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Volumn 61, Issue 19, 2013, Pages 4606-4613

Erratum: Modulation of accessibility of subdomain IB in the pH-dependent interaction of bovine serum albumin with cochineal red A: A combined view from spectroscopy and docking simulations (Journal of Agricultural and Food Chemistry (2013) 61: 19 4606?4613 DOI 10.1021/jf305395n);Modulation of accessibility of subdomain IB in the pH-dependent interaction of bovine serum albumin with cochineal red A: A combined view from spectroscopy and docking simulations

Author keywords

BSA; differential accessibility; electrostatic interaction; food dye; molecular docking

Indexed keywords

BINDING ENERGY; COULOMB INTERACTIONS; ELECTROSTATICS; MODULATION; PH;

EID: 84877766968     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf403115b     Document Type: Erratum
Times cited : (36)

References (35)
  • 1
    • 0021782306 scopus 로고
    • Serum albumin
    • Peters, T. J. Serum albumin Adv. Prot. Chem. 1985, 37, 161-245
    • (1985) Adv. Prot. Chem. , vol.37 , pp. 161-245
    • Peters, T.J.1
  • 2
    • 14744275227 scopus 로고    scopus 로고
    • High-throughput solution-based medicinal library screening against human serum albumin
    • Flarakos, J.; Morand, K. L.; Vouros, P. High-throughput solution-based medicinal library screening against human serum albumin Anal. Chem. 2005, 77, 1345-1353
    • (2005) Anal. Chem. , vol.77 , pp. 1345-1353
    • Flarakos, J.1    Morand, K.L.2    Vouros, P.3
  • 3
    • 0034597380 scopus 로고    scopus 로고
    • Conformation changes of albumin in its interaction with physiologically active compounds as studied by quasi-elastic light scattering spectroscopy and ultrasonic method
    • Hushcha, T. O.; Luik, A. I.; Naboka, Y. N. Conformation changes of albumin in its interaction with physiologically active compounds as studied by quasi-elastic light scattering spectroscopy and ultrasonic method Talanta 2000, 53, 29-34
    • (2000) Talanta , vol.53 , pp. 29-34
    • Hushcha, T.O.1    Luik, A.I.2    Naboka, Y.N.3
  • 4
    • 0031805018 scopus 로고    scopus 로고
    • Use of azo dye ligand chromatography for the partial purification of a novel extracellular peroxidase from Streptomyces viridosporus T7A
    • Burke, N. S.; Crawford, D. L. Use of azo dye ligand chromatography for the partial purification of a novel extracellular peroxidase from Streptomyces viridosporus T7A Appl. Microbiol. Biotechnol. 1998, 49, 523-530
    • (1998) Appl. Microbiol. Biotechnol. , vol.49 , pp. 523-530
    • Burke, N.S.1    Crawford, D.L.2
  • 5
    • 0031901079 scopus 로고    scopus 로고
    • First-derivative spectrophotometric determination of ponceau 4R, sunset yellow and tartrazine in confectionery products
    • Sayar, S.; Ozdemir, Y. First-derivative spectrophotometric determination of ponceau 4R, sunset yellow and tartrazine in confectionery products Food Chem. 1998, 61, 367-372
    • (1998) Food Chem. , vol.61 , pp. 367-372
    • Sayar, S.1    Ozdemir, Y.2
  • 6
    • 0001851995 scopus 로고
    • Some aspects of the structure and conformational properties of serum albumin
    • Rosenoer, V. M. Oratz, M. Rothschild, M. A. Pergamon Press: New York
    • Föster, J. F. Some aspects of the structure and conformational properties of serum albumin. In Albumin Structure, Function and Uses; Rosenoer, V. M.; Oratz, M.; Rothschild, M. A., Eds.; Pergamon Press: New York, 1977; pp 53-84.
