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Volumn 12, Issue , 2015, Pages 458-467

Analysis of binding interaction of genistein and kaempferol with bovine α-lactalbumin

Author keywords

Alpha lactalbumin; Fluorescence quenching; Genistein; Kaempferol

Indexed keywords

BOVINAE;

EID: 84920724824     PISSN: 17564646     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jff.2014.12.012     Document Type: Article
Times cited : (88)

References (46)
  • 1
    • 79960370139 scopus 로고    scopus 로고
    • Interaction of α-lactalbumin with lipids and possible implications for its emulsifying properties
    • Barbana C., Perez M.D. Interaction of α-lactalbumin with lipids and possible implications for its emulsifying properties. International Dairy Journal 2011, 21:727-741.
    • (2011) International Dairy Journal , vol.21 , pp. 727-741
    • Barbana, C.1    Perez, M.D.2
  • 2
    • 27444437672 scopus 로고    scopus 로고
    • Interaction of bovine α-lactalbumin with fatty acids as determined by partition equilibrium and fluorescence spectroscopy
    • Barbana C., Perez M.D., Sanchez L., Dalgalarrondo M., Chobert J.M. Interaction of bovine α-lactalbumin with fatty acids as determined by partition equilibrium and fluorescence spectroscopy. International Dairy Journal 2006, 16:18-25.
    • (2006) International Dairy Journal , vol.16 , pp. 18-25
    • Barbana, C.1    Perez, M.D.2    Sanchez, L.3    Dalgalarrondo, M.4    Chobert, J.M.5
  • 3
    • 0021112616 scopus 로고
    • Manganese (II) electron spin resonance and cadmium-113 nuclear magnetic resonance evidence for the nature of the calcium binding site in alpha-lactalbumins
    • Berliner L.J., Ellis P.D., Murakami K. Manganese (II) electron spin resonance and cadmium-113 nuclear magnetic resonance evidence for the nature of the calcium binding site in alpha-lactalbumins. Biochemistry 1983, 22:5061-5063.
    • (1983) Biochemistry , vol.22 , pp. 5061-5063
    • Berliner, L.J.1    Ellis, P.D.2    Murakami, K.3
  • 5
    • 0014693695 scopus 로고
    • Possible three-dimensional structure of bovine α-lactalbumin based on that of hen's egg-white lysozyme
    • Browne W.J., North A.C.T., Phillips D.C. Possible three-dimensional structure of bovine α-lactalbumin based on that of hen's egg-white lysozyme. Journal of Molecular Biology 1969, 42:65-86.
    • (1969) Journal of Molecular Biology , vol.42 , pp. 65-86
    • Browne, W.J.1    North, A.C.T.2    Phillips, D.C.3
  • 6
    • 77955413591 scopus 로고    scopus 로고
    • Energetic domains analysis of bovine a-lactalbumin upon interaction with copper and dodecyl trimethylammonium bromide
    • Chamani J. Energetic domains analysis of bovine a-lactalbumin upon interaction with copper and dodecyl trimethylammonium bromide. Journal of Molecular Structure 2010, 979:227-234.
    • (2010) Journal of Molecular Structure , vol.979 , pp. 227-234
    • Chamani, J.1
  • 7
    • 84901020409 scopus 로고    scopus 로고
    • Lipid binding specificity of bovine α-lactalbumin: A multidimensional approach
    • Chaudhuri A., Chattopadhyay A. Lipid binding specificity of bovine α-lactalbumin: A multidimensional approach. Biochimica et Biophysica Acta 2014, 1838:2078-2086.
    • (2014) Biochimica et Biophysica Acta , vol.1838 , pp. 2078-2086
    • Chaudhuri, A.1    Chattopadhyay, A.2
  • 8
    • 33847688864 scopus 로고    scopus 로고
    • Pro-apoptotic effect and cytotoxicity of genistein and genistin in human ovarian cancer SK-OV-3 cells
    • Choi E.J., Kim T., Lee M.S. Pro-apoptotic effect and cytotoxicity of genistein and genistin in human ovarian cancer SK-OV-3 cells. Life Sciences 2007, 80:1403-1408.
    • (2007) Life Sciences , vol.80 , pp. 1403-1408
    • Choi, E.J.1    Kim, T.2    Lee, M.S.3
  • 9
    • 0032016551 scopus 로고    scopus 로고
    • Nutritional and functional characteristics of whey proteins in food products
    • de Wit J.N. Nutritional and functional characteristics of whey proteins in food products. Journal of Dairy Science 1998, 81:597-608.
