메뉴 건너뛰기




Volumn 9, Issue 4, 2014, Pages 349-358

Interaction of β-Lactoglobulin with Small Hydrophobic Ligands - Influence of Covalent AITC Modification on β-LG Tryptic Cleavage

Author keywords

Allyl isothiocyanate; Beta lactoglobulin; Bioactive peptides; Covalent modification; Trypsin digestion

Indexed keywords

AMINO ACIDS;

EID: 84912151025     PISSN: 15571858     EISSN: 15571866     Source Type: Journal    
DOI: 10.1007/s11483-014-9361-4     Document Type: Article
Times cited : (13)

References (62)
  • 1
    • 0035238955 scopus 로고    scopus 로고
    • Reactions of phenolic substances with lysozyme — physicochemical characterisation and proteolytic digestion of the derivatives
    • H.M. Rawel, J. Kroll, S. Rohn, Reactions of phenolic substances with lysozyme — physicochemical characterisation and proteolytic digestion of the derivatives, Food Chem. 72, 59–71(2001) http://www.sciencedirect.com/science/article/pii/S0308814600002065.
    • (2001) Food Chem , vol.59-71 , pp. 72
    • Rawel, H.M.1    Kroll, J.2    Rohn, S.3
  • 2
    • 0041341891 scopus 로고    scopus 로고
    • Competitive binding of fatty acids and the fluorescent probe 1-8-anilinonaphthalene sulfonate to bovine beta-lactoglobulin
    • COI: 1:CAS:528:DC%2BD3sXlvFSjtb8%3D
    • M. Collini, L. D’Alfonso, H. Molinari, L. Ragona, M. Catalano, G. Baldini, Competitive binding of fatty acids and the fluorescent probe 1-8-anilinonaphthalene sulfonate to bovine beta-lactoglobulin. Protein Sci. 12, 1596–1603 (2003). doi:10.1110/ps.0304403
    • (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
  • 3
    • 77955052598 scopus 로고    scopus 로고
    • Thermally-induced protein-polyphenol co-assemblies: beta lactoglobulin-based nanocomplexes as protective nanovehicles for EGCG
    • A. Shpigelman, G. Israeli, Y.D. Livney, Thermally-induced protein-polyphenol co-assemblies: beta lactoglobulin-based nanocomplexes as protective nanovehicles for EGCG, Food Hydrocoll. 24, 735–743 (2011) http://www.sciencedirect.com/science/article/B6VP9-4YT6D9V-1/2/4ca30bb97971a654401eb48d0f14cb35.
    • (2011) Food Hydrocoll , vol.24 , pp. 735-743
    • Shpigelman, A.1    Israeli, G.2    Livney, Y.D.3
  • 4
    • 0345313659 scopus 로고    scopus 로고
    • ß-Lactoglobulin Binds Palmitate within Its Central Cavity
    • 274, 170–174
    • S.-Y. Wu, M.D. Pèrez, P. Puyol, L. Sawyer, ß-Lactoglobulin Binds Palmitate within Its Central Cavity;10.1074/jbc.274.1.170, J. Biol. Chem. 274, 170–174 (1999)http://www.jbc.org/content/274/1/170.abstract.
    • (1999) J. Biol. Chem
    • Wu, S.-Y.1    Pèrez, M.D.2    Puyol, P.3    Sawyer, L.4
  • 5
    • 84872275671 scopus 로고    scopus 로고
    • Studies on the interaction of -epigallocatechin-3-gallate from green tea with bovine β-lactoglobulin by spectroscopic methods and docking
    • X. Wu, R. Dey, H.U. Wu, Z. Liu, Q. He, X. Zeng, Studies on the interaction of -epigallocatechin-3-gallate from green tea with bovine β-lactoglobulin by spectroscopic methods and docking. Int. J. Dairy Technol. 66, 7–13 (2012)
    • (2012) Int. J. Dairy Technol , vol.66 , pp. 7-13
    • Wu, X.1    Dey, R.2    Wu, H.U.3    Liu, Z.4    He, Q.5    Zeng, X.6
  • 6
    • 75849156917 scopus 로고    scopus 로고
    • Milk proteins as vehicles for bioactives
    • Y.D. Livney, Milk proteins as vehicles for bioactives, Curr. Opin. Colloid Interface Sci. 15, 73–83(2010) http://www.sciencedirect.com/science/article/B6VRY-4XRJX6S-1/2/632b0178768f55cbc9c783da7f8d46a1.
