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Volumn 42, Issue 6, 2013, Pages 1169-1182

Spectroscopic studies on the interaction between troxerutin and bovine hemoglobin

Author keywords

Bovine hemoglobin; Fluorescence quenching; Thermal stability; Troxerutin

Indexed keywords


EID: 84880043493     PISSN: 00959782     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10953-013-0033-7     Document Type: Article
Times cited : (9)

References (34)
  • 1
    • 37049075436 scopus 로고
    • Micelle-induced release of heme-NO from nitric oxide complex of myoglobin
    • 10.1039/c39930001447
    • Das, T.K.; Mazumdar, S.; Mitra, S.: Micelle-induced release of heme-NO from nitric oxide complex of myoglobin. J. Chem. Soc. Chem. Commun. 18, 1447-1448 (1993)
    • (1993) J. Chem. Soc. Chem. Commun. , vol.18 , pp. 1447-1448
    • Das, T.K.1    Mazumdar, S.2    Mitra, S.3
  • 2
    • 80053390286 scopus 로고    scopus 로고
    • Crystallographic trapping of heme loss intermediates during the nitrite-induced degradation of human hemoglobin
    • 10.1021/bi2009322 1:CAS:528:DC%2BC3MXhtFWqt7zJ
    • Yi, J.; Thomas, L.M.; Musayev, F.N.; Safo, M.K.; Richter-Addo, G.B.: Crystallographic trapping of heme loss intermediates during the nitrite-induced degradation of human hemoglobin. Biochemistry 50, 8323-8332 (2011)
    • (2011) Biochemistry , vol.50 , pp. 8323-8332
    • Yi, J.1    Thomas, L.M.2    Musayev, F.N.3    Safo, M.K.4    Richter-Addo, G.B.5
  • 3
    • 0033537052 scopus 로고    scopus 로고
    • Role of interhelical H-bonds (Wα14-Tα67 and Wβ15-Sβ72) in the hemoglobin allosteric reaction path evaluated by UV resonance Raman spectroscopy of site-mutants
    • 10.1021/ja992228w 1:CAS:528:DyaK1MXnsFOmtro%3D
    • Wang, D.J.; Zhao, X.J.; Shen, T.J.; Ho, C.; Spiro, T.G.: Role of interhelical H-bonds (Wα14-Tα67 and Wβ15-Sβ72) in the hemoglobin allosteric reaction path evaluated by UV resonance Raman spectroscopy of site-mutants. J. Am. Chem. Soc. 121, 11197-11203 (1999)
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 11197-11203
    • Wang, D.J.1    Zhao, X.J.2    Shen, T.J.3    Ho, C.4    Spiro, T.G.5
  • 4
    • 0033790875 scopus 로고    scopus 로고
    • Heme structure of hemoglobin M Iwate [α87(F8)His → Tyr]: A UV and visible resonance Raman study
    • 10.1021/bi001029i 1:CAS:528:DC%2BD3cXmvVantLc%3D
    • Nagai, M.; Aki, M.; Li, R.; Jin, Y.; Sakai, H.; Nagatomo, S.: Heme structure of hemoglobin M Iwate [α87(F8)His → Tyr]: a UV and visible resonance Raman study. Biochemistry 39, 13093-13105 (2000)
    • (2000) Biochemistry , vol.39 , pp. 13093-13105
    • Nagai, M.1    Aki, M.2    Li, R.3    Jin, Y.4    Sakai, H.5    Nagatomo, S.6
  • 5
    • 0014958182 scopus 로고
    • Stereoschemistry of cooperative effects in haemoglobin
    • 10.1038/228726a0 1:CAS:528:DyaE3MXjvVertQ%3D%3D
    • Perutz, M.F.: Stereoschemistry of cooperative effects in haemoglobin. Nature 228, 726-734 (1970)
    • (1970) Nature , vol.228 , pp. 726-734
    • Perutz, M.F.1
  • 6
    • 0035387644 scopus 로고    scopus 로고
    • Electron-transfer reactivity and enzymatic activity of hemoglobin in a SP sephadex membrane
    • 10.1021/ac001397s 1:CAS:528:DC%2BD3MXjtVKhsL0%3D
    • Fan, C.H.; Wang, H.Y.; Sun, S.; Zhu, D.X.; Wagner, G.; Li, G.X.: Electron-transfer reactivity and enzymatic activity of hemoglobin in a SP sephadex membrane. Anal. Chem. 73, 2850-2854 (2001)
