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Volumn 53, Issue 25, 2005, Pages 9810-9816

Phospholipid interactions protect the milk allergen α-lactalbumin from proteolysis during in vitro digestion

Author keywords

Lactalbumin; Digestion; Food allergy; Phosphatidylcholine; Protein lipid interaction

Indexed keywords

ALLERGEN; LACTALBUMIN; PEPSIN A; PEPTIDE HYDROLASE; PHOSPHATIDYLCHOLINE; TRIACYLGLYCEROL LIPASE;

EID: 29744451337     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf0515227     Document Type: Article
Times cited : (115)

References (33)
  • 2
    • 0032199537 scopus 로고    scopus 로고
    • An update on allergens - Cow's milk allergens
    • Wal, J. M. An update on allergens - Cow's milk allergens. Allergy 1998, 53, 1013-1022.
    • (1998) Allergy , vol.53 , pp. 1013-1022
    • Wal, J.M.1
  • 3
    • 0025690072 scopus 로고
    • A critical-evaluation of the predicted and X-ray structures of α-lactalbumin
    • Acharya, K. R.; Stuart, D. I.; Phillips, D. C.; Scheraga, H. A. A critical-evaluation of the predicted and X-ray structures of α-lactalbumin. J. Protein Chem. 1990, 9, 549-563.
    • (1990) J. Protein Chem. , vol.9 , pp. 549-563
    • Acharya, K.R.1    Stuart, D.I.2    Phillips, D.C.3    Scheraga, H.A.4
  • 7
    • 0035007581 scopus 로고    scopus 로고
    • Adsorption dynamics and interfacial properties of α-lactalbumin in native and molten globule state conformation at air-water interface
    • Cornec, M.; Kim, D. A.; Narsimhan, G. Adsorption dynamics and interfacial properties of α-lactalbumin in native and molten globule state conformation at air-water interface. Food Hydrocolloids 2001, 15, 303-313.
    • (2001) Food Hydrocolloids , vol.15 , pp. 303-313
    • Cornec, M.1    Kim, D.A.2    Narsimhan, G.3
  • 8
    • 0002810940 scopus 로고    scopus 로고
    • Allergenicity assessment of foods derived from genetically modified plants
    • Fuchs, R. L.; Astwood, J. D. Allergenicity assessment of foods derived from genetically modified plants. Food Technol. 1996, 50, 83-88.
    • (1996) Food Technol. , vol.50 , pp. 83-88
    • Fuchs, R.L.1    Astwood, J.D.2
  • 9
    • 0033836431 scopus 로고    scopus 로고
    • Structural biology of allergens
    • Aalberse, R. C. Structural biology of allergens. J. Allergy Clin. Immunol. 2000, 106, 228-238.
    • (2000) J. Allergy Clin. Immunol. , vol.106 , pp. 228-238
    • Aalberse, R.C.1
  • 10
    • 0035947036 scopus 로고    scopus 로고
    • What establishes a protein as an allergen?
    • Bredehorst, R.; David, K. What establishes a protein as an allergen? J. Chromatogr. B 2001, 756, 33-40.
    • (2001) J. Chromatogr. B , vol.756 , pp. 33-40
    • Bredehorst, R.1    David, K.2
  • 11
    • 0029764078 scopus 로고    scopus 로고
    • Stability of food allergens to digestion in vitro
    • Astwood, J. D.; Leach, J. N.; Fuchs, R. L. Stability of food allergens to digestion in vitro. Nat. Biotechnol. 1996, 14, 1269-1273.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1269-1273
    • Astwood, J.D.1    Leach, J.N.2    Fuchs, R.L.3
  • 12
    • 0037145909 scopus 로고    scopus 로고
    • Digestibility of food allergens and nonallergenic proteins in simulated gastric fluid and simulated intestinal fluid - A comparative study
    • Fu, T.-J.; Abbott, U. R.; Hatzos, C. Digestibility of food allergens and nonallergenic proteins in simulated gastric fluid and simulated intestinal fluid - A comparative study. J. Agric. Food Chem. 2002, 50, 7154-7160.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 7154-7160
    • Fu, T.-J.1    Abbott, U.R.2    Hatzos, C.3
  • 13
    • 29744436573 scopus 로고
    • Gastric Juice
    • Geigy Pharmaceuticals: Macclesfield, UK