    • (2010) Curr. Opin. Colloid Interface Sci , vol.73-83 , pp. 15
    • Livney, Y.D.1
  • 7
    • 0007426378 scopus 로고    scopus 로고
    • In Vitro Enzymatic Digestion of Benzyl- and Phenylisothiocyanate-Derivatized Food Proteins
    • H.M. Rawel, J. Kroll, I. Schröder, In Vitro Enzymatic Digestion of Benzyl- and Phenylisothiocyanate-Derivatized Food Proteins, J. Agric. Food Chem. 46, 5103–5109(1998) http://dx.doi.org/10.1021/jf980244r.
    • (1998) J. Agric. Food Chem , vol.5103-5109 , pp. 46
    • Rawel, H.M.1    Kroll, J.2    Schröder, I.3
  • 8
    • 3242807589 scopus 로고    scopus 로고
    • Assessment of the reactivity of selected isoflavones against proteins in comparison to quercetin
    • COI: 1:CAS:528:DC%2BD2cXls1KqsL8%3D
    • H.M. Rawel, H. Ranters, S. Rohn, J. Kroll, Assessment of the reactivity of selected isoflavones against proteins in comparison to quercetin. J. Agric. Food Chem. 52, 5263–5271 (2004)
    • (2004) J. Agric. Food Chem , vol.52 , pp. 5263-5271
    • Rawel, H.M.1    Ranters, H.2    Rohn, S.3    Kroll, J.4
  • 9
    • 79851508238 scopus 로고    scopus 로고
    • Formation of conjugates between [beta]-lactoglobulin and allyl isothiocyanate: Effect on protein heat aggregation, foaming and emulsifying properties. Food Colloids 2010: On the Road from Interfaces to Consumers
    • K. Rade-Kukic, C. Schmitt, H.M. Rawel, Formation of conjugates between [beta]-lactoglobulin and allyl isothiocyanate: Effect on protein heat aggregation, foaming and emulsifying properties. Food Colloids 2010: On the Road from Interfaces to Consumers, Food Hydrocoll. 25, 694–706 (2011) http://www.sciencedirect.com/science/article/pii/S0268005X10002006.
    • (2011) Food Hydrocoll , vol.25 , pp. 694-706
    • Rade-Kukic, K.1    Schmitt, C.2    Rawel, H.M.3
  • 10
    • 84899946156 scopus 로고    scopus 로고
    • Characterization of the covalent binding of allyl isothiocyanate to β -lactoglobulin by fluorescence quenching, equilibrium measurement, and mass spectrometry
    • J.K. Keppler, T. Koudelka, K. Palani, M.C. Stuhldreier, F. Temps, A. Tholey, K. Schwarz, Characterization of the covalent binding of allyl isothiocyanate to β -lactoglobulin by fluorescence quenching, equilibrium measurement, and mass spectrometry, J. Biomol. Struct. Dyn.32, 1103-17 (2014) doi: 10.1080/07391102.2013.809605.
    • (2014) J. Biomol. Struct. Dyn , vol.32 , pp. 1103-1117
    • Keppler, J.K.1    Koudelka, T.2    Palani, K.3    Stuhldreier, M.C.4    Temps, F.5    Tholey, A.6    Schwarz, K.7
  • 11
    • 74349084800 scopus 로고    scopus 로고
    • Allyl isothiocyanate as a cancer chemopreventive phytochemical
    • COI: 1:CAS:528:DC%2BC3cXktVeisw%3D%3D
    • Y. Zhang, Allyl isothiocyanate as a cancer chemopreventive phytochemical. Mol. Nutr. Food Res. 54, 127–135 (2010)
    • (2010) Mol. Nutr. Food Res , vol.54 , pp. 127-135
    • Zhang, Y.1
  • 13
    • 0001749707 scopus 로고
    • The Preparation of a Chrystalline Globulin from the Albumin Fraction of Cow’s Milk
    • A.H. Palmer, The Preparation of a Chrystalline Globulin from the Albumin Fraction of Cow’s Milk, J. Biol. Chem. 104, 359–372 (1934) http://www.jbc.org/content/104/2/359.short.
    • (1934) J. Biol. Chem , vol.104 , pp. 359-372
    • Palmer, A.H.1
  • 14
    • 78651171852 scopus 로고
    • Improved method for the preparation of crystalline beta-lactoglobulin and alpha-lactalbumin from cow’s milk
    • COI: 1:CAS:528:DyaG2sXjtVaqsQ%3D%3D
    • R. Aschaffenburg, J. Drewry, Improved method for the preparation of crystalline beta-lactoglobulin and alpha-lactalbumin from cow’s milk. Biochem. J. 65, 273–277 (1957)
    • (1957) Biochem. J , vol.65 , pp. 273-277
    • Aschaffenburg, R.1    Drewry, J.2
  • 15
    • 0034684161 scopus 로고    scopus 로고
    • The core lipocalin, bovine [beta]-lactoglobulin, Biochimica et Biophysica Acta (BBA) - Protein Struct
    • L. Sawyer, G. Kontopidis, The core lipocalin, bovine [beta]-lactoglobulin, Biochimica et Biophysica Acta (BBA) - Protein Struct. Mol. Enzymol. 1482, 136–148 (2000) http://www.sciencedirect.com/science/article/B6T21-41HHN9X-H/2/cc73232c1860ad921ea3cf92a6b4795e.