    • (1977) Albumin Structure, Function and Uses , pp. 53-84
    • Föster, J.F.1
  • 7
    • 84859598351 scopus 로고    scopus 로고
    • Optical spectroscopic exploration of binding of cochineal red A with two homologous serum albumins
    • Bolel, P.; Mahapatra, N.; Halder, M. Optical spectroscopic exploration of binding of cochineal red A with two homologous serum albumins J. Agric. Food Chem. 2012, 60, 3727-3734
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 3727-3734
    • Bolel, P.1    Mahapatra, N.2    Halder, M.3
  • 9
    • 83455195623 scopus 로고    scopus 로고
    • Comprehensive study of tartrazine/cationic surfactant interaction
    • Shahir, A. A.; Javadian, S.; Razavizadeh, B. B. M.; Gharibi, H. Comprehensive study of tartrazine/cationic surfactant interaction J. Phys. Chem. B 2011, 115, 14435-14444
    • (2011) J. Phys. Chem. B , vol.115 , pp. 14435-14444
    • Shahir, A.A.1    Javadian, S.2    Razavizadeh, B.B.M.3    Gharibi, H.4
  • 10
    • 2442711715 scopus 로고    scopus 로고
    • Interactions between some anionic dyes and cationic surfactants with different alkyl chain length studied by the method of continuous variations
    • Forte-Tavcer, P. Interactions between some anionic dyes and cationic surfactants with different alkyl chain length studied by the method of continuous variations Dyes Pigm. 2004, 63, 181-189
    • (2004) Dyes Pigm. , vol.63 , pp. 181-189
    • Forte-Tavcer, P.1
  • 11
    • 0033116302 scopus 로고    scopus 로고
    • More about the inner filter effect: Corrections of Stern-Volmer fluorescence quenching constants are necessary at very low optical absorption of the quencher
    • Borissevitch, I. E. More about the inner filter effect: corrections of Stern-Volmer fluorescence quenching constants are necessary at very low optical absorption of the quencher J. Lumin. 1999, 81, 219-224
    • (1999) J. Lumin. , vol.81 , pp. 219-224
    • Borissevitch, I.E.1
  • 12
    • 33750313393 scopus 로고    scopus 로고
    • Spectrofluorimetric studies on the binding of salicylic acid to bovine serum albumin using warfarin and ibuprofen as site markers with the aid of parallel factor analysis
    • Ni, Y.; Su, S.; Kokot, S. Spectrofluorimetric studies on the binding of salicylic acid to bovine serum albumin using warfarin and ibuprofen as site markers with the aid of parallel factor analysis Anal. Chim. Acta 2006, 580, 206-215
    • (2006) Anal. Chim. Acta , vol.580 , pp. 206-215
    • Ni, Y.1    Su, S.2    Kokot, S.3
  • 13
    • 84866661019 scopus 로고    scopus 로고
    • Structures of bovine, equine and leporine serum albumin
    • Bujacz, A. Structures of bovine, equine and leporine serum albumin Acta Crystallogr., Sect. D 2012, 68, 1278-1289
    • (2012) Acta Crystallogr., Sect. D , vol.68 , pp. 1278-1289
    • Bujacz, A.1
  • 14
    • 73349120806 scopus 로고    scopus 로고
    • Stewart Computational Chemistry: Colorado Springs, CO
    • Stewart, J. J. P. MOPAC2009; Stewart Computational Chemistry: Colorado Springs, CO, 2008.
    • (2008) MOPAC2009
    • Stewart, J.J.P.1
  • 15
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a lamarckian genetic algorithm and an empirical binding free energy function