    • th ed.; Diem, K., Lentner, C., Eds; Geigy Pharmaceuticals: Macclesfield, UK, 1973; pp 646-651.
    • (1973) th Ed. , pp. 646-651
    • Diem, K.1    Lentner, C.2
  • 15
    • 1642491766 scopus 로고    scopus 로고
    • β-lactoglobulin/polysaccharide interactions during in vitro gastric and pancreatic hydrolysis assessed in dialysis bags of different molecular weight cutoffs
    • Mouecoucou, J.; Villaume, C.; Sánchez, C.; Mejean, L. β-lactoglobulin/polysaccharide interactions during in vitro gastric and pancreatic hydrolysis assessed in dialysis bags of different molecular weight cutoffs. Biochim. Biophys. Acta G-Gen. Subj. 2004, 1670, 105-112.
    • (2004) Biochim. Biophys. Acta G-Gen. Subj. , vol.1670 , pp. 105-112
    • Mouecoucou, J.1    Villaume, C.2    Sánchez, C.3    Mejean, L.4
  • 16
    • 0141884357 scopus 로고    scopus 로고
    • Solubilization of carotenoids from carrot juice and spinach in lipid phases: I. Modelling the gastric lumen
    • Rich, G. T.; Bailey, A. L.; Faulks, R. M.; Parker, M. L.; Wickham, M. S. J.; Fillery-Travis, A. Solubilization of carotenoids from carrot juice and spinach in lipid phases: I. Modelling the gastric lumen. Lipids 2003, 38, 933-945.
    • (2003) Lipids , vol.38 , pp. 933-945
    • Rich, G.T.1    Bailey, A.L.2    Faulks, R.M.3    Parker, M.L.4    Wickham, M.S.J.5    Fillery-Travis, A.6
  • 17
    • 12544254069 scopus 로고    scopus 로고
    • Stability of the major allergen Brazil nut 2S albumin (Ber e 1) to physiologically relevant in vitro gastrointestinal digestion
    • Moreno, F. J.; Mellon, F. A.; Wickham, M. S. J.; Bottrill, A. R.; Mills, E. N. C. Stability of the major allergen Brazil nut 2S albumin (Ber e 1) to physiologically relevant in vitro gastrointestinal digestion. FEBS J. 2005, 272, 341-352.
    • (2005) FEBS J. , vol.272 , pp. 341-352
    • Moreno, F.J.1    Mellon, F.A.2    Wickham, M.S.J.3    Bottrill, A.R.4    Mills, E.N.C.5
  • 19
    • 0019886182 scopus 로고
    • Interaction of α-lactalbumin with dimyristoyl phosphatidylcholine vesicles - II. A fluorescence polarization study
    • Herreman, W.; van Tornout, P.; van Cauwelaert, F. H.; Hanssens, I. Interaction of α-lactalbumin with dimyristoyl phosphatidylcholine vesicles - II. A fluorescence polarization study. Biochim. Biophys. Acta 1981, 640, 419-429.
    • (1981) Biochim. Biophys. Acta , vol.640 , pp. 419-429
    • Herreman, W.1    Van Tornout, P.2    Van Cauwelaert, F.H.3    Hanssens, I.4
  • 20
    • 0021876398 scopus 로고
    • Influence of the protein conformation on the interaction between α-lactalbumin and dimyristoyl phosphatidylcholine vesicles
    • Hanssens, I.; van Ceunebroeck, J.-C.; Pottel, H.; Preaux, G.; van Cauwelaert, F. Influence of the protein conformation on the interaction between α-lactalbumin and dimyristoyl phosphatidylcholine vesicles. Biochim. Biophys. Acta 1985, 817, 154-164.
    • (1985) Biochim. Biophys. Acta , vol.817 , pp. 154-164
    • Hanssens, I.1    Van Ceunebroeck, J.-C.2    Pottel, H.3    Preaux, G.4    Van Cauwelaert, F.5
  • 21
    • 0022423885 scopus 로고
    • Comparison of the transient folding intermediates in lysozyme and α-lactalbumin
    • Kuwajima, K.; Hiraoka, Y.; Ikeguchi, M.; Sugai, S. Comparison of the transient folding intermediates in lysozyme and α-lactalbumin. Biochemistry 1985, 24, 874-881.
    • (1985) Biochemistry , vol.24 , pp. 874-881
    • Kuwajima, K.1    Hiraoka, Y.2    Ikeguchi, M.3    Sugai, S.4
  • 22
    • 0032529077 scopus 로고    scopus 로고
    • The ATPase and ATP-binding functions of P-glycoprotein - Modulation by interaction with defined phospholipids
    • Romsicki, Y.; Sharom, F. J. The ATPase and ATP-binding functions of P-glycoprotein - Modulation by interaction with defined phospholipids. Eur. J. Biochem. 1998, 256, 170-178.