    • (2000) Mol. Enzymol , vol.1482 , pp. 136-148
    • Sawyer, L.1    Kontopidis, G.2
  • 17
    • 84898606059 scopus 로고    scopus 로고
    • Differences in heat stability and ligand binding among b-lactoglobulin genetic variants A, B and C using (1)H NMR and fluorescence quenching
    • J.K. Keppler, F.D. Sönnichsen, P.-C. Lorenzen, K. Schwarz, Differences in heat stability and ligand binding among b-lactoglobulin genetic variants A, B and C using (1)H NMR and fluorescence quenching. Biochim. Biophys. Acta 6, 1083–1093 (2014) doi:10.1016/j.bbapap.2014.02.007.
    • (2014) Biochim. Biophys. Acta , vol.6 , pp. 1083-1093
    • Keppler, J.K.1    Sönnichsen, F.D.2    Lorenzen, P.-C.3    Schwarz, K.4
  • 18
    • 84867896149 scopus 로고    scopus 로고
    • Binding affinity between dietary polyphenols and β-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed
    • M. Stojadinovic, Binding affinity between dietary polyphenols and β-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed, Food Chem. 136, 1263–1271 (2013) http://resolver.scholarsportal.info/resolve/03088146/v136i3-4/1263_babdpataaocf.xml.
    • (2013) Food Chem , vol.136 , pp. 1263-1271
    • Stojadinovic, M.1
  • 19
    • 33744508956 scopus 로고    scopus 로고
    • Interactions in oil/water/oil films stabilized by β-lactoglobulin; role of the surface charge, A Collection of Papers in Honor of Professor Ivan B. Ivanov (Laboratory of Chemical Physics and Engineering, University of Sofia)
    • E.S. Basheva, T.D. Gurkov, N.C. Christov, B. Campbell, Interactions in oil/water/oil films stabilized by β-lactoglobulin; role of the surface charge, A Collection of Papers in Honor of Professor Ivan B. Ivanov (Laboratory of Chemical Physics and Engineering, University of Sofia) Celebrating his Contributions to Colloid and Surface Science on the Occasion of his 70th Birthday 282–283, 99–108 (2006) http://www.sciencedirect.com/science/article/pii/S0927775706000690.
    • (2006) Celebrating his Contributions to Colloid and Surface Science on the Occasion of his 70th Birthday , vol.282-283 , pp. 99-108
    • Basheva, E.S.1    Gurkov, T.D.2    Christov, N.C.3    Campbell, B.4
  • 20
    • 42149148462 scopus 로고    scopus 로고
    • Droplet surface properties and rheology of concentrated Oil in water emulsions stabilized by heat-modified β-lactoglobulin B
    • COI: 1:CAS:528:DC%2BD1cXitFehtrc%3D
    • J.C. Knudsen, L.H. Øgendal, L.H. Skibsted, Droplet surface properties and rheology of concentrated Oil in water emulsions stabilized by heat-modified β-lactoglobulin B. Langmuir 24, 2603–2610 (2008)
    • (2008) Langmuir , vol.24 , pp. 2603-2610
    • Knudsen, J.C.1    Øgendal, L.H.2    Skibsted, L.H.3
  • 21
    • 0037145868 scopus 로고    scopus 로고
    • Impact of protein surface denaturation on droplet flocculation in hexadecane Oil-in-water emulsions stabilized by β-lactoglobulin
    • COI: 1:CAS:528:DC%2BD38XnvFWntbY%3D
    • H.-J. Kim, E.A. Decker, D.J. McClements, Impact of protein surface denaturation on droplet flocculation in hexadecane Oil-in-water emulsions stabilized by β-lactoglobulin. J. Agric. Food Chem. 50, 7131–7137 (2002)
    • (2002) J. Agric. Food Chem , vol.50 , pp. 7131-7137
    • Kim, H.-J.1    Decker, E.A.2    McClements, D.J.3
  • 22
    • 0001417865 scopus 로고    scopus 로고
    • Static and Dynamic Scattering of b-Lactoglobulin Aggregates Formed after Heat-Induced Denaturation at pH 2
    • P. Aymard, T. Nicolai, D. Durand, A. Clark, Static and Dynamic Scattering of b-Lactoglobulin Aggregates Formed after Heat-Induced Denaturation at pH 2, Macromolecules 32, 2542–2552 (1999) http://dx.doi.org/10.1021/ma981689j.