    • Morris, G. M.; Goodsell, D. S.; Halliday, R. S.; Huey, R.; Hart, W. E.; Belew, R. K.; Olson, A. J. Automated docking using a lamarckian genetic algorithm and an empirical binding free energy function J. Comput. Chem. 1998, 19, 1639-1662
    • (1998) J. Comput. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 16
    • 0347141860 scopus 로고    scopus 로고
    • Studies on the reaction between ciprofloxacin and bovine serum albumin
    • Zhang, X. W.; Zhao, F. L.; Li, K. A. Studies on the reaction between ciprofloxacin and bovine serum albumin Chem. J. Chinese Univ. 1999, 20, 1063-1067
    • (1999) Chem. J. Chinese Univ. , vol.20 , pp. 1063-1067
    • Zhang, X.W.1    Zhao, F.L.2    Li, K.A.3
  • 18
    • 0019593952 scopus 로고
    • Fluorescence quenching studies with proteins
    • Eftink, M. R.; Ghiron, C. A. Fluorescence quenching studies with proteins Anal. Biochem. 1981, 114, 199-227
    • (1981) Anal. Biochem. , vol.114 , pp. 199-227
    • Eftink, M.R.1    Ghiron, C.A.2
  • 19
    • 0015230409 scopus 로고
    • Solute perturbation of protein fluorescence-quenching of tryptophyl fluorescence of model compounds and of lysozyme by iodide ion
    • Lehrer, S. S. Solute perturbation of protein fluorescence-quenching of 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.S.1
  • 21
    • 0025470458 scopus 로고
    • The adsorption of bovine serum albumin on positively and negatively charged polystyrene latices
    • Elgersma, A. V.; Zsom, R. L. J.; Norde, W.; Lyklema, J. The adsorption of bovine serum albumin on positively and negatively charged polystyrene latices J. Colloid Interface Sci. 1990, 138, 145-156
    • (1990) J. Colloid Interface Sci. , vol.138 , pp. 145-156
    • Elgersma, A.V.1    Zsom, R.L.J.2    Norde, W.3    Lyklema, J.4
  • 22
    • 0037062804 scopus 로고    scopus 로고
    • Protein transport in nanoporous membranes modified with self-assembled monolayers of functionalized thiols
    • Chun, K. Y.; Stroeve, P. Protein transport in nanoporous membranes modified with self-assembled monolayers of functionalized thiols Langmuir 2002, 18, 4653-4658
    • (2002) Langmuir , vol.18 , pp. 4653-4658
    • Chun, K.Y.1    Stroeve, P.2
  • 23
    • 33645699944 scopus 로고    scopus 로고
    • Protein tryptophan accessibility studied by fluorescence quenching
    • Moller, M.; Denicola, A. Protein tryptophan accessibility studied by fluorescence quenching Biochem. Mol. Biol. Educ. 2002, 30, 175-178
    • (2002) Biochem. Mol. Biol. Educ. , vol.30 , pp. 175-178
    • Moller, M.1    Denicola, A.2
  • 24
    • 3042673067 scopus 로고    scopus 로고
    • Crystal structural analysis of human serum albumin complexed with hemin and fatty acid
    • Zunszain, P. A.; Ghuman, J.; Komatsu, T.; Tsuchida, E.; Curry, S. Crystal structural analysis of human serum albumin complexed with hemin and fatty acid BMC Struct. Biol. 2003, 3, 6-14
    • (2003) BMC Struct. Biol. , vol.3 , pp. 6-14
    • Zunszain, P.A.1    Ghuman, J.2    Komatsu, T.3    Tsuchida, E.4    Curry, S.5
  • 25
    • 0042691054 scopus 로고    scopus 로고
    • Interaction of albumins and hemin with aromatic antioxidants: A spectrophotometric and fluorometric study
    • Rus, O. B.; Puchkaev, A. V.; Ivanov, A. I.; Metelitsa, D. I. Interaction of albumins and hemin with aromatic antioxidants: a spectrophotometric and fluorometric study Appl. Biochem. Microbiol. 2000, 36, 36-45
