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Volumn 54, Issue 14, 2006, Pages 4962-4969

Interactions between bovine β-lactoglobulin A and various bioactive peptides as studied by front-face fluorescence spectroscopy

Author keywords

Bioactive peptide; Bovine lactoglobulin A; Front face fluorescence spectroscopy; Protein peptide interaction

Indexed keywords

LACTOGLOBULIN; PEPTIDE; PHENYLALANINE;

EID: 33746483941     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf060506m     Document Type: Article
Times cited : (13)

References (60)
  • 1
    • 0034684161 scopus 로고    scopus 로고
    • The core lipocalin, bovine β-lactoglobulin
    • Sawyer, L.; Kontopidis, G. The core lipocalin, bovine β-lactoglobulin. Biochim. Biophys. Acta 2000, 1482, 136-148.
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 136-148
    • Sawyer, L.1    Kontopidis, G.2
  • 2
    • 0034492691 scopus 로고    scopus 로고
    • Opioid peptides encrypted in intact milk protein sequences
    • Meisel, H.; FitzGerald, R. J. Opioid peptides encrypted in intact milk protein sequences. Br. J. Nutr. 2000, 84, S27-S31.
    • (2000) Br. J. Nutr. , vol.84
    • Meisel, H.1    FitzGerald, R.J.2
  • 3
    • 0034199281 scopus 로고    scopus 로고
    • Bioactive milk peptides: A prospectus
    • Clare, D. A.; Swaisgood, H. E. Bioactive milk peptides: a prospectus. J. Dairy Sci. 2000, 83, 1187-1195.
    • (2000) J. Dairy Sci. , vol.83 , pp. 1187-1195
    • Clare, D.A.1    Swaisgood, H.E.2
  • 4
    • 0034494479 scopus 로고    scopus 로고
    • Effects of milk-derived bioactives: An overview
    • Shah, N. P. Effects of milk-derived bioactives: an overview. Br. J. Nutr. 2000, 84, S3-S10.
    • (2000) Br. J. Nutr. , vol.84
    • Shah, N.P.1
  • 5
    • 0034633086 scopus 로고    scopus 로고
    • Bioactive peptides derived from bovine whey proteins: Opioid and ace-inhibitory
    • Pihlanto-Leppälä, A. Bioactive peptides derived from bovine whey proteins: opioid and ace-inhibitory. Trends Food Sci. Technol. 2001, 11, 347-356.
    • (2001) Trends Food Sci. Technol. , vol.11 , pp. 347-356
    • Pihlanto-Leppälä, A.1
  • 6
    • 2342544490 scopus 로고    scopus 로고
    • Functional and biological properties of peptides obtained by enzymatic hydrolysis of whey proteins
    • Gauthier, S. F.; Pouliot, Y. Functional and biological properties of peptides obtained by enzymatic hydrolysis of whey proteins. J. Dairy Sci. 2003, 86, E78-E87.
    • (2003) J. Dairy Sci. , vol.86
    • Gauthier, S.F.1    Pouliot, Y.2
  • 7
    • 0028965716 scopus 로고
    • Impact of esterification on the folding and the susceptibility to peptic proteolysis of β-lactoglobulin
    • Chobert, J.-M.; Briand, L.; Grinberg, V.; Haertlé, T. Impact of esterification on the folding and the susceptibility to peptic proteolysis of β-lactoglobulin. Biochim. Biophys. Acta 1995, 1248, 170-176.
    • (1995) Biochim. Biophys. Acta , vol.1248 , pp. 170-176
    • Chobert, J.-M.1    Briand, L.2    Grinberg, V.3    Haertlé, T.4
  • 8
    • 0000420114 scopus 로고    scopus 로고
    • Digestibility of bovine milk whey protein and β-lactoglobulin in vitro and in vivo
    • Kitabatake, N.; Kinekawa, Y.-I. Digestibility of bovine milk whey protein and β-lactoglobulin in vitro and in vivo. J. Agric. Food Chem. 1998, 46, 4917-4923.