    • (1999) Macromolecules , vol.32 , pp. 2542-2552
    • Aymard, P.1    Nicolai, T.2    Durand, D.3    Clark, A.4
  • 23
    • 0037041940 scopus 로고    scopus 로고
    • Gelling Properties of Heat-Denatured β-Lactoglobulin Aggregates in a High-Salt Buffer
    • M. Vittayanont, J.F. Steffe, S.L. Flegler, D.M. Smith, Gelling Properties of Heat-Denatured β-Lactoglobulin Aggregates in a High-Salt Buffer, J. Agric. Food Chem. 50, 2987–2992 (2002) http://dx.doi.org/10.1021/jf011410p.
    • (2002) J. Agric. Food Chem , vol.50 , pp. 2987-2992
    • Vittayanont, M.1    Steffe, J.F.2    Flegler, S.L.3    Smith, D.M.4
  • 24
    • 84857059676 scopus 로고    scopus 로고
    • Study of the acid and thermal stability of β-lactoglobulin–ligand complexes using fluorescence quenching. 6th International Conference on Water in Food
    • L. Liang, M. Subirade, Study of the acid and thermal stability of β-lactoglobulin–ligand complexes using fluorescence quenching. 6th International Conference on Water in Food, Food Chem. 132, 2023–2029 (2012) http://www.sciencedirect.com/science/article/pii/S0308814611018115.
    • (2012) Food Chem , vol.132 , pp. 2023-2029
    • Liang, L.1    Subirade, M.2
  • 25
    • 0000443256 scopus 로고
    • Structural and conformational basis of the resistance of.beta.-lactoglobulin to peptic and chymotryptic digestion
    • COI: 1:CAS:528:DyaL1cXksFegt7o%3D
    • I.M. Reddy, N.K.D. Kella, J.E. Kinsella, Structural and conformational basis of the resistance of.beta.-lactoglobulin to peptic and chymotryptic digestion. J. Agric. Food Chem. 36, 737–741 (1988)
    • (1988) J. Agric. Food Chem , vol.36 , pp. 737-741
    • Reddy, I.M.1    Kella, N.K.D.2    Kinsella, J.E.3
  • 28
    • 33646515568 scopus 로고    scopus 로고
    • Emerging Therapeutic Potential of Whey Proteins and Peptides
    • A.S. Yalcin, Emerging Therapeutic Potential of Whey Proteins and Peptides, Curr. Pharm. Des. 12, 1637–1643 (2006) http://www.ingentaconnect.com/content/ben/cpd/2006/00000012/00000013/art00008.
    • (2006) Curr. Pharm. Des , vol.12 , pp. 1637-1643
    • Yalcin, A.S.1
  • 30
    • 0035208510 scopus 로고    scopus 로고
    • IgE and IgG binding epitopes on alpha-lactalbumin and beta-lactoglobulin in cow’s milk allergy
    • K.M. Järvinen, P. Chatchatee, L. Bardina, K. Beyer, H.A. Sampson, IgE and IgG binding epitopes on alpha-lactalbumin and beta-lactoglobulin in cow’s milk allergy. Int. Arch. Allergy Immunol. 126, 111–118 (2001)
    • (2001) Int. Arch. Allergy Immunol , vol.126 , pp. 111-118
    • Järvinen, K.M.1    Chatchatee, P.2    Bardina, L.3    Beyer, K.4    Sampson, H.A.5
  • 31
    • 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
    • J. Leonil, D. Molle, J. Fauquant, J.L. Maubois, R.J. Pearce, S. Bouhallab, 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, J. Dairy Sci. 80, 2270–2281 (1997) http://www.sciencedirect.com/science/article/pii/S0022030297761769.