    • (1998) Journal of Dairy Science , vol.81 , pp. 597-608
    • de Wit, J.N.1
  • 10
    • 0032794189 scopus 로고    scopus 로고
    • Fourier-transform infrared spectroscopy study of the pressure-induced changes in the structure of the bovine α-lactalbumin: The stabilizing role of the calcium ion
    • Dzwolak W., Kato M., Shimizu A., Taniguchi Y. Fourier-transform infrared spectroscopy study of the pressure-induced changes in the structure of the bovine α-lactalbumin: The stabilizing role of the calcium ion. Biochimica et Biophysica Acta 1999, 1433:45-55.
    • (1999) Biochimica et Biophysica Acta , vol.1433 , pp. 45-55
    • Dzwolak, W.1    Kato, M.2    Shimizu, A.3    Taniguchi, Y.4
  • 12
    • 84920726663 scopus 로고    scopus 로고
    • Study of the interaction of galangin, kaempferol and quercetin with BSA
    • Fu Z.D., Chen X.Q., Jiao F.P. Study of the interaction of galangin, kaempferol and quercetin with BSA. Latin American Applied Research 2012, 42:211-216.
    • (2012) Latin American Applied Research , vol.42 , pp. 211-216
    • Fu, Z.D.1    Chen, X.Q.2    Jiao, F.P.3
  • 15
    • 0033961193 scopus 로고    scopus 로고
    • A calorimetric study of the influence of calcium on the stability of bovine α-lactalbumin
    • Hendrix T., Griko Y.V., Privalov P.L. A calorimetric study of the influence of calcium on the stability of bovine α-lactalbumin. Biophysical Chemistry 2000, 84:27-34.
    • (2000) Biophysical Chemistry , vol.84 , pp. 27-34
    • Hendrix, T.1    Griko, Y.V.2    Privalov, P.L.3
  • 16
    • 23044497761 scopus 로고    scopus 로고
    • A differential scanning calorimetric study of the influence of copper and dodecyl trimethyl ammonium bromide on the stability of bovine α-lactalbumin
    • Housaindokht M.R., Chamani J., Moosavi-Movahedi A.A. A differential scanning calorimetric study of the influence of copper and dodecyl trimethyl ammonium bromide on the stability of bovine α-lactalbumin. International Journal of Biological Macromolecules 2005, 36:169-175.
    • (2005) International Journal of Biological Macromolecules , vol.36 , pp. 169-175
    • Housaindokht, M.R.1    Chamani, J.2    Moosavi-Movahedi, A.A.3
  • 17
    • 1842612537 scopus 로고    scopus 로고
    • Spectroscopic studies on the interaction of cinnamic acid and its hydroxyl derivatives with human serum albumin
    • Jiang M., Xie M.X., Zheng D., Liu Y., Li X.Y., Cheng X. Spectroscopic studies on the interaction of cinnamic acid and its hydroxyl derivatives with human serum albumin. Journal of Molecular Structure 2004, 692:71-80.
    • (2004) Journal of Molecular Structure , vol.692 , pp. 71-80
    • Jiang, M.1    Xie, M.X.2    Zheng, D.3    Liu, Y.4    Li, X.Y.5    Cheng, X.6
  • 18
    • 84884532812 scopus 로고    scopus 로고
    • Interactions between sodium oleate and α-lactalbumin
    • Kehoe J.J., Brodkorb A. Interactions between sodium oleate and α-lactalbumin. Food Hydrocolloids 2014, 34:217-226.
    • (2014) Food Hydrocolloids , vol.34 , pp. 217-226
    • Kehoe, J.J.1    Brodkorb, A.2
  • 19
    • 0031728288 scopus 로고    scopus 로고
    • The isoflavone genistein inhibits copper and peroxyl radical mediated low density lipoprotein oxidation in vitro
    • Kerry N., Abbey M. The isoflavone genistein inhibits copper and peroxyl radical mediated low density lipoprotein oxidation in vitro. Atherosclerosis 1998, 140:341-347.
    • (1998) Atherosclerosis , vol.140 , pp. 341-347
    • Kerry, N.1    Abbey, M.2
  • 20
    • 50549095066 scopus 로고    scopus 로고
    • Genistein inhibits aldose reductase activity and high glucose-induced TGF-β2 expression in human lens epithelial cells
    • Kim Y.S., Kim N.H., Jung D.H., Jang D.S., Lee Y.M., Kim J.M., Kim J.S. Genistein inhibits aldose reductase activity and high glucose-induced TGF-β2 expression in human lens epithelial cells. European Journal of Pharmacology 2008, 594:18-25.
    • (2008) European Journal of Pharmacology , vol.594 , pp. 18-25
    • Kim, Y.S.1    Kim, N.H.2    Jung, D.H.3    Jang, D.S.4    Lee, Y.M.5    Kim, J.M.6    Kim, J.S.7