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 4917-4923
    • Kitabatake, N.1    Kinekawa, Y.-I.2
  • 10
    • 0345313659 scopus 로고    scopus 로고
    • β-lactoglobulin binds palmitate within its central cavity
    • Wu, S.-Y.; Pérez, M. D.; Puyol, P.; Sawyer, L. β-lactoglobulin binds palmitate within its central cavity. J. Biol. Chem. 1999, 274, 170-174.
    • (1999) J. Biol. Chem. , vol.274 , pp. 170-174
    • Wu, S.-Y.1    Pérez, M.D.2    Puyol, P.3    Sawyer, L.4
  • 11
    • 0039842514 scopus 로고    scopus 로고
    • Structural changes accompanying pH-induced dissociation of the β-lactoglobulin dimer
    • Uhrinova, S.; Smith, M. H.; Jameson, G. B.; Uhrin, D., Sawyer, L.; Barlow, P. N. Structural changes accompanying pH-induced dissociation of the β-lactoglobulin dimer. Biochemistry 2000, 39, 3565-3574.
    • (2000) Biochemistry , vol.39 , pp. 3565-3574
    • Uhrinova, S.1    Smith, M.H.2    Jameson, G.B.3    Uhrin, D.4    Sawyer, L.5    Barlow, P.N.6
  • 12
    • 0001497241 scopus 로고
    • The reversible transformation of β-lactoglobulin at pH 7.5
    • Tanford, C.; Bunville, L. G.; Nozaki, Y. The reversible transformation of β-lactoglobulin at pH 7.5. J. Am. Chem. Soc. 1959, 81, 4032-4036.
    • (1959) J. Am. Chem. Soc. , vol.81 , pp. 4032-4036
    • Tanford, C.1    Bunville, L.G.2    Nozaki, Y.3
  • 13
    • 0014198603 scopus 로고
    • Effect of pH on β-lactoglobulins
    • McKenzie, H. A.; Sawyer, W. H. Effect of pH on β-lactoglobulins. Nature 1967, 274, 1101-1104.
    • (1967) Nature , vol.274 , pp. 1101-1104
    • McKenzie, H.A.1    Sawyer, W.H.2
  • 15
    • 0029302371 scopus 로고
    • Interaction of β-Lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein: A review
    • Pérez, M. P.; Calvo, M. Interaction of β-Lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein: a review. J. Dairy Sci. 1995, 78, 978-988.
    • (1995) J. Dairy Sci. , vol.78 , pp. 978-988
    • Pérez, M.P.1    Calvo, M.2
  • 16
    • 12344317233 scopus 로고    scopus 로고
    • Structure des protéines solubles majeures
    • Lavoisier: Paris
    • Dufour, E. Structure des protéines solubles majeures. In Minéraux et produits laitiers; Lavoisier: Paris, 2004; pp 151-177.
    • (2004) Minéraux et Produits Laitiers , pp. 151-177
    • Dufour, E.1
  • 17
  • 18
    • 0023661017 scopus 로고
    • Crystal structure of the trigonal form of bovine β-lactoglobulin and its complex with retinol at 2.5 Å resolution
    • Monaco, H. L.; Zanotti, G.; Spadon, P.; Bolognesi, M.; Sawyer, L.; Eliopoulos, E. Crystal structure of the trigonal form of bovine β-lactoglobulin and its complex with retinol at 2.5 Å resolution. J. Mol. Biol. 1987, 197, 695-706.
    • (1987) J. Mol. Biol. , vol.197 , pp. 695-706
    • Monaco, H.L.1    Zanotti, G.2    Spadon, P.3    Bolognesi, M.4    Sawyer, L.5    Eliopoulos, E.6
  • 19
    • 0036037132 scopus 로고    scopus 로고
    • The ligand-binding site of bovine β-lactoglobulin: Evidence for a function
    • Kontopidis, G.; Holt, C.; Sawyer, L. The ligand-binding site of bovine β-lactoglobulin: evidence for a function. J. Mol. Biol. 2002, 318, 1043-1055.
