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Volumn 34, Issue 5-6, 1999, Pages 429-435

Glycation of bovine β-lactoglobulin: Effect on the protein structure

Author keywords

Binding sites; Conformation; Denaturation; Glycation; Lactose; Lactoglobulin

Indexed keywords

BOVINAE;

EID: 0001296410     PISSN: 09505423     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2621.1999.00318.x     Document Type: Article
Times cited : (71)

References (28)
  • 3
    • 0000138954 scopus 로고    scopus 로고
    • Evidence of multiple glycosylation of bovine β-lactoglobulin by electrospray ionisation mass spectrometry
    • Burr, R., Moore, C.H. & Hill, J.P. (1996). Evidence of multiple glycosylation of bovine β-Lactoglobulin by electrospray ionisation mass spectrometry. Milchwissenschaft, 51, 488-492.
    • (1996) Milchwissenschaft , vol.51 , pp. 488-492
    • Burr, R.1    Moore, C.H.2    Hill, J.P.3
  • 5
  • 9
    • 0000008542 scopus 로고    scopus 로고
    • Heat-induced aggregation of β-lactoglobulin: Role of the free thiol group and disulfide bonds
    • Hoffmann, M.A.M. & Van Mil, P.J.J.M. (1997). Heat-induced aggregation of β-Lactoglobulin: role of the free thiol group and disulfide bonds. Journal of Agricultural and Food Chemistry, 45, 2942-2948.
    • (1997) Journal of Agricultural and Food Chemistry , vol.45 , pp. 2942-2948
    • Hoffmann, M.A.M.1    Van Mil, P.J.J.M.2
  • 10
    • 0002284922 scopus 로고
    • Modifications of high-order structures upon heating of β-Lactoglobulin: Dependence of the protein concentration
    • Iametti, S., Cairoli, S., DeGregori, B. & Bonomi, F. (1995). Modifications of high-order structures upon heating of β-Lactoglobulin: dependence of the protein concentration. Journal of Agricultural and Food Chemistry, 43, 53-58.
    • (1995) Journal of Agricultural and Food Chemistry , vol.43 , pp. 53-58
    • Iametti, S.1    Cairoli, S.2    Degregori, B.3    Bonomi, F.4
  • 11
    • 0029924648 scopus 로고    scopus 로고
    • Modifications occur at different structural levels during the heat denaturation of β-lactoglobulin
    • Iametti, S., De Gregori, B., Vecchio, G. & Bonomi, F. (1996). Modifications occur at different structural levels during the heat denaturation of β-Lactoglobulin. European Journal of Biochemistry, 237, 106-112.
    • (1996) European Journal of Biochemistry , vol.237 , pp. 106-112
    • Iametti, S.1    De Gregori, B.2    Vecchio, G.3    Bonomi, F.4
  • 12
    • 0014469268 scopus 로고
    • Determination of available lysine in proteins
    • Kakade, M.L. & Liener, I.E. (1969). Determination of available lysine in proteins. Analytical Biochemistry, 27, 273-280.
    • (1969) Analytical Biochemistry , vol.27 , pp. 273-280
    • Kakade, M.L.1    Liener, I.E.2
  • 13
    • 0023765564 scopus 로고
    • Enhanced thermodynamic stability of β-lactoglobulin at low pH
    • Kella, N.K.D. & Kinsella, J.E. (1988). Enhanced thermodynamic stability of β-Lactoglobulin at low pH. Biochemical Journal, 255, 113-118.
    • (1988) Biochemical Journal , vol.255 , pp. 113-118
    • Kella, N.K.D.1    Kinsella, J.E.2
  • 14
    • 0031253029 scopus 로고    scopus 로고
    • Characterization by ionization mass spectrometry of lactosyl-β-lactoglobulin conjugates formed during heat treatment of milk and whey and identification of one lactose binding site
    • Léonil, J., Mollé, D., Fauquant, J., Maubois, J.-L., Pearce, R.J. & Bouhallab, S. (1997). Characterization by ionization mass spectrometry of lactosyl-β-Lactoglobulin conjugates formed during heat treatment of milk and whey and identification of one lactose binding site. Journal of Dairy Science, 80, 2270-2281.
    • (1997) Journal of Dairy Science , vol.80 , pp. 2270-2281
    • Léonil, J.1    Mollé, D.2    Fauquant, J.3    Maubois, J.-L.4    Pearce, R.J.5    Bouhallab, S.6
  • 15
    • 24544447317 scopus 로고
    • Heat-induced gel formation of β-lactoglobulin: A study on the secondary and tertiary structure as followed by circular dichroism spectroscopy
    • Matsuura, J.E. & Manning, M.C. (1994). Heat-induced gel formation of β-Lactoglobulin: a study on the secondary and tertiary structure as followed by circular dichroism spectroscopy. Journal of Agricultural and Food Chemistry, 42, 1650-1656.
    • (1994) Journal of Agricultural and Food Chemistry , vol.42 , pp. 1650-1656
    • Matsuura, J.E.1    Manning, M.C.2
  • 17
    • 0000443256 scopus 로고
    • Structural and conformational basis of the resistance of β-Lactoglobulin to peptic and chymotryptic digestion
    • Mohan Reddy, I., Kella, N.K.D. & Kinsella, J.E. (1988). Structural and conformational basis of the resistance of β-Lactoglobulin to peptic and chymotryptic digestion. Journal of Agricultural and Food Chemistry, 36, 737-741.
    • (1988) Journal of Agricultural and Food Chemistry , vol.36 , pp. 737-741