  • 22
    • 67349201766 scopus 로고    scopus 로고
    • Studies on the interactions of kaempferol to calcineurin by spectroscopic methods and docking
    • Lei H., Qi Y., Jia Z., Lin W., Wei Q. Studies on the interactions of kaempferol to calcineurin by spectroscopic methods and docking. Biochimica et Biophysica Acta 2009, 1794:1269-1275.
    • (2009) Biochimica et Biophysica Acta , vol.1794 , pp. 1269-1275
    • Lei, H.1    Qi, Y.2    Jia, Z.3    Lin, W.4    Wei, Q.5
  • 26
    • 68949209203 scopus 로고    scopus 로고
    • Interaction of curcumin and diacetylcurcumin with the lipocalin member b-lactoglobulin
    • Mohammadi F., Bordbar A.K., Divsalar A., Mohammadi K., Saboury A.A. Interaction of curcumin and diacetylcurcumin with the lipocalin member b-lactoglobulin. Protein Journal 2009, 28:117-123.
    • (2009) Protein Journal , vol.28 , pp. 117-123
    • Mohammadi, F.1    Bordbar, A.K.2    Divsalar, A.3    Mohammadi, K.4    Saboury, A.A.5
  • 27
    • 68949207066 scopus 로고    scopus 로고
    • Analysis of binding interaction of curcumin and diacetylcurcumin with human and bovine serum albumin using fluorescence and circular dichroism spectroscopy
    • Mohammadi F., Bordbar A.K., Divsalar A., Mohammadi K., Saboury A.A. Analysis of binding interaction of curcumin and diacetylcurcumin with human and bovine serum albumin using fluorescence and circular dichroism spectroscopy. Protein Journal 2009, 28:189-196.
    • (2009) Protein Journal , vol.28 , pp. 189-196
    • Mohammadi, F.1    Bordbar, A.K.2    Divsalar, A.3    Mohammadi, K.4    Saboury, A.A.5
  • 28
    • 76649129899 scopus 로고    scopus 로고
    • Circular dichroism and fluorescence spectroscopic study on the interaction of bisdemethoxycurcumin and diacetylbisdemethoxycurcumin with human serum albumin
    • Mohammadi F., Bordbar A.K., Divsalar A., Mohammadi K., Saboury A.A. Circular dichroism and fluorescence spectroscopic study on the interaction of bisdemethoxycurcumin and diacetylbisdemethoxycurcumin with human serum albumin. Canadian Journal of Chemistry 2010, 88:155-163.
    • (2010) Canadian Journal of Chemistry , vol.88 , pp. 155-163
    • Mohammadi, F.1    Bordbar, A.K.2    Divsalar, A.3    Mohammadi, K.4    Saboury, A.A.5
  • 29
    • 0036134708 scopus 로고    scopus 로고
    • Kinetics of conformational changes induced by the binding of various metal ions to bovine α-lactalbumin
    • Noyelle K., Van Dael H. Kinetics of conformational changes induced by the binding of various metal ions to bovine α-lactalbumin. Journal of Inorganic Biochemistry 2002, 88:69-76.
    • (2002) Journal of Inorganic Biochemistry , vol.88 , pp. 69-76
    • Noyelle, K.1    Van Dael, H.2
  • 30
    • 70350575524 scopus 로고    scopus 로고
    • Encapsulation, stabilization, and controlled release of food ingredients and bioactives
    • CRC Press, Boca Raton, FL, M.S. Rahman (Ed.)
    • Pegg R.B., Shahidi F. Encapsulation, stabilization, and controlled release of food ingredients and bioactives. Handbook of food preservation 2007, CRC Press, Boca Raton, FL. 2nd ed. M.S. Rahman (Ed.).
    • (2007) Handbook of food preservation
    • Pegg, R.B.1    Shahidi, F.2
  • 32
    • 0034685838 scopus 로고    scopus 로고
    • α-Lactalbumin: Structure and function
    • Permyakov E.A., Berliner L.J. α-Lactalbumin: Structure and function. FEBS Letters 2000, 473:269-274.
    • (2000) FEBS Letters , vol.473 , pp. 269-274
    • Permyakov, E.A.1    Berliner, L.J.2
  • 34
    • 0021979565 scopus 로고
    • Cation binding effects on the pH, thermal and urea denaturation transitions in alpha-lactalbumin
    • Permyakov E.A., Morozova L.A., Burstein E.A. Cation binding effects on the pH, thermal and urea denaturation transitions in alpha-lactalbumin. The Journal of Biophysical Chemistry 1985, 21:21-31.
    • (1985) The Journal of Biophysical Chemistry , vol.21 , pp. 21-31
    • Permyakov, E.A.1    Morozova, L.A.2    Burstein, E.A.3
  • 35
    • 70450224072 scopus 로고    scopus 로고