    • (2002) J. Mol. Biol. , vol.318 , pp. 1043-1055
    • Kontopidis, G.1    Holt, C.2    Sawyer, L.3
  • 21
    • 0032839589 scopus 로고    scopus 로고
    • Effect of heat treatment on bovine β-lactoglobulin A, B, and C explored using thiol availability and fluorescence
    • Manderson, G. A.; Hardman, M. J.; Creamer, L. K. Effect of heat treatment on bovine β-lactoglobulin A, B, and C explored using thiol availability and fluorescence. J. Agric. Food Chem. 1999, 47, 3617-3627.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 3617-3627
    • Manderson, G.A.1    Hardman, M.J.2    Creamer, L.K.3
  • 22
    • 0001943903 scopus 로고    scopus 로고
    • Fluorescence spectroscopy in peptide and protein analysis
    • Meyers, R. A., Ed.; John Wiley & Sons Ltd.: Chichester, U.K.
    • Ladokhin, A. S. Fluorescence spectroscopy in peptide and protein analysis. In Encyclopedia of Analytical Chemistry; Meyers, R. A., Ed.; John Wiley & Sons Ltd.: Chichester, U.K., 2000; p 5762.
    • (2000) Encyclopedia of Analytical Chemistry , pp. 5762
    • Ladokhin, A.S.1
  • 23
    • 0032533554 scopus 로고    scopus 로고
    • Conformation of β-lactoglobulin at an oil/water interface as determined from proteolysis and spectroscopic methods
    • Dufour, E.; Dalgalarrondo, M.; Adam, L. Conformation of β-lactoglobulin at an oil/water interface as determined from proteolysis and spectroscopic methods. J. Colloid Interface Sci. 1998, 207, 264-272.
    • (1998) J. Colloid Interface Sci. , vol.207 , pp. 264-272
    • Dufour, E.1    Dalgalarrondo, M.2    Adam, L.3
  • 24
    • 0032004945 scopus 로고    scopus 로고
    • Effects of pH and salt environment on the association of β-lactoglobulin revealed by intrinsic fluorescence studies
    • Renard, D.; Lefebvre, J.; Griffin, M. C. A.; Griffin, W. G. Effects of pH and salt environment on the association of β-lactoglobulin revealed by intrinsic fluorescence studies. Int. J. Biol. Macromol. 1998, 22, 41-49.
    • (1998) Int. J. Biol. Macromol. , vol.22 , pp. 41-49
    • Renard, D.1    Lefebvre, J.2    Griffin, M.C.A.3    Griffin, W.G.4
  • 25
    • 0031160713 scopus 로고    scopus 로고
    • Binding of retinoids to β-lactoglobulin isolated by bioselective adsorption
    • Wang, Q.; Allen, J. C.; Swaisgood, H. E. Binding of retinoids to β-lactoglobulin isolated by bioselective adsorption. J. Dairy Sci. 1997, 80, 1047-1053.
    • (1997) J. Dairy Sci. , vol.80 , pp. 1047-1053
    • Wang, Q.1    Allen, J.C.2    Swaisgood, H.E.3
  • 26
    • 0031160714 scopus 로고    scopus 로고
    • Binding of Vitamin D and cholesterol to β-Lactoglobulin
    • Wang, Q.; Allen, J. C.; Swaisgood, H. E. Binding of Vitamin D and cholesterol to β-Lactoglobulin. J. Dairy Sci. 1997, 80, 1054-1059.
    • (1997) J. Dairy Sci. , vol.80 , pp. 1054-1059
    • Wang, Q.1    Allen, J.C.2    Swaisgood, H.E.3
  • 27
    • 0027089776 scopus 로고
    • A fluorescently labeled intestinal fatty acid binding protein. Interactions with fatty acids and its use in monitoring free fatty acids
    • Richieri, G. V.; Ogata, R. T.; Kleinfeld, A. M. A fluorescently labeled intestinal fatty acid binding protein. Interactions with fatty acids and its use in monitoring free fatty acids. J. Biol. Chem. 1992, 267, 23495-23501.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23495-23501
    • Richieri, G.V.1    Ogata, R.T.2    Kleinfeld, A.M.3
  • 28
    • 0031892161 scopus 로고    scopus 로고
    • Mapping fatty acid binding to {beta}-lactoglobulin: Ligand binding is restricted by modification of Cys 121
    • Narayan, M.; Berliner, L. Mapping fatty acid binding to {beta}-lactoglobulin: ligand binding is restricted by modification of Cys 121. J. Protein Sci. 1998, 7, 150-157.