    • (1997) J. Dairy Sci , vol.80 , pp. 2270-2281
    • Leonil, J.1    Molle, D.2    Fauquant, J.3    Maubois, J.L.4    Pearce, R.J.5    Bouhallab, S.6
  • 32
    • 12344318373 scopus 로고    scopus 로고
    • Beta-lactoglobulin-dextran conjugates: effect of polysaccharide size on emulsion stability
    • COI: 1:CAS:528:DC%2BD2cXhtVOrur7L
    • C.A. Dunlap, G.L. Côté, Beta-lactoglobulin-dextran conjugates: effect of polysaccharide size on emulsion stability. J. Agric. Food Chem. 53, 419–423 (2005)
    • (2005) J. Agric. Food Chem , vol.53 , pp. 419-423
    • Dunlap, C.A.1    Côté, G.L.2
  • 33
    • 33749608762 scopus 로고    scopus 로고
    • Beta-lactoglobulin-dextran Maillard conjugates: their effect on interfacial thickness and emulsion stability
    • COI: 1:CAS:528:DC%2BD28XhtVOnsLjP
    • T.J. Wooster, M.A. Augustin, Beta-lactoglobulin-dextran Maillard conjugates: their effect on interfacial thickness and emulsion stability. J. Colloid Interface Sci. 303, 564–572 (2006)
    • (2006) J. Colloid Interface Sci , vol.303 , pp. 564-572
    • Wooster, T.J.1    Augustin, M.A.2
  • 34
    • 0000131309 scopus 로고
    • Interaction between proteins and glucosinolate isothiocyanates and oxazolidinethiones from Brassica napus seed
    • R. Björkman, Interaction between proteins and glucosinolate isothiocyanates and oxazolidinethiones from Brassica napus seed, Phytochemistry 12, 1585–1590 (1973) http://www.sciencedirect.com/science/article/pii/0031942273803723.
    • (1973) Phytochemistry , vol.12 , pp. 1585-1590
    • Björkman, R.1
  • 35
    • 33845900989 scopus 로고    scopus 로고
    • TRP channel activation by reversible covalent modification
    • COI: 1:CAS:528:DC%2BD2sXhsVGksg%3D%3D
    • A. Hinman, H.-H. Chuang, D.M. Bautista, D. Julius, TRP channel activation by reversible covalent modification. Proc. Natl. Acad. Sci. U. S. A. 103, 19564–19568 (2006)
    • (2006) Proc. Natl. Acad. Sci. U. S. A , vol.103 , pp. 19564-19568
    • Hinman, A.1    Chuang, H.-H.2    Bautista, D.M.3    Julius, D.4
  • 36
    • 0000329369 scopus 로고
    • Interaction of proteins with allyl isothiocyanate
    • 35, 85–88
    • S. Kawakishi, T. Kaneko, Interaction of proteins with allyl isothiocyanate, J. Agric. Food Chem. 35, 85–88 (1987) doi:10.1021/jf00073a020/http://dx.doi.org/10.1021/jf00073a020.
    • (1987) J. Agric. Food Chem
    • Kawakishi, S.1    Kaneko, T.2
  • 37
    • 0000311445 scopus 로고
    • Interaction of allyl isothiocyanate with mustard 12S protein
    • 34, 448–452
    • N.V. Kishore Kumar Murthy, M.S. Narasinga Rao, Interaction of allyl isothiocyanate with mustard 12S protein, J. Agric. Food Chem. 34, 448–452 (1986) doi:10.1021/jf00069a017/http://dx.doi.org/10.1021/jf00069a017.
    • (1986) J. Agric. Food Chem
    • Kishore Kumar Murthy, N.V.1    Narasinga Rao, M.S.2
  • 38
    • 84880348207 scopus 로고    scopus 로고
    • Milk whey protein modification by coffee-specific phenolics: effect on structural and functional properties
    • COI: 1:CAS:528:DC%2BC3sXpvVGht7k%3D
    • M. Ali, T. Homann, M. Khalil, H.-P. Kruse, H. Rawel, Milk whey protein modification by coffee-specific phenolics: effect on structural and functional properties. J. Agric. Food Chem. 61, 6911–6920 (2013)
    • (2013) J. Agric. Food Chem , vol.61 , pp. 6911-6920
    • Ali, M.1    Homann, T.2    Khalil, M.3    Kruse, H.-P.4    Rawel, H.5
  • 39
    • 0037180988 scopus 로고    scopus 로고
    • Stabilization of oil-in-water emulsions by beta-lactoglobulin-polyethylene glycol conjugates
    • COI: 1:CAS:528:DC%2BD38XptVOgsA%3D%3D
    • J.N. Losso, S. Nakai, Stabilization of oil-in-water emulsions by beta-lactoglobulin-polyethylene glycol conjugates. J. Agric. Food Chem. 50, 1207–1212 (2002)
    • (2002) J. Agric. Food Chem , vol.50 , pp. 1207-1212
    • Losso, J.N.1    Nakai, S.2
  • 40
    • 0034633086 scopus 로고    scopus 로고
    • Bioactive peptides derived from bovine whey proteins: opioid and ace-inhibitory peptides, Trends Food Sci
    • A. Pihlanto-Leppälä, Bioactive peptides derived from bovine whey proteins: opioid and ace-inhibitory peptides, Trends Food Sci. Technol. 11, 347–356 (2000) http://www.sciencedirect.com/science/article/pii/S0924224401000036.