    • Alpha-lactalbumin, engineered to be nonnative and inactive, kills tumor cells when in complex with oleic acid: A new biological function resulting from partial unfolding
    • Pettersson-Kastberg J., Mossberg A., Trulsson M., Yong Y.J., Min S., Lim Y., O'Brien J.E., Svanborg C., Mok K.H. Alpha-lactalbumin, engineered to be nonnative and inactive, kills tumor cells when in complex with oleic acid: A new biological function resulting from partial unfolding. Journal of Molecular Biology 2009, 394:994-1010.
    • (2009) Journal of Molecular Biology , vol.394 , pp. 994-1010
    • Pettersson-Kastberg, J.1    Mossberg, A.2    Trulsson, M.3    Yong, Y.J.4    Min, S.5    Lim, Y.6    O'Brien, J.E.7    Svanborg, C.8    Mok, K.H.9
  • 36
    • 0037900865 scopus 로고    scopus 로고
    • + binding to high affinity sites of calcium-containing proteins measured by capillary electrophoresis
    • + binding to high affinity sites of calcium-containing proteins measured by capillary electrophoresis. Journal of Inorganic Biochemistry 2003, 95:113-123.
    • (2003) Journal of Inorganic Biochemistry , vol.95 , pp. 113-123
    • Rasmussen, B.W.1    Bjerrum, M.J.2
  • 37
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: Forces contributing to stability
    • Ross P.D., Subramanian S. 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
  • 38
    • 0022214652 scopus 로고
    • Thermodynamics of the binding of calcium and strontium to bovine α-lactalbumin
    • Schaer J.J., Miles M., Cox J.X. Thermodynamics of the binding of calcium and strontium to bovine α-lactalbumin. FEBS Letters 1985, 190:77-80.
    • (1985) FEBS Letters , vol.190 , pp. 77-80
    • Schaer, J.J.1    Miles, M.2    Cox, J.X.3
  • 39
    • 0017872481 scopus 로고
    • Environment of tryptophan residues in α-lactalbumin
    • Takase K., Niki R., Arima S. Environment of tryptophan residues in α-lactalbumin. The Journal of Biochemistry 1978, 83:371-378.
    • (1978) The Journal of Biochemistry , vol.83 , pp. 371-378
    • Takase, K.1    Niki, R.2    Arima, S.3
  • 40
  • 41
    • 1842426864 scopus 로고
    • Oxygen quenching of fluorescence in solution: An experimental study of the diffusion process
    • Ware W.R. Oxygen quenching of fluorescence in solution: An experimental study of the diffusion process. The Journal of Physical Chemistry 1962, 66:455-458.
    • (1962) The Journal of Physical Chemistry , vol.66 , pp. 455-458
    • Ware, W.R.1
  • 43
    • 80155155891 scopus 로고    scopus 로고
    • Interaction of dietary polyphenols with bovine milk proteins: Molecular structure affinity relationship and influencing bioactivity aspects
    • Xia J., Mao F., Yang F., Zhao Y., Zhang C., Yamamoto K. Interaction of dietary polyphenols with bovine milk proteins: Molecular structure affinity relationship and influencing bioactivity aspects. Molecular Nutrition and Food Research 2011, 55:1637-1645.
    • (2011) Molecular Nutrition and Food Research , vol.55 , pp. 1637-1645
    • Xia, J.1    Mao, F.2    Yang, F.3    Zhao, Y.4    Zhang, C.5    Yamamoto, K.6
  • 44
    • 33747773827 scopus 로고    scopus 로고
    • Structural changes of α-lactalbumin induced by low pH and oleic acid
    • Yang F., Zhang M., Chen J., Liang Y. Structural changes of α-lactalbumin induced by low pH and oleic acid. Biochimica et Biophysica Acta 2006, 1764:1389-1396.
    • (2006) Biochimica et Biophysica Acta , vol.1764 , pp. 1389-1396
    • Yang, F.1    Zhang, M.2    Chen, J.3    Liang, Y.4
  • 46
    • 84859542905 scopus 로고    scopus 로고
    • SERS spectroscopy of kaempferol and galangin under the interaction of human serum albumin with adsorbed silver nanoparticles
    • Zhang W., Bai X., Wang Y., Zhao B., Zhao D., Zhao Y. SERS spectroscopy of kaempferol and galangin under the interaction of human serum albumin with adsorbed silver nanoparticles. Spectrochimica Acta Part A 2012, 92:234-237.
    • (2012) Spectrochimica Acta Part A , vol.92 , pp. 234-237
    • Zhang, W.1    Bai, X.2    Wang, Y.3    Zhao, B.4    Zhao, D.5    Zhao, Y.6


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