    • Mohan Reddy, I.1    Kella, N.K.D.2    Kinsella, J.E.3
  • 18
    • 0032524087 scopus 로고    scopus 로고
    • Selective detection of lactolated peptides in hydrolysates by liquid chromatography/electrospray tandem mass spectrometry
    • Mollé, D., Morgan, F., Bouhallab, S. & Léonil, J. (1998). Selective detection of lactolated peptides in hydrolysates by liquid chromatography/electrospray tandem mass spectrometry. Analytical Biochemistry, 259, 152-161.
    • (1998) Analytical Biochemistry , vol.259 , pp. 152-161
    • Mollé, D.1    Morgan, F.2    Bouhallab, S.3    Léonil, J.4
  • 20
    • 0031577271 scopus 로고    scopus 로고
    • Non enzymatic lactosylation of bovine β-Lactoglobulin under mild heat treatment leads to structural heterogeneity of the glycoforms
    • Morgan, F., Léonil, J., Mollé, D. & Bouhallab, S. (1997). Non enzymatic lactosylation of bovine β-Lactoglobulin under mild heat treatment leads to structural heterogeneity of the glycoforms. Biochemical and Biophysical Research Communication, 236, 413-417.
    • (1997) Biochemical and Biophysical Research Communication , vol.236 , pp. 413-417
    • Morgan, F.1    Léonil, J.2    Mollé, D.3    Bouhallab, S.4
  • 21
    • 0345059266 scopus 로고    scopus 로고
    • Modification of bovine β-Lactoglobulin by glycation in a powdered state or in an aqueous solution: Effect on association behavior and protein conformation
    • Morgan, F., Léonil, J., Mollé, D. & Bouhallab, S. (1999a). Modification of bovine β-Lactoglobulin by glycation in a powdered state or in an aqueous solution: effect on association behavior and protein conformation. Journal of Agricultural and Food Chemistry, 47, 83-91.
    • (1999) Journal of Agricultural and Food Chemistry , vol.47 , pp. 83-91
    • Morgan, F.1    Léonil, J.2    Mollé, D.3    Bouhallab, S.4
  • 23
    • 0002256616 scopus 로고
    • Heat-induced changes in lactose: Isomerization, degradation, Maillard browning
    • edited by P. F. Fox. Brussels: IDF
    • O'Brien, J. (1995). Heat-induced changes in lactose: isomerization, degradation, Maillard browning. In: Heat-Induced Changes in Milk, 2nd edn (edited by P. F. Fox). Pp. 134-170. Brussels: IDF.
    • (1995) Heat-induced Changes in Milk, 2nd Edn , pp. 134-170
    • O'Brien, J.1
  • 24
    • 0000008540 scopus 로고    scopus 로고
    • Thermal unfolding of β-Lactoglobulin: Characterization of initial unfolding events responsible for heat-induced aggregation
    • Prabakaran, S. & Damodaran, S. (1997). Thermal unfolding of β-Lactoglobulin: characterization of initial unfolding events responsible for heat-induced aggregation. Journal of Agricultural and Food Chemistry, 45, 4303-4308.
    • (1997) Journal of Agricultural and Food Chemistry , vol.45 , pp. 4303-4308
    • Prabakaran, S.1    Damodaran, S.2
  • 25
    • 0028985708 scopus 로고
    • Thermal denaturation of β-Lactoglobulin: Effect of protein concentration at pH 6.75 and 8.05
    • Qi, X.L., Brownlow, S., Holt, C. & Sellers, P. (1995). Thermal denaturation of β-Lactoglobulin: effect of protein concentration at pH 6.75 and 8.05. Biochimica et Biophysica Acta, 1248, 43-49.
    • (1995) Biochimica et Biophysica Acta , vol.1248 , pp. 43-49
    • Qi, X.L.1    Brownlow, S.2    Holt, C.3    Sellers, P.4
  • 26
    • 0030993642 scopus 로고    scopus 로고
    • Effect of temperature on the secondary structure of β-Lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: A test of the molten globule hypothesis
    • Qi, X.L., Holt, C., McNulty, D., Clarke, D.T., Brownlow, S. & Jones, G.R. (1997). Effect of temperature on the secondary structure of β-Lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis. Biochemical Journal, 324, 341-346.
    • (1997) Biochemical Journal , vol.324 , pp. 341-346
    • Qi, X.L.1    Holt, C.2    McNulty, D.3    Clarke, D.T.4    Brownlow, S.5    Jones, G.R.6
  • 27
    • 0028567981 scopus 로고
    • A model for the denaturation and aggregation of β-Lactoglobulin
    • Roefs, S.P.F.M. & de Kruif, C.G. (1994). A model for the denaturation and aggregation of β-Lactoglobulin. European Journal of Biochemistry, 226, 883-889.
    • (1994) European Journal of Biochemistry , vol.226 , pp. 883-889
    • Roefs, S.P.F.M.1    De Kruif, C.G.2
  • 28
    • 0031227534 scopus 로고    scopus 로고
    • Production and epitopic characterization of monoclonal antibodies against bovine β-lactoglobulin
    • Vénien, A., Levieux, D., Astier, C., Briand, L., Chobert, J.-M. & Haertlé, T. (1997). Production and epitopic characterization of monoclonal antibodies against bovine β-Lactoglobulin. Journal of Dairy Science, 80, 1977-1987.
    • (1997) Journal of Dairy Science , vol.80 , pp. 1977-1987
    • Vénien, A.1    Levieux, D.2    Astier, C.3    Briand, L.4    Chobert, J.-M.5    Haertlé, T.6


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