    • (2000) Technol , vol.11 , pp. 347-356
    • Pihlanto-Leppälä, A.1
  • 41
    • 84857025302 scopus 로고    scopus 로고
    • MALDI based identification of whey protein derived tryptic marker peptides that resist protein glycation, Food
    • T. Cucu, B. de Meulenaer, B. Kerkaert, I. Vandenberghe, B. Devreese, MALDI based identification of whey protein derived tryptic marker peptides that resist protein glycation, Food Res. Int. 47, 23–30 (2012) http://www.sciencedirect.com/science/article/pii/S0963996911006727.
    • (2012) Res. Int , vol.47 , pp. 23-30
    • Cucu, T.1    de Meulenaer, B.2    Kerkaert, B.3    Vandenberghe, I.4    Devreese, B.5
  • 42
    • 0035603339 scopus 로고    scopus 로고
    • Maillard glycation of beta-lactoglobulin with several sugars: comparative study of the properties of the obtained polymers and of the substituted sites
    • F. Chevalier, J.-M. Chobert, D. Mollé, T. Haertlé, Maillard glycation of beta-lactoglobulin with several sugars: comparative study of the properties of the obtained polymers and of the substituted sites, Lait 81, 651–666 (2001) http://dx.doi.org/10.1051/lait:2001155.
    • (2001) Lait , vol.81 , pp. 651-666
    • Chevalier, F.1    Chobert, J.-M.2    Mollé, D.3    Haertlé, T.4
  • 44
    • 74049136098 scopus 로고    scopus 로고
    • Application of liquid chromatography–tandem mass spectrometry for the characterization of galactosylated and tagatosylated β-lactoglobulin peptides derived from in vitro gastrointestinal digestion, Adv
    • M. Corzo-Martínez, R. Lebrón-Aguilar, M. Villamiel, J.E. Quintanilla-López, F.J. Moreno, Application of liquid chromatography–tandem mass spectrometry for the characterization of galactosylated and tagatosylated β-lactoglobulin peptides derived from in vitro gastrointestinal digestion, Adv. Sep. Methods Food Anal. 1216, 7205–7212 (2009) http://www.sciencedirect.com/science/article/pii/S0021967309012606.
    • (2009) Sep. Methods Food Anal , vol.1216 , pp. 7205-7212
    • Corzo-Martínez, M.1    Lebrón-Aguilar, R.2    Villamiel, M.3    Quintanilla-López, J.E.4    Moreno, F.J.5
  • 45
    • 45849113263 scopus 로고    scopus 로고
    • Mass Spectrometric Characterization of Glycated β-Lactoglobulin Peptides Derived from Galacto-oligosaccharides Surviving the In Vitro Gastrointestinal Digestion
    • F.J. Moreno, J.E. Quintanilla-López, R. Lebrón-Aguilar, A. Olano, M.L. Sanz, Mass Spectrometric Characterization of Glycated β-Lactoglobulin Peptides Derived from Galacto-oligosaccharides Surviving the In Vitro Gastrointestinal Digestion, J. Am. Soc. Mass Spectrom. 19, 927–937 (2008) http://www.sciencedirect.com/science/article/pii/S1044030508002675.
    • (2008) J. Am. Soc. Mass Spectrom , vol.19 , pp. 927-937
    • Moreno, F.J.1    Quintanilla-López, J.E.2    Lebrón-Aguilar, R.3    Olano, A.4    Sanz, M.L.5
  • 46
    • 0033851278 scopus 로고    scopus 로고
    • Reactions of Allyl Isothiocyanate with Alanine, Glycine, and Several Peptides in Model Systems
    • 48, 3560–3565
    • K. Cejpek, J. Valusek, J. Velisek, Reactions of Allyl Isothiocyanate with Alanine, Glycine, and Several Peptides in Model Systems, J. Agric. Food Chem. 48, 3560–3565 (2000) doi:10.1021/jf991019s/http://dx.doi.org/10.1021/jf991019s.
    • (2000) J. Agric. Food Chem
    • Cejpek, K.1    Valusek, J.2    Velisek, J.3
  • 48
    • 0033200126 scopus 로고    scopus 로고
    • Identification of Fluorescein-5′-Isothiocyanate-Modification Sites in Proteins by Electrospray-Ionization Mass Spectrometry
    • V. Schnaible, M. Przybylski, Identification of Fluorescein-5′-Isothiocyanate-Modification Sites in Proteins by Electrospray-Ionization Mass Spectrometry, Bioconjugate Chem 10, 861–866 (1999) http://dx.doi.org/http://dx.doi.org/10.1021/bc990039x.