    • (2001) Anal. Chem. , vol.73 , pp. 2850-2854
    • Fan, C.H.1    Wang, H.Y.2    Sun, S.3    Zhu, D.X.4    Wagner, G.5    Li, G.X.6
  • 7
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • 10.1038/358209a0 1:CAS:528:DyaK38XlsVGmurg%3D
    • He, X.M.; Carter, D.C.: Atomic structure and chemistry of human serum albumin. Nature 358, 209-215 (1992)
    • (1992) Nature , vol.358 , pp. 209-215
    • He, X.M.1    Carter, D.C.2
  • 8
    • 77956645556 scopus 로고    scopus 로고
    • Binding of oxytetracycline to bovine serum albumin: Spectroscopic and molecular modeling investigations
    • 10.1021/jf101417w 1:CAS:528:DC%2BC3cXhtVOnsrrF
    • Chi, Z.X.; Liu, R.T.; Teng, Y.; Fang, X.Y.; Gao, C.Z.: Binding of oxytetracycline to bovine serum albumin: spectroscopic and molecular modeling investigations. J. Agric. Food Chem. 58, 10262-10269 (2010)
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 10262-10269
    • Chi, Z.X.1    Liu, R.T.2    Teng, Y.3    Fang, X.Y.4    Gao, C.Z.5
  • 9
    • 78651291244 scopus 로고    scopus 로고
    • Phenotypic characterization of the binding of tetracycline to human serum albumin
    • 10.1021/bm1011568 1:CAS:528:DC%2BC3cXhsFGhs7jI
    • Chi, Z.X.; Liu, R.T.: Phenotypic characterization of the binding of tetracycline to human serum albumin. Biomacromolecules 12, 203-209 (2011)
    • (2011) Biomacromolecules , vol.12 , pp. 203-209
    • Chi, Z.X.1    Liu, R.T.2
  • 10
    • 84857386435 scopus 로고    scopus 로고
    • Heme reactivity is uncoupled from quaternary structure in gel-encapsulated hemoglobin: A resonance Raman spectroscopic study
    • 10.1021/ja210126j 1:CAS:528:DC%2BC38XhtVymurw%3D
    • Jones, E.M.; Balakrishnan, G.; Spiro, T.G.: Heme reactivity is uncoupled from quaternary structure in gel-encapsulated hemoglobin: a resonance Raman spectroscopic study. J. Am. Chem. Soc. 134, 3461-3471 (2012)
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 3461-3471
    • Jones, E.M.1    Balakrishnan, G.2    Spiro, T.G.3
  • 11
    • 0030047619 scopus 로고    scopus 로고
    • Stabilization of the tetrameric structure of human and bovine hemoglobins by pseudocrosslinking with muconic acid
    • 10.1006/abbi.1996.0055 1:CAS:528:DyaK28Xnslygsg%3D%3D
    • Razynska, A.; Matheson-Urbaitis, B.; Fronticelli, C.; Collins, J.H.; Bucci, E.: Stabilization of the tetrameric structure of human and bovine hemoglobins by pseudocrosslinking with muconic acid. Arch. Biochem. Biophys. 326, 119-125 (1996)
    • (1996) Arch. Biochem. Biophys. , vol.326 , pp. 119-125
    • Razynska, A.1    Matheson-Urbaitis, B.2    Fronticelli, C.3    Collins, J.H.4    Bucci, E.5
  • 12
    • 77956429695 scopus 로고    scopus 로고
    • Ultrasound-promoted enzymatic synthesis of troxerutin esters in nonaqueous solvents
    • 10.1016/j.ultsonch.2010.06.010 1:CAS:528:DC%2BC3cXhtFGqsbvN
    • Xiao, Y.M.; Yang, L.R.; Mao, P.; Zhao, Z.; Lin, X.F.: Ultrasound-promoted enzymatic synthesis of troxerutin esters in nonaqueous solvents. Ultrason. Sonochem. 18, 303-309 (2011)
    • (2011) Ultrason. Sonochem. , vol.18 , pp. 303-309
    • Xiao, Y.M.1    Yang, L.R.2    Mao, P.3    Zhao, Z.4    Lin, X.F.5
  • 13
    • 77956345140 scopus 로고    scopus 로고
    • Chronic administration of troxerutin protects mouse kidney against d-galactose-induced oxidative DNA damage
