Identification of a β-lactoglobulin lactosylation site (375 views)
Biochim Biophys Acta Protein Struct Mol Enzymol (ISSN: 0167-4838), 1998 Nov 10; 1388(2): 295-304.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 1.687, 5-year impact factor: 0
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0032506267&partnerID=40&md5=239f7289fb31abd3dd1cdaaafb62f264
Keywords: β-Lactoglobulin, Amadori Compound, Glycosylation, Lactosylation, Liquid Chromatography-Mass Spectrometry, Maillard Reaction, Milk, Thermal Treatment, Beta Lactoglobulin, Lysine, Organic Solvent, Trypsin, Amino Acid Sequence, Article, Glycation, Heating, Ligand Binding, Molecular Model, Priority Journal, Protein Structure, Binding Sites, High Pressure Liquid, Milk Proteins, Molecular Sequence Data, Peptide Fragments,
Affiliations:
Dipto. di Scienza degli Alimenti, Univ. Napoli 'Federico II', Parco G., 80055 Portici, Naples, Italy
CRISCEB-Ctro. Ric. I., Seconda Univ. Napoli, Via C., 80138 Naples, Italy
References:
Papiz, M.Z., Sawyer, L., Eliopoulos, E.E., North, A.C.T., Findlay, J.B.C., Sivapradasarao, R., Jones, T.A., Kraulis, P.J., (1986) Nature, 324, pp. 383-38
De Wit, J.N., Klarenbeek, K., (1984) J. Dairy Sci., 67, pp. 207-2710
Lapanje, S., Poklar, N., (1989) Biophys. Chem., 34, pp. 155-161
Casal, H., Kohler, U., Mantsh, H.N., (1988) Biochim. Biophys. Acta, 957, pp. 11-20
Anema, S., McKenna, A., (1996) J. Agric. Food Chem., 44, pp. 422-428
Jang, H.D., Swaisgood, H.E., (1990) Arch. Biochem. Biophys., 283, pp. 318-328
Finot, P.A., Deutch, R., Bujard, E., (1981) In: Maillard Reaction in Food, pp. 345-355. , Pergamon Press, Oxford
Harding, J.J., (1985) Adv. Protein Chem., 37, pp. 247-334
Friedman, M., (1996) The Maillard Reaction: Consequences for the Chemical and Life Science, pp. 129-147. , in: R. Ikan (Ed.), John Wiley and Sons, New York
Resmini, P., Pellegrino, L., Batteli, G., (1990) Ital. J. Food Sci., 3, pp. 173-183
Finot, P.A., Bricout, J., Viani, R., Mauron, J., (1968) Experientia, 25, pp. 134-135
Nakayama, H., Teneda, S., Mitsuhashi, T., Kuwajima, S., Aoki, S., Kuroda, Y., Misawa, K., Nakagawa, S., (1991) J. Immunol. Methods, 140, pp. 119-125
Matsuda, T., Ishiguro, H., Ohkubo, I., Sasaki, M., Nakamura, R., (1992) J. Biochem., 111, pp. 383-387
Fogliano, V., Monti, S.M., Ritieni, A., Marchisano, C., Peluso, G., Randazzo, G., (1997) Food Chem., 58, pp. 53-58
Matsuda, T., Kato, Y., Watanabe, K., Nakamura, R., (1985) J. Agric. Food Chem., 33, pp. 1193-1196
Kitabatake, N., Cuq, J.L., Cheftel, J.C., (1985) J. Agric. Food Chem., 33, pp. 125-130
Hattori, M., Ogino, A., Nakai, H., Takahashi, K., (1997) J. Agric. Food Chem., 45, pp. 703-708
Morgan, F., Leonil, J., Mollé, D., Bauhallab, S., (1997) Biochem. Biophys. Res. Commun., 236, pp. 413-417
Aschaffenburg, R., Dewry, J., (1959) 15th Int. Dairy Congr. Lond., 3, pp. 1631-1637
Laemmli, U.K., (1970) Nature, 227, pp. 680-685
Bernstein, F.C., Koetzle, T.F., Williams, G.J.B., Meyer, E.F., Brice, M.D., Rodgers, J.R., Kennard, O., Tasumi, M., (1977) J. Mol. Biol., 112, pp. 535-542
Hubbard, S.J., Campbell, S.F., Thornton, J.M., (1991) J. Mol. Biol., 220, pp. 507-530
Iberg, N., Fluckiger, R., (1986) J. Biol. Chem., 29, pp. 13542-13545
Brownlow, S., Morais-Chabral, J.H., Cooper, R., Flower, D.R., Yewdall, S.J., Polikarpov, I., North, A.T.C., Sawyer, L., (1997) Structure, 5, pp. 481-495
Papiz, M. Z., Sawyer, L., Eliopoulos, E. E., North, A. C. T., Findlay, J. B. C., Sivapradasarao, R., Jones, T. A., Kraulis, P. J., (1986) Nature, 324, pp. 383-38
De Wit, J. N., Klarenbeek, K., (1984) J. Dairy Sci., 67, pp. 207-2710
Jang, H. D., Swaisgood, H. E., (1990) Arch. Biochem. Biophys., 283, pp. 318-328
Finot, P. A., Deutch, R., Bujard, E., (1981) In: Maillard Reaction in Food, pp. 345-355. , Pergamon Press, Oxford