    • (1999) Bioconjugate Chem , vol.10 , pp. 861-866
    • Schnaible, V.1    Przybylski, M.2
  • 51
    • 1142299461 scopus 로고    scopus 로고
    • Solid-state glycation of β-lactoglobulin by lactose and galactose: localization of the modified amino acids using mass spectrometric techniques
    • F. Fenaille, F. Morgan, V. Parisod, J.-C. Tabet, P.A. Guy, Solid-state glycation of β-lactoglobulin by lactose and galactose: localization of the modified amino acids using mass spectrometric techniques, J. Mass Spectrom. 39, 16–28. (2004) http://dx.doi.org/10.1002/jms.539.
    • (2004) J. Mass Spectrom , vol.39 , pp. 16-28
    • Fenaille, F.1    Morgan, F.2    Parisod, V.3    Tabet, J.-C.4    Guy, P.A.5
  • 52
    • 13544263199 scopus 로고    scopus 로고
    • Epitope mapping of a monoclonal antibody specific to bovine dry milk. Involvement of residues 66–76 of strand D in thermal denatured beta-lactoglobulin
    • COI: 1:CAS:528:DC%2BD2MXovVGgsg%3D%3D
    • C.Y. Song, W.L. Chen, M.C. Yang, J.P. Huang, S.J. Mao, Epitope mapping of a monoclonal antibody specific to bovine dry milk. Involvement of residues 66–76 of strand D in thermal denatured beta-lactoglobulin. J.Biol. Chem. 280, 3574–3582 (2005)
    • (2005) J.Biol. Chem , vol.280 , pp. 3574-3582
    • Song, C.Y.1    Chen, W.L.2    Yang, M.C.3    Huang, J.P.4    Mao, S.J.5
  • 53
    • 0031577271 scopus 로고    scopus 로고
    • Nonenzymatic lactosylation of bovine beta-lactoglobulin under mild heat treatment leads to structural heterogeneity of the glycoforms
    • COI: 1:CAS:528:DyaK2sXkvVWrtr0%3D
    • F. Morgan, J. Léonil, D. Mollé, S. Bouhallab, Nonenzymatic lactosylation of bovine beta-lactoglobulin under mild heat treatment leads to structural heterogeneity of the glycoforms. Biochem. Biophys. Res. Commun. 236, 413–417 (1997)
    • (1997) Biochem. Biophys. Res. Commun , vol.236 , pp. 413-417
    • Morgan, F.1    Léonil, J.2    Mollé, D.3    Bouhallab, S.4
  • 54
    • 65949117445 scopus 로고    scopus 로고
    • Covalent modification of lysine residues by allyl isothiocyanate in physiological conditions: plausible transformation of isothiocyanate from thiol to amine
    • COI: 1:CAS:528:DC%2BD1MXhvFGms7Y%3D
    • T. Nakamura, Y. Kawai, N. Kitamoto, T. Osawa, Y. Kato, Covalent modification of lysine residues by allyl isothiocyanate in physiological conditions: plausible transformation of isothiocyanate from thiol to amine. Chem. Res. Toxicol. 22, 536–542 (2009)
    • (2009) Chem. Res. Toxicol , vol.22 , pp. 536-542
    • Nakamura, T.1    Kawai, Y.2    Kitamoto, N.3    Osawa, T.4    Kato, Y.5
  • 55
    • 0032987138 scopus 로고    scopus 로고
    • Investigation of some covalent and noncovalent complexes by matrix-assisted laser desorption/ionization time-of-flight and electrospray mass spectrometry, Rapid Commun
    • 13, 1143–1151
    • E. Bordini, M. Hamdan, Investigation of some covalent and noncovalent complexes by matrix-assisted laser desorption/ionization time-of-flight and electrospray mass spectrometry, Rapid Commun. Mass Spectrom. 13, 1143–1151 (1999) http://dx.doi.org/10.1002/(SICI)1097-0231(19990630)13:12<1143:AID-RCM626>3.0.CO;2-J.