    • 10.1016/j.fct.2010.07.011 1:CAS:528:DC%2BC3cXhtFGjtbzP
    • Liu, C.M.; Ma, J.Q.; Lou, Y.: Chronic administration of troxerutin protects mouse kidney against d-galactose-induced oxidative DNA damage. Food Chem. Toxicol. 48, 2809-2817 (2010)
    • (2010) Food Chem. Toxicol. , vol.48 , pp. 2809-2817
    • Liu, C.M.1    Ma, J.Q.2    Lou, Y.3
  • 14
    • 39149102818 scopus 로고    scopus 로고
    • Aescin and troxerutin as a successful combination for the treatment of inner ear perfusion disturbances
    • 10.1016/j.phymed.2007.11.025 1:CAS:528:DC%2BD1cXkslKmt7w%3D
    • Siegers, C.P.; Ali, S.S.; Tegtmeier, M.: Aescin and troxerutin as a successful combination for the treatment of inner ear perfusion disturbances. Phytomedicine 15, 160-163 (2008)
    • (2008) Phytomedicine , vol.15 , pp. 160-163
    • Siegers, C.P.1    Ali, S.S.2    Tegtmeier, M.3
  • 15
    • 0037432596 scopus 로고    scopus 로고
    • Vascular permeabilization by intravenous arachidonate peritoneal cavity: Antagonism by ethamsylate
    • 10.1016/S0014-2999(03)01545-0 1:CAS:528:DC%2BD3sXisV2rs7w%3D
    • Hannaert, P.; Alvarez-Guerra, M.; Hider, H.; Chiavaroli, C.; Garay, R.P.: Vascular permeabilization by intravenous arachidonate peritoneal cavity: antagonism by ethamsylate. Eur. J. Pharmacol. 466, 207-212 (2003)
    • (2003) Eur. J. Pharmacol. , vol.466 , pp. 207-212
    • Hannaert, P.1    Alvarez-Guerra, M.2    Hider, H.3    Chiavaroli, C.4    Garay, R.P.5
  • 16
    • 4544230202 scopus 로고    scopus 로고
    • Radioprotection of normal tissues in tumor-bearing mice by troxerutin
    • 10.1269/jrr.45.221 1:CAS:528:DC%2BD2cXot1Oqtro%3D
    • Maurya, D.K.; Salvi, V.P.; Nair, C.K.K.: Radioprotection of normal tissues in tumor-bearing mice by troxerutin. J. Radiat. Res. 45, 221-228 (2004)
    • (2004) J. Radiat. Res. , vol.45 , pp. 221-228
    • Maurya, D.K.1    Salvi, V.P.2    Nair, C.K.K.3
  • 17
    • 76949095167 scopus 로고    scopus 로고
    • Chronic administration of troxerutin protects mouse brain against d-galactose-induced impairment of cholinergic system
    • 10.1016/j.nlm.2009.09.006 1:CAS:528:DC%2BC3cXisFOitLY%3D
    • Lu, J.; Wu, D.M.; Hu, B.; Cheng, W.; Zheng, Y.L.; Zhang, Z.F.; Ye, Q.; Fan, S.H.; Shan, Q.; Wang, Y.J.: Chronic administration of troxerutin protects mouse brain against d-galactose-induced impairment of cholinergic system. Neurobiol. Learn. Mem. 93, 157-164 (2010)
    • (2010) Neurobiol. Learn. Mem. , vol.93 , pp. 157-164
    • Lu, J.1    Wu, D.M.2    Hu, B.3    Cheng, W.4    Zheng, Y.L.5    Zhang, Z.F.6    Ye, Q.7    Fan, S.H.8    Shan, Q.9    Wang, Y.J.10
  • 19
    • 12944318828 scopus 로고    scopus 로고
    • Troxerutin protects the isolated perfused rat liver from a possible lipid peroxidation by coumarin
    • 10.1016/j.phymed.2004.01.007 1:CAS:528:DC%2BD2MXisVSltL8%3D
    • Adam, B.S.; Pentz, R.; Siegers, C.P.; Strubelt, O.; Tegtmeier, M.: Troxerutin protects the isolated perfused rat liver from a possible lipid peroxidation by coumarin. Phytomedicine 12, 52-61 (2005)
    • (2005) Phytomedicine , vol.12 , pp. 52-61
    • Adam, B.S.1    Pentz, R.2    Siegers, C.P.3    Strubelt, O.4    Tegtmeier, M.5
  • 20
    • 31344469151 scopus 로고    scopus 로고
    • The interaction of hemoglobin with hexadecyltrimethylammonium bromide
    • 10.1016/j.ijbiomac.2005.11.007 1:CAS:528:DC%2BD28XotVCltw%3D%3D