Harding, J. J., (1985) Adv. Protein Chem., 37, pp. 247-334
Finot, P. A., Bricout, J., Viani, R., Mauron, J., (1968) Experientia, 25, pp. 134-135
Laemmli, U. K., (1970) Nature, 227, pp. 680-685
Bernstein, F. C., Koetzle, T. F., Williams, G. J. B., Meyer, E. F., Brice, M. D., Rodgers, J. R., Kennard, O., Tasumi, M., (1977) J. Mol. Biol., 112, pp. 535-542
Hubbard, S. J., Campbell, S. F., Thornton, J. M., (1991) J. Mol. Biol., 220, pp. 507-530
Biochim Biophys Acta Protein Struct Mol Enzymol (ISSN: 0167-4838), 1998 Nov 10; 1388(2): 295-304.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 1.687, 5-year impact factor: 0
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0032506267&partnerID=40&md5=239f7289fb31abd3dd1cdaaafb62f264
Keywords: β-Lactoglobulin, Amadori Compound, Glycosylation, Lactosylation, Liquid Chromatography-Mass Spectrometry, Maillard Reaction, Milk, Thermal Treatment, Beta Lactoglobulin, Lysine, Organic Solvent, Trypsin, Amino Acid Sequence, Article, Glycation, Heating, Ligand Binding, Molecular Model, Priority Journal, Protein Structure, Binding Sites, High Pressure Liquid, Milk Proteins, Molecular Sequence Data, Peptide Fragments,
Affiliations:
Dipto. di Scienza degli Alimenti, Univ. Napoli 'Federico II', Parco G., 80055 Portici, Naples, Italy
CRISCEB-Ctro. Ric. I., Seconda Univ. Napoli, Via C., 80138 Naples, Italy
References:
Papiz, M.Z., Sawyer, L., Eliopoulos, E.E., North, A.C.T., Findlay, J.B.C., Sivapradasarao, R., Jones, T.A., Kraulis, P.J., (1986) Nature, 324, pp. 383-38
De Wit, J.N., Klarenbeek, K., (1984) J. Dairy Sci., 67, pp. 207-2710
Lapanje, S., Poklar, N., (1989) Biophys. Chem., 34, pp. 155-161
Casal, H., Kohler, U., Mantsh, H.N., (1988) Biochim. Biophys. Acta, 957, pp. 11-20
Anema, S., McKenna, A., (1996) J. Agric. Food Chem., 44, pp. 422-428
Jang, H.D., Swaisgood, H.E., (1990) Arch. Biochem. Biophys., 283, pp. 318-328
Finot, P.A., Deutch, R., Bujard, E., (1981) In: Maillard Reaction in Food, pp. 345-355. , Pergamon Press, Oxford
Harding, J.J., (1985) Adv. Protein Chem., 37, pp. 247-334
Friedman, M., (1996) The Maillard Reaction: Consequences for the Chemical and Life Science, pp. 129-147. , in: R. Ikan (Ed.), John Wiley and Sons, New York
Resmini, P., Pellegrino, L., Batteli, G., (1990) Ital. J. Food Sci., 3, pp. 173-183
Finot, P.A., Bricout, J., Viani, R., Mauron, J., (1968) Experientia, 25, pp. 134-135
Nakayama, H., Teneda, S., Mitsuhashi, T., Kuwajima, S., Aoki, S., Kuroda, Y., Misawa, K., Nakagawa, S., (1991) J. Immunol. Methods, 140, pp. 119-125
Matsuda, T., Ishiguro, H., Ohkubo, I., Sasaki, M., Nakamura, R., (1992) J. Biochem., 111, pp. 383-387
Fogliano, V., Monti, S.M., Ritieni, A., Marchisano, C., Peluso, G., Randazzo, G., (1997) Food Chem., 58, pp. 53-58
Matsuda, T., Kato, Y., Watanabe, K., Nakamura, R., (1985) J. Agric. Food Chem., 33, pp. 1193-1196
Kitabatake, N., Cuq, J.L., Cheftel, J.C., (1985) J. Agric. Food Chem., 33, pp. 125-130
Hattori, M., Ogino, A., Nakai, H., Takahashi, K., (1997) J. Agric. Food Chem., 45, pp. 703-708
Morgan, F., Leonil, J., Mollé, D., Bauhallab, S., (1997) Biochem. Biophys. Res. Commun., 236, pp. 413-417
Aschaffenburg, R., Dewry, J., (1959) 15th Int. Dairy Congr. Lond., 3, pp. 1631-1637
Laemmli, U.K., (1970) Nature, 227, pp. 680-685
Bernstein, F.C., Koetzle, T.F., Williams, G.J.B., Meyer, E.F., Brice, M.D., Rodgers, J.R., Kennard, O., Tasumi, M., (1977) J. Mol. Biol., 112, pp. 535-542
Hubbard, S.J., Campbell, S.F., Thornton, J.M., (1991) J. Mol. Biol., 220, pp. 507-530
Iberg, N., Fluckiger, R., (1986) J. Biol. Chem., 29, pp. 13542-13545
Brownlow, S., Morais-Chabral, J.H., Cooper, R., Flower, D.R., Yewdall, S.J., Polikarpov, I., North, A.T.C., Sawyer, L., (1997) Structure, 5, pp. 481-495