    • (1999) Mass Spectrom
    • Bordini, E.1    Hamdan, M.2
  • 56
    • 0026618996 scopus 로고
    • Preincubation with cysteine prevents modification of sulfhydryl groups in proteins by unreacted acrylamide in a gel
    • COI: 1:CAS:528:DyaK3sXlsFCgtw%3D%3D
    • M. Chiari, P.G. Righetti, A. Negri, F. Ceciliani, S. Ronchi, Preincubation with cysteine prevents modification of sulfhydryl groups in proteins by unreacted acrylamide in a gel. Electrophoresis 13, 882–884 (1992)
    • (1992) Electrophoresis , vol.13 , pp. 882-884
    • Chiari, M.1    Righetti, P.G.2    Negri, A.3    Ceciliani, F.4    Ronchi, S.5
  • 57
    • 0004097075 scopus 로고    scopus 로고
    • O. Curcuruto, E. Bordini, L. Rovatti, M. Hamdan, Liquid chromatography/tandem mass spectrometry to monitor acrylamide adducts with bovine β-lactoglobulin B, Rapid Commun. . 12, 1494–1500
    • O. Curcuruto, E. Bordini, L. Rovatti, M. Hamdan, Liquid chromatography/tandem mass spectrometry to monitor acrylamide adducts with bovine β-lactoglobulin B, Rapid Commun. Mass Spectrom. 12, 1494–1500 (1998) http://dx.doi.org/10.1002/(SICI)1097-0231(19981030)12:20<1494:AID-RCM354>3.0.CO;2-K.
    • (1998) Mass Spectrom
  • 58
    • 0000008542 scopus 로고    scopus 로고
    • Heat-induced aggregation of β-lactoglobulin: role of the free thiol group and disulfide bonds
    • COI: 1:CAS:528:DyaK2sXltV2qsbg%3D
    • M.A.M. Hoffmann, P.J.J.M. van Mil, Heat-induced aggregation of β-lactoglobulin: role of the free thiol group and disulfide bonds. J. Agric. Food Chem. 45, 2942–2948 (1997)
    • (1997) J. Agric. Food Chem , vol.45 , pp. 2942-2948
    • Hoffmann, M.A.M.1    van Mil, P.J.J.M.2
  • 59
    • 0035530454 scopus 로고    scopus 로고
    • The Maillard Reaction Products Of β-Lactoglobulin Glucosylated In Mild Conditions
    • F. Chevalier, J.-M. Chobert, M. Dalgalarrondo, T. Haertlé, Characterization Of The Maillard Reaction Products Of β-Lactoglobulin Glucosylated In Mild Conditions, J. Food Biochem. 25, 33–55 (2001) http://dx.doi.org/10.1111/j.1745-4514.2001.tb00723.x.
    • (2001) J. Food Biochem , vol.25 , pp. 33-55
    • Chevalier, F.1    Chobert, J.-M.2    Dalgalarrondo, M.3    Haertlé, T.4    Of, C.5
  • 60
    • 0032524087 scopus 로고    scopus 로고
    • Selective detection of lactolated peptides in hydrolysates by liquid chromatography/electrospray tandem mass spectrometry
    • D. Mollé, F. Morgan, S. Bouhallab, J. Léonil, Selective detection of lactolated peptides in hydrolysates by liquid chromatography/electrospray tandem mass spectrometry. Anal. Biochem. 259, 152–161 (1998)
    • (1998) Anal. Biochem , vol.259 , pp. 152-161
    • Mollé, D.1    Morgan, F.2    Bouhallab, S.3    Léonil, J.4
  • 61
    • 0032047290 scopus 로고    scopus 로고
    • Converting Enzyme Inhibitory Peptides Derived from Bovine Milk Proteins
    • A. Pihlanto-Leppälä, T. Rokka, H. Korhonen, Angiotensin I Converting Enzyme Inhibitory Peptides Derived from Bovine Milk Proteins, Int. Dairy J. 8, 325–331 (1998) http://www.sciencedirect.com/science/article/pii/S095869469800048X.
    • (1998) Int. Dairy J , vol.8 , pp. 325-331
    • Pihlanto-Leppälä, A.1    Rokka, T.2    Korhonen, H.3    Angiotensin, I.4
  • 62
    • 0034804066 scopus 로고    scopus 로고
    • Identification of Novel Hypocholesterolemic Peptides Derived from Bovine Milk β-Lactoglobulin, Biochem
    • S. Nagaoka, Y. Futamura, K. Miwa, T. Awano, K. Yamauchi, Y. Kanamaru, K. Tadashi, T. Kuwata, Identification of Novel Hypocholesterolemic Peptides Derived from Bovine Milk β-Lactoglobulin, Biochem. Biophys. Res. Commun. 281, 11–17 (2001) http://www.sciencedirect.com/science/article/pii/S0006291X01942986.
    • (2001) Biophys. Res. Commun , vol.281 , pp. 11-17
    • Nagaoka, S.1    Futamura, Y.2    Miwa, K.3    Awano, T.4    Yamauchi, K.5    Kanamaru, Y.6    Tadashi, K.7    Kuwata, T.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.