    • (1998) J. Protein Sci. , vol.7 , pp. 150-157
    • Narayan, M.1    Berliner, L.2
  • 29
    • 0032483094 scopus 로고    scopus 로고
    • Retinol and retinoic acid bind to a surface cleft in bovine β-lactoglobulin: A method of binding site determination using fluorescence resonance energy transfer
    • Lange, D. C.; Kothari, R.; Patel, R. C.; Patel, S. C. Retinol and retinoic acid bind to a surface cleft in bovine β-lactoglobulin: a method of binding site determination using fluorescence resonance energy transfer. Biophys. Chem. 1998, 74, 45-51.
    • (1998) Biophys. Chem. , vol.74 , pp. 45-51
    • Lange, D.C.1    Kothari, R.2    Patel, R.C.3    Patel, S.C.4
  • 30
    • 33644596182 scopus 로고    scopus 로고
    • Thermodynamics of binding interactions between bovine β-lactoglobulin a and the antihypertensive peptide β-Lg f142-148
    • Roufik, S.; Gauthier, S. F.; Leng, X.; Turgeon, S. L. Thermodynamics of binding interactions between bovine β-lactoglobulin A and the antihypertensive peptide β-Lg f142-148. Biomacromolecules, 2006, 7, 419-426.
    • (2006) Biomacromolecules , vol.7 , pp. 419-426
    • Roufik, S.1    Gauthier, S.F.2    Leng, X.3    Turgeon, S.L.4
  • 31
    • 0033778182 scopus 로고    scopus 로고
    • New insight on beta-lactoglobulin binding sites by 1-anilinonaphthalene- 8-sulfonate fluorescence decay
    • Collini, M.; D'Alfonso, L.; Baldini, G. New insight on beta-lactoglobulin binding sites by 1-anilinonaphthalene- 8-sulfonate fluorescence decay. Protein Sci. 2000, 9, 1968-1974.
    • (2000) Protein Sci. , vol.9 , pp. 1968-1974
    • Collini, M.1    D'Alfonso, L.2    Baldini, G.3
  • 32
    • 0041341891 scopus 로고    scopus 로고
    • Competitive binding of fatty acids and the fluorescent probe 1-8-anilinonaphthalene sulfonate to bovine β-lactoglobulin
    • Collini, M.; D'Alfonso, L.; Molinari, H.; Ragona, L.; Catalano, M.; Baldini, G. Competitive binding of fatty acids and the fluorescent probe 1-8-anilinonaphthalene sulfonate to bovine β-lactoglobulin. Protein Sci. 2003, 12, 1596-1603.
    • (2003) Protein Sci. , vol.12 , pp. 1596-1603
    • Collini, M.1    D'Alfonso, L.2    Molinari, H.3    Ragona, L.4    Catalano, M.5    Baldini, G.6
  • 34
    • 21144474448 scopus 로고
    • Front-face fluorescence applied to structural studies of proteins and lipid-protein interactions of visco-elastic food products. 2. Application to wheat gluten
    • Genot, C.; Tonetti, F.; Montenay-Garestier, T.; Marion, D.; Drapon, R. Front-face fluorescence applied to structural studies of proteins and lipid-protein interactions of visco-elastic food products. 2. Application to wheat gluten. Sci. Aliments 1992, 12, 687-704.
    • (1992) Sci. Aliments , vol.12 , pp. 687-704
    • Genot, C.1    Tonetti, F.2    Montenay-Garestier, T.3    Marion, D.4    Drapon, R.5
  • 35
    • 0018411264 scopus 로고
    • Front-face fluorometry of liquid samples
    • Eisinger, J.; Flores, J. Front-face fluorometry of liquid samples. Anal. Biochem. 1979, 94, 15-21.