    • Liu, W.J.; Guo, X.; Guo, R.: The interaction of hemoglobin with hexadecyltrimethylammonium bromide. Int. J. Biol. Macromol. 37, 232-238 (2005)
    • (2005) Int. J. Biol. Macromol. , vol.37 , pp. 232-238
    • Liu, W.J.1    Guo, X.2    Guo, R.3
  • 21
    • 35348971410 scopus 로고    scopus 로고
    • Probing the interaction of ellagic acid with human serum albumin: A fluorescence spectroscopic study
    • 10.1016/j.jphotochem.2007.05.018
    • Nand, R.K.; Sarkar, N.; Banerjee, R.: Probing the interaction of ellagic acid with human serum albumin: a fluorescence spectroscopic study. J. Photochem. Photobiol. A 192, 152-158 (2007)
    • (2007) J. Photochem. Photobiol. A , vol.192 , pp. 152-158
    • Nand, R.K.1    Sarkar, N.2    Banerjee, R.3
  • 22
    • 33846846332 scopus 로고    scopus 로고
    • Interaction of curcumin with human serum albumin: Thermodynamic properties, fluorescence energy transfer and denaturation effects
    • 10.1016/j.cplett.2007.01.006 1:CAS:528:DC%2BD2sXhsFKqtbw%3D
    • Barik, A.; Mishra, B.; Kunwar, A.; Priyadarsini, K.I.: Interaction of curcumin with human serum albumin: thermodynamic properties, fluorescence energy transfer and denaturation effects. Chem. Phys. Lett. 436, 239-243 (2007)
    • (2007) Chem. Phys. Lett. , vol.436 , pp. 239-243
    • Barik, A.1    Mishra, B.2    Kunwar, A.3    Priyadarsini, K.I.4
  • 23
    • 0015907980 scopus 로고
    • Quenching of fluorescence by oxygen. Probe for structural fluctuations in macromolecules
    • 10.1021/bi00745a020 1:CAS:528:DyaE3sXlsVeks78%3D
    • Lakowicz, J.R.; Weber, G.: Quenching of fluorescence by oxygen. Probe for structural fluctuations in macromolecules. Biochemistry 12, 4161-4170 (1973)
    • (1973) Biochemistry , vol.12 , pp. 4161-4170
    • Lakowicz, J.R.1    Weber, G.2
  • 24
    • 1842426864 scopus 로고
    • Oxygen quenching of fluorescence in solution: An experimental study of the diffusion process
    • 10.1021/j100809a020 1:CAS:528:DyaF38XktVygtLw%3D
    • Ware, W.R.: Oxygen quenching of fluorescence in solution: an experimental study of the diffusion process. J. Phys. Chem. 66, 455-458 (1962)
    • (1962) J. Phys. Chem. , vol.66 , pp. 455-458
    • Ware, W.R.1
  • 25
    • 35348862691 scopus 로고    scopus 로고
    • The interaction between hemoglobin and two surfactants with different charges
    • 10.1016/j.ijbiomac.2007.07.006 1:CAS:528:DC%2BD2sXhtF2qt7jE
    • Liu, W.J.; Guo, X.; Guo, R.: The interaction between hemoglobin and two surfactants with different charges. Int. J. Biol. Macromol. 41, 548-557 (2007)
    • (2007) Int. J. Biol. Macromol. , vol.41 , pp. 548-557
    • Liu, W.J.1    Guo, X.2    Guo, R.3
  • 26
    • 0344690387 scopus 로고    scopus 로고
    • The interaction between triton X-100 and bovine serum albumin
    • 1:CAS:528:DC%2BD3cXls1egtrc%3D
    • Wei, X.F.; Liu, H.Z.: The interaction between triton X-100 and bovine serum albumin. Chin. J. Anal. Chem. 28, 699-701 (2000)
    • (2000) Chin. J. Anal. Chem. , vol.28 , pp. 699-701
    • Wei, X.F.1    Liu, H.Z.2
  • 27
    • 77954400472 scopus 로고    scopus 로고
    • 2O microemulsion
    • 10.1111/j.1751-1097.2010.00752.x 1:CAS:528:DC%2BC3cXhtVaiurrM
    • 2O microemulsion. Photochem. Photobiol. 86, 835-843 (2010)
    • (2010) Photochem. Photobiol. , vol.86 , pp. 835-843
    • Liu, W.J.1    Guo, R.2
  • 28
    • 78751702234 scopus 로고    scopus 로고
