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Volumn 24, Issue 5, 2009, Pages 355-362

Investigation of the interactions of quercetin and morin with trypsin

Author keywords

Fluorescence spectroscopy; Morin; Quercetin; Three dimensional fluorescence spectra; Trypsin

Indexed keywords

FLAVONOIDS; FLUORESCENCE; PH; PHENOLS;

EID: 70350422779     PISSN: 15227235     EISSN: 15227243     Source Type: Journal    
DOI: 10.1002/bio.1121     Document Type: Article
Times cited : (25)

References (37)
  • 2
    • 0003723604 scopus 로고
    • Proteinase inhibitors as drugs
    • In, Elsevier, Amsterdam
    • H. P. Schnebli, N. J. Braun, Proteinase inhibitors as drugs. In Proteinase Inhibitors. Elsevier, Amsterdam, 1986; 613-627.
    • (1986) Proteinase Inhibitors , pp. 613-627
    • Schnebli, H.P.1    Braun, N.J.2
  • 3
    • 0034824115 scopus 로고    scopus 로고
    • Thermodynamic analysis of binding of p-substituted benzamidines to trypsin
    • R. Talhout, J. B. F. N. Engberts, Thermodynamic analysis of binding of p-substituted benzamidines to trypsin. Eur. J. Biochem. 2001; 268, 1554-1560.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1554-1560
    • Talhout, R.1    Engberts, J.B.F.N.2
  • 4
    • 33947102664 scopus 로고    scopus 로고
    • Adsorption of trypsin on hydrophilic and hydrophobic surfaces
    • S. Koutsopoulos, K. Patzsch, W. T. E. Bosker, W. Norde, Adsorption of trypsin on hydrophilic and hydrophobic surfaces. Langmuir 2007; 23, 2000-2006.
    • (2007) Langmuir , vol.23 , pp. 2000-2006
    • Koutsopoulos, S.1    Patzsch, K.2    Bosker, W.T.E.3    Norde, W.4
  • 5
    • 0346022974 scopus 로고    scopus 로고
    • Understanding protein-ligand interaction: The price of protein flexibility
    • D. Rauh, G. Klebe, M. T. Stubbs, Understanding protein-ligand interaction: the price of protein flexibility. J. Mol. Biol. 2004; 335, 1325-1341.
    • (2004) J. Mol. Biol. , vol.335 , pp. 1325-1341
    • Rauh, D.1    Klebe, G.2    Stubbs, M.T.3
  • 6
    • 0000705433 scopus 로고
    • Studies on the active center of trypsin: The binding of amidines and guanidines as models of the substrate side chain
    • M. Mares-Guia, E. Shaw, Studies on the active center of trypsin: the binding of amidines and guanidines as models of the substrate side chain. J. Biol. Chem. 1965; 240, 1579-1585.
    • (1965) J. Biol. Chem. , vol.240 , pp. 1579-1585
    • Mares-Guia, M.1    Shaw, E.2
  • 8
    • 0032513281 scopus 로고    scopus 로고
    • Quantitative analysis of flavonols, flavones, and flavanones in fruits, vegetables and beverages by HPLC with photo-diode array and mass spectrometric detection
    • U. Justesen, P. Knuthsen, T. Leth, Quantitative analysis of flavonols, flavones, and flavanones in fruits, vegetables and beverages by HPLC with photo-diode array and mass spectrometric detection, J. Chromatogr. A 1998; 799, 101-110.
    • (1998) J. Chromatogr. A , vol.799 , pp. 101-110
    • Justesen, U.1    Knuthsen, P.2    Leth, T.3
  • 9
    • 11844253806 scopus 로고    scopus 로고
    • Flavonoid-serum albumin complexation: Determination of binding constants and binding sites by fluorescence spectroscopy
    • C. Dufour, O. Dangles, Flavonoid-serum albumin complexation: determination of binding constants and binding sites by fluorescence spectroscopy. Biochim. Biophys. Acta 2005; 1721, 164-173.
