska, M.2
  • 31
    • 33745472421 scopus 로고    scopus 로고
    • Studies on the interaction of tricyclazole with β-cyclodextrin and human serum albumin by spectroscopy
    • DOI 10.1007/s10895-006-0087-7
    • H.X. Zhang X. Huang P. Mei K.H. Li C.N. Yan 2006 Studies on the interaction of tricyclazole with β-cyclodextrin and human serum albumin by spectroscopy J. Fluoresc. 16 287 294 10.1007/s10895-006-0087-7 1:CAS:528:DC%2BD28XmsFOnsb4%3D (Pubitemid 43952754)
    • (2006) Journal of Fluorescence , vol.16 , Issue.3 , pp. 287-294
    • Zhang, H.-X.1    Huang, X.2    Mei, P.3    Li, K.-H.4    Yan, C.-N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.