    • (2000) Appl. Biochem. Microbiol. , vol.36 , pp. 36-45
    • Rus, O.B.1    Puchkaev, A.V.2    Ivanov, A.I.3    Metelitsa, D.I.4
  • 28
    • 0033618249 scopus 로고    scopus 로고
    • Interaction of 7-hydroxy-8-(phenylazo)-1,3-naphthalenedisulfonate with bovine plasma albumin: Spectroscopic studies
    • Patel, A. B.; Srivastava, S.; Phadke, R. S. Interaction of 7-hydroxy-8-(phenylazo)-1,3-naphthalenedisulfonate with bovine plasma albumin: spectroscopic studies J. Biol. Chem. 1999, 274, 21755-21762
    • (1999) J. Biol. Chem. , vol.274 , pp. 21755-21762
    • Patel, A.B.1    Srivastava, S.2    Phadke, R.S.3
  • 29
    • 55349105837 scopus 로고    scopus 로고
    • Interaction of serum albumin with vinyl sulfonate azo dye
    • Sereikaite, J.; Bumelis, V. A. Interaction of serum albumin with vinyl sulfonate azo dye Cent. Eur. J. Chem. 2008, 6, 509-512
    • (2008) Cent. Eur. J. Chem. , vol.6 , pp. 509-512
    • Sereikaite, J.1    Bumelis, V.A.2
  • 30
    • 84865692573 scopus 로고    scopus 로고
    • Spectroscopic investigation of the effect of salt on binding of tartrazine with two homologous serum albumins: Quantification by use of the Debye-Hückel limiting law and observation of enthalpy-entropy compensation
    • Bolel, P.; Datta, S.; Mahapatra, N.; Halder, M. Spectroscopic investigation of the effect of salt on binding of tartrazine with two homologous serum albumins: quantification by use of the Debye-Hückel limiting law and observation of enthalpy-entropy compensation J. Phys. Chem. B 2012, 116, 10195-10204
    • (2012) J. Phys. Chem. B , vol.116 , pp. 10195-10204
    • Bolel, P.1    Datta, S.2    Mahapatra, N.3    Halder, M.4
  • 32
    • 14744268162 scopus 로고    scopus 로고
    • Studies on the interaction between 1-hexylcarbamoyl-5-fluorouracil and bovine serum albumin
    • Hu, Y. J.; Liu, Y.; Shen, X. S.; Fang, X. Y.; Qu, S. S. Studies on the interaction between 1-hexylcarbamoyl-5-fluorouracil and bovine serum albumin J. Mol. Str. 2005, 738, 143-147
    • (2005) J. Mol. Str. , vol.738 , pp. 143-147
    • Hu, Y.J.1    Liu, Y.2    Shen, X.S.3    Fang, X.Y.4    Qu, S.S.5
  • 34
    • 0028906380 scopus 로고
    • Endonuclease-III interactions with DNA substrates. 2. The DNA-repair enzyme endonuclease-III binds differently to intact DNA and to apyrimidinic apurinic DNA substrates as shown by tryptophan fluorescence quenching
    • Xing, D. X.; Dorr, R.; Cunningham, R. P.; Scholes, C. P. Endonuclease-III interactions with DNA substrates. 2. The DNA-repair enzyme endonuclease-III binds differently to intact DNA and to apyrimidinic apurinic DNA substrates as shown by tryptophan fluorescence quenching Biochemistry 1995, 34, 2537-2544
    • (1995) Biochemistry , vol.34 , pp. 2537-2544
    • Xing, D.X.1    Dorr, R.2    Cunningham, R.P.3    Scholes, C.P.4
  • 35
    • 51249164070 scopus 로고
    • Selective quenching of tryptophanyl fluorescence in bovine serum-albumin by the iodide ion
    • Maruthamuthu, M.; Selvakumar, G. Selective quenching of tryptophanyl fluorescence in bovine serum-albumin by the iodide ion Proc. Indian Acad. Sci. Chem. Sci. 1995, 107, 79-86
    • (1995) Proc. Indian Acad. Sci. Chem. Sci. , vol.107 , pp. 79-86
    • Maruthamuthu, M.1    Selvakumar, G.2


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