    • (1979) Anal. Biochem. , vol.94 , pp. 15-21
    • Eisinger, J.1    Flores, J.2
  • 36
    • 0018909387 scopus 로고
    • Hemoglobin determined in 15 μL of whole blood by "front- face" fluorometry
    • Blumberg, W. E.; Doleiden, F. H.; Lamola, A. A. Hemoglobin determined in 15 μL of whole blood by "front-face" fluorometry. Clin. Chem. 1980, 26, 409-413.
    • (1980) Clin. Chem. , vol.26 , pp. 409-413
    • Blumberg, W.E.1    Doleiden, F.H.2    Lamola, A.A.3
  • 37
    • 0022399784 scopus 로고
    • Intrinsic fluorometric determination of the stable state of aggregation in hemoglobins
    • Hirsch, R. E.; San George, R. C.; Nagel, R. L. Intrinsic fluorometric determination of the stable state of aggregation in hemoglobins. Anal. Biochem. 1985, 149, 415-420.
    • (1985) Anal. Biochem. , vol.149 , pp. 415-420
    • Hirsch, R.E.1    San George, R.C.2    Nagel, R.L.3
  • 38
    • 0024499001 scopus 로고
    • Stopped-flow front-face fluorometer: A prototype design to measure hemoglobin R → T transition kinetics
    • Hirsch, R. E.; Nagel, R. L. Stopped-flow front-face fluorometer: a prototype design to measure hemoglobin R → T transition kinetics. Anal. Biochem. 1989, 176, 19-21.
    • (1989) Anal. Biochem. , vol.176 , pp. 19-21
    • Hirsch, R.E.1    Nagel, R.L.2
  • 39
    • 0041349500 scopus 로고    scopus 로고
    • Fluorescence spectroscopy investigation of acid- or rennet-induced coagulation of milk
    • Herbert, T.; Riaublanc, A.; Bouchet, B.; Gallant, D. J.; Dufour, E. Fluorescence spectroscopy investigation of acid- or rennet-induced coagulation of milk. J. Dairy Sci. 1999, 82, 2056-2062.
    • (1999) J. Dairy Sci. , vol.82 , pp. 2056-2062
    • Herbert, T.1    Riaublanc, A.2    Bouchet, B.3    Gallant, D.J.4    Dufour, E.5
  • 40
    • 0039424037 scopus 로고    scopus 로고
    • Monitoring the identity and the structure of soft cheeses by fluorescence spectroscopy
    • Herbert, S.; Riou, N. M.; Devaux, M. F.; Riaublanc, A.; Bouchet, . B.; Gallant, D. J.; Dufour, E. Monitoring the identity and the structure of soft cheeses by fluorescence spectroscopy. Lait 2000, 80, 621-634.
    • (2000) Lait , vol.80 , pp. 621-634
    • Herbert, S.1    Riou, N.M.2    Devaux, M.F.3    Riaublanc, A.4    Bouchet, B.5    Gallant, D.J.6    Dufour, E.7
  • 41
    • 0038661140 scopus 로고    scopus 로고
    • Fluorescence spectroscopy: A tool for the investigation of cheese melting-correlation with rheological characteristics
    • Karoui, R.; Laguet, A.; Dufour, E. Fluorescence spectroscopy: a tool for the investigation of cheese melting-correlation with rheological characteristics. Lait 2003, 83, 251-264.
    • (2003) Lait , vol.83 , pp. 251-264
    • Karoui, R.1    Laguet, A.2    Dufour, E.3
  • 42
    • 0037462069 scopus 로고    scopus 로고
    • Front-face fluorescence spectroscopy study of globular proteins in emulsions: Displacement of BSA by a nonionic surfactant
    • Rampon, V.; Genot, C.; Riaublanc, A.; Anton, M.; Axelos, M. A. V.; McClements, D. J. Front-face fluorescence spectroscopy study of globular proteins in emulsions: displacement of BSA by a nonionic surfactant. J. Agric. Food Chem. 2003, 51, 2482-2489.