    • (2005) Biochim. Biophys. Acta , vol.1721 , pp. 164-173
    • Dufour, C.1    Dangles, O.2
  • 10
    • 10944248747 scopus 로고    scopus 로고
    • Comparative analysis of topoisomerase IB inhibition and DNA intercalation by flavonoids and similar compounds: Structural determinates of activity
    • M. R. Webb, S. E. Ebeler, Comparative analysis of topoisomerase IB inhibition and DNA intercalation by flavonoids and similar compounds: structural determinates of activity. Biochem. J. 2004; 384, 527-541.
    • (2004) Biochem. J. , vol.384 , pp. 527-541
    • Webb, M.R.1    Ebeler, S.E.2
  • 11
    • 0029610477 scopus 로고
    • Review of the biology of quercetin and related bioflavonoids
    • J. V. Formica, W. Regelson, Review of the biology of quercetin and related bioflavonoids. Food. Chem. Toxicol. 1995; 33, 1061-1080.
    • (1995) Food. Chem. Toxicol. , vol.33 , pp. 1061-1080
    • Formica, J.V.1    Regelson, W.2
  • 12
    • 0035906326 scopus 로고    scopus 로고
    • Role of plant polyphenols in genomic stability
    • L. R. Ferguson, Role of plant polyphenols in genomic stability. Mutat. Res. 2001; 475, 89-111.
    • (2001) Mutat. Res. , vol.475 , pp. 89-111
    • Ferguson, L.R.1
  • 13
    • 33745280263 scopus 로고    scopus 로고
    • Characterization of the interaction between human serum albumin and morin
    • M. X. Xie, M. Long, Y. Liu, C. Qin, Y. D. Wang, Characterization of the interaction between human serum albumin and morin. Biochim. Biophys. Acta 2006; 1760, 1184-1191.
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 1184-1191
    • Xie, M.X.1    Long, M.2    Liu, Y.3    Qin, C.4    Wang, Y.D.5
  • 14
    • 34548359418 scopus 로고    scopus 로고
    • Spectroscopic study on binding of rutin to human serum albumin
    • A. V. Pastukhov, L. A. Levchenko, A. P. Sadkov, Spectroscopic study on binding of rutin to human serum albumin. J. Mol. Struct. 2007; 842, 60-66.
    • (2007) J. Mol. Struct. , vol.842 , pp. 60-66
    • Pastukhov, A.V.1    Levchenko, L.A.2    Sadkov, A.P.3
  • 15
    • 55249103413 scopus 로고    scopus 로고
    • Characteristics of the isomeric flavonoids apigenin and genistein binding to hemoglobin by spectroscopic methods
    • doi:10.1016/j.molstruc.2008.04.017
    • J. L. Yuan, H. Liu, X. Kang, Z. Lv, G. L. Zou, Characteristics of the isomeric flavonoids apigenin and genistein binding to hemoglobin by spectroscopic methods. J. Mol. Struct. doi:10.1016/j.molstruc.2008.04.017.
    • J. Mol. Struct
    • Yuan, J.L.1    Liu, H.2    Kang, X.3    Lv, Z.4    Zou, G.L.5
  • 17
    • 0037300833 scopus 로고    scopus 로고
    • Probing the binding of the flavonoidm quercetin to human serum albumin by circular dichroism, electronic absorption spectroscopy and molecular modeling methods
    • F. Zsila, Z. Bikádi, M. Simonyi, Probing the binding of the flavonoidm quercetin to human serum albumin by circular dichroism, electronic absorption spectroscopy and molecular modeling methods. Biochem. Pharmacol. 2003; 65, 447-456.
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 447-456
    • Zsila, F.1    Bikádi, Z.2    Simonyi, M.3
  • 18
    • 0036434544 scopus 로고    scopus 로고
    • The interaction of quercetin with human serum albumin: A fluorescence spectroscopic study. Biochem