    • Interaction of triprolidine hydrochloride with serum albumins: Thermodynamic and binding characteristics and influence of site probes
    • 10.1016/j.jpba.2010.12.012 1:CAS:528:DC%2BC3MXhtVWku70%3D
    • Sandhya, B.; Hegde, A.H.; Kalanur, S.S.; Katrahalli, U.; Seetharamappa, J.: Interaction of triprolidine hydrochloride with serum albumins: thermodynamic and binding characteristics and influence of site probes. J. Pharm. Biomed. Anal. 54, 1180-1186 (2011)
    • (2011) J. Pharm. Biomed. Anal. , vol.54 , pp. 1180-1186
    • Sandhya, B.1    Hegde, A.H.2    Kalanur, S.S.3    Katrahalli, U.4    Seetharamappa, J.5
  • 29
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: Forces contributing to stability
    • 10.1021/bi00514a017 1:CAS:528:DyaL3MXktF2qsb0%3D
    • Ross, P.D.; Subramanian, S.: Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 20, 3096-3102 (1981)
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 30
    • 84865417743 scopus 로고    scopus 로고
    • Interaction of pyrrolizine derivatives with bovine serum albumin by fluorescence and UV-Vis spectroscopy
    • 10.1016/j.saa.2012.05.013 1:CAS:528:DC%2BC38Xhtl2gtbbL
    • Zhang, J.; Xiong, D.X.; Chen, L.N.; Kang, Q.L.; Zeng, B.R.: Interaction of pyrrolizine derivatives with bovine serum albumin by fluorescence and UV-Vis spectroscopy. Spectrochim. Acta A 96, 132-138 (2012)
    • (2012) Spectrochim. Acta A , vol.96 , pp. 132-138
    • Zhang, J.1    Xiong, D.X.2    Chen, L.N.3    Kang, Q.L.4    Zeng, B.R.5
  • 31
    • 0017661379 scopus 로고
    • Simoni quenching of fluorescence by oxygen. Probe for structural fluctuations in macromolecules, R. D.: Conjugated polyene fatty acids as fluorescent probes: Binding to bovine serum albumin
    • 10.1021/bi00642a024 1:CAS:528:DyaE1cXhvFKr
    • Sklar, L.A.; Hudson, B.S.: Simoni quenching of fluorescence by oxygen. Probe for structural fluctuations in macromolecules, R. D.: conjugated polyene fatty acids as fluorescent probes: binding to bovine serum albumin. Biochemistry 16, 5100-5108 (1977)
    • (1977) Biochemistry , vol.16 , pp. 5100-5108
    • Sklar, L.A.1    Hudson, B.S.2
  • 32
    • 79551631402 scopus 로고    scopus 로고
    • Characterization of phenosafranine-hemoglobin interactions in aqueous solution
    • 10.1007/s10953-010-9647-1 1:CAS:528:DC%2BC3MXht1SqtrY%3D
    • Liu, W.; Ding, F.; Sun, Y.: Characterization of phenosafranine-hemoglobin interactions in aqueous solution. J. Solution Chem. 40, 231-246 (2011)
    • (2011) J. Solution Chem. , vol.40 , pp. 231-246
    • Liu, W.1    Ding, F.2    Sun, Y.3
  • 33
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set
    • 10.1006/abio.2000.4880 1:CAS:528:DC%2BD3cXosFGhu7Y%3D
    • Sreerama, N.; Woody, R.W.: Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set. Anal. Biochem. 287, 252-260 (2000)
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 34
    • 70350398116 scopus 로고    scopus 로고
    • Structure and function of hemoglobin confined inside silica nanotubes
    • 10.1021/jp9032707 1:CAS:528:DC%2BD1MXptVKntbc%3D
    • Kapoor, S.; Mandal, S.S.; Bhattacharyya, A.J.: Structure and function of hemoglobin confined inside silica nanotubes. J. Phys. Chem. B 113, 14189-14195 (2009)
    • (2009) J. Phys. Chem. B , vol.113 , pp. 14189-14195
    • Kapoor, S.1    Mandal, S.S.2    Bhattacharyya, A.J.3


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