    • (1998) Eur. J. Biochem. , vol.256 , pp. 170-178
    • Romsicki, Y.1    Sharom, F.J.2
  • 23
    • 0028829497 scopus 로고
    • Raising the pH of the pepsin-catalyzed hydrolysis of bovine whey proteins increases the antigenicity of the hydrolysates
    • Schmidt, D. G.; Meijer, R. J.; Slangen, C. J.; van Beresteijn, E. C. Raising the pH of the pepsin-catalyzed hydrolysis of bovine whey proteins increases the antigenicity of the hydrolysates. Clin. Exp. Allergy 1995, 25, 1007-1017.
    • (1995) Clin. Exp. Allergy , vol.25 , pp. 1007-1017
    • Schmidt, D.G.1    Meijer, R.J.2    Slangen, C.J.3    Van Beresteijn, E.C.4
  • 24
    • 0028511883 scopus 로고
    • Proteins at liquid interfaces: Role of the molten globule state
    • Dickinson, E.; Matsumura, Y. Proteins at liquid interfaces: Role of the molten globule state. Colloid Surf. B - Biointerfaces 1994, 3, 1-17.
    • (1994) Colloid Surf. B - Biointerfaces , vol.3 , pp. 1-17
    • Dickinson, E.1    Matsumura, Y.2
  • 25
    • 0020335465 scopus 로고
    • Binding of naphthalene dyes to the N-conformer and A-conformer of bovine α-lactalbumin
    • Mulqueen, P. M.; Kronman, M. J. Binding of naphthalene dyes to the N-conformer and A-conformer of bovine α-lactalbumin. Arch. Biochem. Biophys. 1982, 215, 28-39.
    • (1982) Arch. Biochem. Biophys. , vol.215 , pp. 28-39
    • Mulqueen, P.M.1    Kronman, M.J.2
  • 26
    • 0027543524 scopus 로고
    • Molten globule state of food proteins
    • Hirose, M. Molten globule state of food proteins. Trends Food Sci. Technol. 1993, 4, 48-51.
    • (1993) Trends Food Sci. Technol. , vol.4 , pp. 48-51
    • Hirose, M.1
  • 27
    • 0023040490 scopus 로고
    • Fusion of phospholipid-vesicles induced by α-lactalbumin at acidic pH
    • Kim, J.; Kim, H. Fusion of phospholipid-vesicles induced by α-lactalbumin at acidic pH. Biochemistry 1986, 25, 7867-7874.
    • (1986) Biochemistry , vol.25 , pp. 7867-7874
    • Kim, J.1    Kim, H.2
  • 28
    • 0029886518 scopus 로고    scopus 로고
    • Structural requirements for the association of native and partially folded conformations of α-lactalbumin with model membranes
    • Bañuelos, S.; Muga, A. Structural requirements for the association of native and partially folded conformations of α-lactalbumin with model membranes. Biochemistry 1996, 35, 3892-3898.
    • (1996) Biochemistry , vol.35 , pp. 3892-3898
    • Bañuelos, S.1    Muga, A.2
  • 29
    • 0034615552 scopus 로고    scopus 로고
    • The two sides of enzyme - Substrate specificity: Lessons from the aspartic proteinases
    • Dunn, B. M.; Hung, S.-H. The two sides of enzyme - substrate specificity: Lessons from the aspartic proteinases. Biochim. Biophys. Acta - Protein Struct. Mol. Enzymol. 2000, 1477, 231-240.
    • (2000) Biochim. Biophys. Acta - Protein Struct. Mol. Enzymol. , vol.1477 , pp. 231-240
    • Dunn, B.M.1    Hung, S.-H.2
  • 30
    • 0024372055 scopus 로고
    • Interaction of α-lactalbumin with phospholipid vesicles as studied by photoactivated hydrophobic labeling
    • Kim, J.; Kim, H. Interaction of α-lactalbumin with phospholipid vesicles as studied by photoactivated hydrophobic labeling. Biochim. Biophys. Acta 1989, 983, 1-8.
    • (1989) Biochim. Biophys. Acta , vol.983 , pp. 1-8
    • Kim, J.1    Kim, H.2
  • 31
    • 0024424857 scopus 로고
    • Effect of phosphatidylcholine on the α-lactalbumin-induced fusion of vesicles
    • Park, B. S.; Kim, J.; Kim, U. H.; Kim, H. Effect of phosphatidylcholine on the α-lactalbumin-induced fusion of vesicles. Lipids 1989, 24, 854-858.
    • (1989) Lipids , vol.24 , pp. 854-858
    • Park, B.S.1    Kim, J.2    Kim, U.H.3    Kim, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.