    • B. Sengupta, P. K. Sengupta, The interaction of quercetin with human serum albumin: a fluorescence spectroscopic study. Biochem. Biophys. Res. Commun. 2002; 299, 400-403.
    • (2002) Biophys. Res. Commun. , vol.299 , pp. 400-403
    • Sengupta, B.1    Sengupta, P.K.2
  • 20
    • 33846929891 scopus 로고    scopus 로고
    • Interactions between flavonoids and hemoglobin in lecithin liposomes
    • J. Q. Xi, R. Guo, Interactions between flavonoids and hemoglobin in lecithin liposomes. Inter. J. Biol. Macromol. 2007; 40, 305-311.
    • (2007) Inter. J. Biol. Macromol. , vol.40 , pp. 305-311
    • Xi, J.Q.1    Guo, R.2
  • 21
    • 41949122581 scopus 로고    scopus 로고
    • GM1-induced structural changes of bovine serum albumin after chemical and thermal disruption of the secondary structure: A spectroscopic comparison
    • A. Gayen, C. Chatterjee, C. Mukhopadhyay, GM1-induced structural changes of bovine serum albumin after chemical and thermal disruption of the secondary structure: a spectroscopic comparison. Biomacromolecules 2008; 9, 974-983.
    • (2008) Biomacromolecules , vol.9 , pp. 974-983
    • Gayen, A.1    Chatterjee, C.2    Mukhopadhyay, C.3
  • 23
    • 0015907980 scopus 로고
    • Quenching of fluorescence by oxygen. Probe for structural fluctuations in macromolecules
    • J. R. Lakowicz, G. Weber, Quenching of fluorescence by oxygen. Probe for structural fluctuations in macromolecules. Biochemistry 1973; 12, 4161-4170.
    • (1973) Biochemistry , vol.12 , pp. 4161-4170
    • Lakowicz, J.R.1    Weber, G.2
  • 24
    • 0015230409 scopus 로고
    • Solute perturbation of protein fluorescence. Quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion
    • S. Lehrer, Solute perturbation of protein fluorescence. Quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry 1971; 10, 3254-3263.
    • (1971) Biochemistry , vol.10 , pp. 3254-3263
    • Lehrer, S.1
  • 25
    • 46749141417 scopus 로고    scopus 로고
    • Spectroscopic studies on the interaction of lanthanum(III) 2-oxo-propionic acid salicyloyl hydrazone complex with bovine serum albumin
    • Y. Z. Zhang, X. X. Chen, J. Dai, X. P. Zhang, H. X. Liu, Y. Liu, Spectroscopic studies on the interaction of lanthanum(III) 2-oxo-propionic acid salicyloyl hydrazone complex with bovine serum albumin. Luminescence 2008; 23, 15-156.
    • (2008) Luminescence , vol.23 , pp. 15-156
    • Zhang, Y.Z.1    Chen, X.X.2    Dai, J.3    Zhang, X.P.4    Liu, H.X.5    Liu, Y.6
  • 26
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: Forces contributing to stability
    • P. D. Ross, S. Subramanian, 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
  • 27
    • 23444447825 scopus 로고    scopus 로고
    • Studies of interaction between colchicine and bovine serum albumin by fluorescence quenching method
    • Y. J. Hu, Y. Liu, L. X. Zhang, Studies of interaction between colchicine and bovine serum albumin by fluorescence quenching method. J. Mol. Struct. 2005; 750, 174-178.
    • (2005) J. Mol. Struct. , vol.750 , pp. 174-178
    • Hu, Y.J.1    Liu, Y.2    Zhang, L.X.3
  • 28
    • 27644475219 scopus 로고    scopus 로고
    • Interaction of cromolyn sodium with human serum albumin: A fluorescence quenching study