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 2482-2489
    • Rampon, V.1    Genot, C.2    Riaublanc, A.3    Anton, M.4    Axelos, M.A.V.5    McClements, D.J.6
  • 43
    • 0037462051 scopus 로고    scopus 로고
    • Front-face fluorescence spectroscopy study of globular proteins in emulsions: Influence of droplet flocculation
    • Rampon, V.; Genot, C.; Riaublanc, A.; Anton, M.; Axelos, M. A.; McClements, D. J. Front-face fluorescence spectroscopy study of globular proteins in emulsions: influence of droplet flocculation. J. Agric. Food Chem. 2003, 51, 2490-2495.
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 2490-2495
    • Rampon, V.1    Genot, C.2    Riaublanc, A.3    Anton, M.4    Axelos, M.A.5    McClements, D.J.6
  • 44
    • 13244252287 scopus 로고    scopus 로고
    • Front-face fluorescence spectroscopy allows the characterization of mild heat treatments applied to milk. Relations with the denaturation of milk proteins
    • Kulmyrzaev, A. A.; Levieux, D.; Dufour, E. Front-face fluorescence spectroscopy allows the characterization of mild heat treatments applied to milk. Relations with the denaturation of milk proteins. J. Agric. Food Chem. 2005, 53, 502-507.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 502-507
    • Kulmyrzaev, A.A.1    Levieux, D.2    Dufour, E.3
  • 45
    • 21344454877 scopus 로고    scopus 로고
    • Direct quantification of protein partitioning in oil-in-water emulsion by front-face fluorescence: Avoiding the need for centrifugation
    • Granger, C.; Barey, P.; Toutain, J.; Cansell, M. Direct quantification of protein partitioning in oil-in-water emulsion by front-face fluorescence: avoiding the need for centrifugation. Colloids Surf., B 2005, 43, 158-162.
    • (2005) Colloids Surf., B , vol.43 , pp. 158-162
    • Granger, C.1    Barey, P.2    Toutain, J.3    Cansell, M.4
  • 46
    • 30744435393 scopus 로고    scopus 로고
    • Mapping of ice cream formulation using front-face fluorescence spectroscopy
    • Granger, C.; Da Costa, J. P.; Toutain, J.; Barey, P.; Cansell, M. Mapping of ice cream formulation using front-face fluorescence spectroscopy. Int. Dairy J. 2006, 16, 489-496.
    • (2006) Int. Dairy J. , vol.16 , pp. 489-496
    • Granger, C.1    Da Costa, J.P.2    Toutain, J.3    Barey, P.4    Cansell, M.5
  • 47
    • 0000538001 scopus 로고
    • Front-face fluorescence applied to structural studies of proteins and lipid-protein interactions of visco-elastic food products. 1-Designing of front-face adaptor and validity of front-face fluorescence measurements
    • Genot, C.; Tonetti, F.; Montenay-Garestier, T.; Drapon, R. Front-face fluorescence applied to structural studies of proteins and lipid-protein interactions of visco-elastic food products. 1-Designing of front-face adaptor and validity of front-face fluorescence measurements. Sci. Aliments 1992, 12, 199-212.
    • (1992) Sci. Aliments , vol.12 , pp. 199-212
    • Genot, C.1    Tonetti, F.2    Montenay-Garestier, T.3    Drapon, R.4
  • 49
    • 0014117822 scopus 로고
    • On the average hydrophobicity of proteins and the relation between it and protein structure
    • Bigelow, C. C. On the average hydrophobicity of proteins and the relation between it and protein structure. J. Theor. Biol. 1967, 16, 187-211.
    • (1967) J. Theor. Biol. , vol.16 , pp. 187-211
    • Bigelow, C.C.1
  • 51
    • 0025784171 scopus 로고
    • Binding of retinoids and β-carotene to β-lactoglobulin. Influence of protein modifications
    • Dufour, E.; Haertlé, T. Binding of retinoids and β-carotene to β-lactoglobulin. Influence of protein modifications. Biochim. Biophys. Acta 1991, 1079, 316-320.
    • (1991) Biochim. Biophys. Acta , vol.1079 , pp. 316-320
    • Dufour, E.1    Haertlé, T.2
  • 52
    • 0027522088 scopus 로고
    • Probing the fatty acid binding site of beta-lactoglobulins
    • Frapin, D.; Dufour, E.; Haertlé, T. Probing the fatty acid binding site of beta-lactoglobulins. J. Protein Chem. 1993, 12, 443-449.