Papiz, M. Z., Sawyer, L., Eliopoulos, E. E., North, A. C. T., Findlay, J. B. C., Sivapradasarao, R., Jones, T. A., Kraulis, P. J., (1986) Nature, 324, pp. 383-38
De Wit, J. N., Klarenbeek, K., (1984) J. Dairy Sci., 67, pp. 207-2710
Jang, H. D., Swaisgood, H. E., (1990) Arch. Biochem. Biophys., 283, pp. 318-328
Finot, P. A., Deutch, R., Bujard, E., (1981) In: Maillard Reaction in Food, pp. 345-355. , Pergamon Press, Oxford
Harding, J. J., (1985) Adv. Protein Chem., 37, pp. 247-334
Finot, P. A., Bricout, J., Viani, R., Mauron, J., (1968) Experientia, 25, pp. 134-135
Laemmli, U. K., (1970) Nature, 227, pp. 680-685
Bernstein, F. C., Koetzle, T. F., Williams, G. J. B., Meyer, E. F., Brice, M. D., Rodgers, J. R., Kennard, O., Tasumi, M., (1977) J. Mol. Biol., 112, pp. 535-542
Hubbard, S. J., Campbell, S. F., Thornton, J. M., (1991) J. Mol. Biol., 220, pp. 507-530
Identification of a β-lactoglobulin lactosylation site
Thermal treatment of milk leads to non-enzymatic glycosylation of proteins through Maillard reaction. Free NH2 groups of basic amino acids react with the reducing carbonyl group of lactose forming the so-called Amadori products. Electrospray mass spectrometry analysis shows that β-lactoglobulin (β-LG), the major whey protein, undergoes lactosylation under industrial thermal treatment. In order to investigate the specificity of reactive sites for lactose binding the analysis of trypsin hydrolysates of β-LG isolated from different industrial milks was performed. Results demonstrate that Lys-100 is a preferential lactosylation site of β-LG during industrial milk treatment. These results were confirmed by an analysis of the three-dimensional model of the protein which showed that Lys-100 had the highest solvent accessibility and proximity to another amino group making Lys-100 the best candidate to lactosylation. Lys-47, previously identified by other authors, showed a good proximity to another Lys residue, but an intermediate level of exposition to solvent. Copyright (C) 1998 Elsevier Science B.V.
Thermal treatment of milk leads to non-enzymatic glycosylation of proteins through Maillard reaction. Free NH2 groups of basic amino acids react with the reducing carbonyl group of lactose forming the so-called Amadori products. Electrospray mass spectrometry analysis shows that β-lactoglobulin (β-LG), the major whey protein, undergoes lactosylation under industrial thermal treatment. In order to investigate the specificity of reactive sites for lactose binding the analysis of trypsin hydrolysates of β-LG isolated from different industrial milks was performed. Results demonstrate that Lys-100 is a preferential lactosylation site of β-LG during industrial milk treatment. These results were confirmed by an analysis of the three-dimensional model of the protein which showed that Lys-100 had the highest solvent accessibility and proximity to another amino group making Lys-100 the best candidate to lactosylation. Lys-47, previously identified by other authors, showed a good proximity to another Lys residue, but an intermediate level of exposition to solvent. Copyright (C) 1998 Elsevier Science B.V.
Identification of a β-lactoglobulin lactosylation site
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Identification of a β-lactoglobulin lactosylation site
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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17 Records (17 excluding Abstracts).
Total impact factor: 56.755 (56.755 excluding Abstracts).
Total 5 year impact factor: 60.612 (60.612 excluding Abstracts).
Total impact factor: 56.755 (56.755 excluding Abstracts).
Total 5 year impact factor: 60.612 (60.612 excluding Abstracts).
375 views. Last view on Friday 17 February 2023, 1:04:38
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