    • Y. J. Hu, Y. Liu, Z. B. Pi, S. S. Qu, Interaction of cromolyn sodium with human serum albumin: a fluorescence quenching study. Bioorg. Med. Chem. 2005; 13, 6609-6614.
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 6609-6614
    • Hu, Y.J.1    Liu, Y.2    Pi, Z.B.3    Qu, S.S.4
  • 30
    • 11344257292 scopus 로고    scopus 로고
    • Molecular spectroscopic study on the interaction of tetracyclines with serum albumins
    • S. Y. Bi, D. Q. Song, L. Ding, Y. Tian, X. Zhou, X. Liu, Molecular spectroscopic study on the interaction of tetracyclines with serum albumins. Spectrochim. Acta Pt A 2005; 61, 629-636.
    • (2005) Spectrochim. Acta Pt A , vol.61 , pp. 629-636
    • Bi, S.Y.1    Song, D.Q.2    Ding, L.3    Tian, Y.4    Zhou, X.5    Liu, X.6
  • 31
    • 0017661379 scopus 로고
    • Conjugate polyene fatty acids as fluorescent membrane probes
    • L. A. Sklar, B. S. Hudson, R. D. Simoni, Conjugate polyene fatty acids as fluorescent membrane probes. Biochemistry 1977; 16, 5100-5108.
    • (1977) Biochemistry , vol.16 , pp. 5100-5108
    • Sklar, L.A.1    Hudson, B.S.2    Simoni, R.D.3
  • 32
    • 0033608984 scopus 로고    scopus 로고
    • Formation of the covalent serpinproteinase complex involves translocation of the proteinase by more than 70 Å and full insertion of the reactive center loop into βsheet A
    • E. Stratikos, P. G. W. Gettins, Formation of the covalent serpinproteinase complex involves translocation of the proteinase by more than 70 Å and full insertion of the reactive center loop into βsheet A. Proc. Natl Acad. Sci. USA 1999; 96, 4808-4813.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 4808-4813
    • Stratikos, E.1    Gettins, P.G.W.2
  • 33
    • 0002593607 scopus 로고
    • Multicomponent analysis by synchronous luminescence spectrometry
    • J. B. F. Lloyd, Multicomponent analysis by synchronous luminescence spectrometry. Nature 1971; 231, 6-65.
    • (1971) Nature , vol.231 , pp. 6-65
    • Lloyd, J.B.F.1
  • 34
    • 0027249523 scopus 로고
    • The binding interaction of coomassie blue with protein
    • W. C. Abert, W. M. Gregory, G. S. Allan, The binding interaction of coomassie blue with protein. Anal. Biochem. 1993; 213, 407-413.
    • (1993) Anal. Biochem. , vol.213 , pp. 407-413
    • Abert, W.C.1    Gregory, W.M.2    Allan, G.S.3
  • 36
    • 33644935077 scopus 로고    scopus 로고
    • In situ estimation of the entire color and spectra of age pigment-like materials: Application of a front-surface 3D-fluorescence technique
    • G. L. Lin, Y. Y. Liao, X. H. Wang, S. L. Sheng, D. Z. Yin, In situ estimation of the entire color and spectra of age pigment-like materials: application of a front-surface 3D-fluorescence technique. Exp. Gerontol. 2006; 41, 328-336.
    • (2006) Exp. Gerontol. , vol.41 , pp. 328-336
    • Lin, G.L.1    Liao, Y.Y.2    Wang, X.H.3    Sheng, S.L.4    Yin, D.Z.5
  • 37
    • 0000200876 scopus 로고
    • Studies on the ultraviolet difference spectra of proteins and polypeptides
    • A. N. Glazer, E. L. Smith, Studies on the ultraviolet difference spectra of proteins and polypeptides. J. Biol. Chem. 1961; 236, 2942-2947.
    • (1961) J. Biol. Chem. , vol.236 , pp. 2942-2947
    • Glazer, A.N.1    Smith, E.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.