    • (1993) J. Protein Chem. , vol.12 , pp. 443-449
    • Frapin, D.1    Dufour, E.2    Haertlé, T.3
  • 53
    • 0019331472 scopus 로고
    • Spectroscopic characterization of β-lactoglobulin-retinol complex
    • Fugate, R. D.; Song, P.-S. Spectroscopic characterization of β-lactoglobulin-retinol complex. Biochim. Biophys. Acta 1980, 625, 28-42.
    • (1980) Biochim. Biophys. Acta , vol.625 , pp. 28-42
    • Fugate, R.D.1    Song, P.-S.2
  • 54
    • 0031738305 scopus 로고    scopus 로고
    • 12-Bromododecanoic acid binds inside the calyx of bovine β-lactoglobulin
    • Qin, B. Y.; Creamer, L. K.; Baker, E. N.; Jameson, G. B. 12-Bromododecanoic acid binds inside the calyx of bovine β-lactoglobulin. FEBS Lett. 1998, 438, 272-278.
    • (1998) FEBS Lett. , vol.438 , pp. 272-278
    • Qin, B.Y.1    Creamer, L.K.2    Baker, E.N.3    Jameson, G.B.4
  • 55
    • 0032516433 scopus 로고    scopus 로고
    • Towards understanding tryptophan fluorescence in proteins
    • Chen, Y.; Berkley, M. D. Towards understanding tryptophan fluorescence in proteins. Biochemistry 1998, 37, 9976-9982.
    • (1998) Biochemistry , vol.37 , pp. 9976-9982
    • Chen, Y.1    Berkley, M.D.2
  • 56
    • 0031035893 scopus 로고    scopus 로고
    • Fatty acids and retinoids bind independently and simultaneously to β-lactoglobulin
    • Narayan, M.; Berliner, L. J. Fatty acids and retinoids bind independently and simultaneously to β-lactoglobulin. Biochemistry 1997, 36, 1906-1911.
    • (1997) Biochemistry , vol.36 , pp. 1906-1911
    • Narayan, M.1    Berliner, L.J.2
  • 57
    • 0025609431 scopus 로고
    • β-lactoglobulin binds retinol and protoporphyrin K at two different binding sites
    • Dufour, E.; Marden, M. C.; Haertlé, T. β-lactoglobulin binds retinol and protoporphyrin K at two different binding sites. FEBS Lett. 1990, 277, 223-226.
    • (1990) FEBS Lett. , vol.277 , pp. 223-226
    • Dufour, E.1    Marden, M.C.2    Haertlé, T.3
  • 58
    • 0001510699 scopus 로고
    • Binding affinities of β-ionone and related flavor compounds to β-lactoglobulin: Effects of chemical modifications
    • Dufour, E.; Haertlé, T. Binding affinities of β-ionone and related flavor compounds to β-lactoglobulin: Effects of chemical modifications. J. Agric. Food Chem. 1990, 38, 1691-1695.
    • (1990) J. Agric. Food Chem. , vol.38 , pp. 1691-1695
    • Dufour, E.1    Haertlé, T.2
  • 59
    • 0037070357 scopus 로고    scopus 로고
    • Interactions between bovine β-lactoglobulin and peptides under different physicochemical conditions
    • Noiseux, I.; Gauthier, S. F.; Turgeon, S. L. Interactions between bovine β-lactoglobulin and peptides under different physicochemical conditions. J. Agric. Food Chem. 2002, 50, 1587-1592.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 1587-1592
    • Noiseux, I.1    Gauthier, S.F.2    Turgeon, S.L.3
  • 60
    • 30344441808 scopus 로고    scopus 로고
    • In vitro digestibility of bioactive peptides derived from bovine β-lactoglobulin
    • Roufik, S.; Gauthier, S. F.; Turgeon, S. L. In vitro digestibility of bioactive peptides derived from bovine β-lactoglobulin. Int. Dairy J. 2006, 16, 294-302.
    • (2006) Int. Dairy J. , vol.16 , pp. 294-302
    • Roufik, S.1    Gauthier, S.F.2    Turgeon, S.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.