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Volumn 24, Issue 3, 2013, Pages 305-313

Reduced allergenicity of β-lactoglobulin in vitro by tea catechins binding

Author keywords

lactoglobulin; catechin; IgG IgE binding; protein polyphenols interactions; reduced allergenicity

Indexed keywords


EID: 84884217322     PISSN: 09540105     EISSN: 14653443     Source Type: Journal    
DOI: 10.1080/09540105.2012.686989     Document Type: Article
Times cited : (10)

References (28)
  • 1
    • 13844298151 scopus 로고    scopus 로고
    • Potential tannase producers from the genera Aspergillus and Penicillium
    • Batra, A., & Saxena, R.K. (2005). Potential tannase producers from the genera Aspergillus and Penicillium. Process Biochemistry, 40, 1553-1557.
    • (2005) Process Biochemistry , vol.40 , pp. 1553-1557
    • Batra, A.1    Saxena, R.K.2
  • 4
    • 0029790266 scopus 로고    scopus 로고
    • The lipocalin protein family: Structure and function
    • Flower, D.R. (1996). The lipocalin protein family: Structure and function. Biochemical Journal, 318, 1-14.
    • (1996) Biochemical Journal , vol.318 , pp. 1-14
    • Flower, D.R.1
  • 7
    • 0019331472 scopus 로고
    • Spectroscopic characterization of β-lactoglobulin retinol complex
    • Fugate, R., & Song, P. (1980). Spectroscopic characterization of β-lactoglobulin retinol complex. Biochimica and Biophysica Acta, 625, 28-42.
    • (1980) Biochimica and Biophysica Acta , vol.625 , pp. 28-42
    • Fugate, R.1    Song, P.2
  • 10
    • 0033969515 scopus 로고    scopus 로고
    • Reduced immunogenicity of β-lactoglobulin by conjugation with carboxymethyl dextran
    • Hattori, M., Nagasawa, K., Ohgata, K., Sone, N., Fukuda, A., Matsuda, H., et al. (2000a). Reduced immunogenicity of β-lactoglobulin by conjugation with carboxymethyl dextran. Bioconjugate Chemisty, 11, 84-93.
    • (2000) Bioconjugate Chemisty , vol.11 , pp. 84-93
    • Hattori, M.1    Nagasawa, K.2    Ohgata, K.3    Sone, N.4    Fukuda, A.5    Matsuda, H.6
  • 12
    • 0016432123 scopus 로고
    • Immunogenic properties of modified antigen E. II. Ability of urea-denatured antigen and a polypeptide chain to prime T cells specific for antigen
    • Ishizaka, K., Okudaira, H., & King, T. (1975). Immunogenic properties of modified antigen E. II. Ability of urea-denatured antigen and a polypeptide chain to prime T cells specific for antigen. Journal Immunology, 114, 110-115.
    • (1975) Journal Immunology , vol.114 , pp. 110-115
    • Ishizaka, K.1    Okudaira, H.2    King, T.3
  • 14
    • 49449118509 scopus 로고    scopus 로고
    • Effect of green and black teas (Camellia sinensis L.) on the characteristic microflora of yogurt during fermentation and refrigerated storage
    • Jaziri, I., Slama, M.B., Mhadhbi, H., Urdaci, M.C., & Hamdi, M. (2009). Effect of green and black teas (Camellia sinensis L.) on the characteristic microflora of yogurt during fermentation and refrigerated storage. Food Chemistry, 112, 614-620.
    • (2009) Food Chemistry , vol.112 , pp. 614-620
    • Jaziri, I.1    Slama, M.B.2    Mhadhbi, H.3    Urdaci, M.C.4    Hamdi, M.5
  • 17
    • 0015895751 scopus 로고
    • Quenching of protein fluorescence by oxygen. detection of structural fluctuations in proteins on the nanosecond time scale
    • Lakowicz, J.R., & Weber, G. (1973). Quenching of protein fluorescence by oxygen. detection of structural fluctuations in proteins on the nanosecond time scale. Biochemistry, 12, 4171-4179.
    • (1973) Biochemistry , vol.12 , pp. 4171-4179
    • Lakowicz, J.R.1    Weber, G.2
  • 19
    • 0032892220 scopus 로고    scopus 로고
    • Effect of extracts of oak (Quercus petraea) bark, oak leaves, aloe vera (Curacao aloe), coconut shell and wine on the colloidal stability of milk and concentrated milk
    • O'Connell, J.E., & Fox, P.F. (1999). Effect of extracts of oak (Quercus petraea) bark, oak leaves, aloe vera (Curacao aloe), coconut shell and wine on the colloidal stability of milk and concentrated milk. Food Chemistry, 66, 93-96.
    • (1999) Food Chemistry , vol.66 , pp. 93-96
    • O'Connell, J.E.1    Fox, P.F.2
  • 20
    • 0029302371 scopus 로고
    • Interaction of â-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein
    • Pèrez, M.D., & Calvo, M. (1995). Interaction of â-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein. Journal of Dairy Science, 78, 978-988.
    • (1995) Journal of Dairy Science , vol.78 , pp. 978-988
    • Pèrez, M.D.1    Calvo, M.2
  • 23
    • 84954965877 scopus 로고
    • Emulsifying and structural properties of β-lactoglobulin at different pHs
    • Shimizu, M., Saito, M., & Yamauchi, K. (1985). Emulsifying and structural properties of β-lactoglobulin at different pHs. Agricultural Biology and Chemistry, 49, 189-194.
    • (1985) Agricultural Biology and Chemistry , vol.49 , pp. 189-194
    • Shimizu, M.1    Saito, M.2    Yamauchi, K.3
  • 24
  • 25
    • 77951631566 scopus 로고    scopus 로고
    • Dual effect of milk on the antioxidant capacity of green, Darjeeling, and English breakfast teas
    • Svetli, D., Guy, S., & Heidar-Ali, T. (2010). Dual effect of milk on the antioxidant capacity of green, Darjeeling, and English breakfast teas. Food Chemistry, 122, 539-545.
    • (2010) Food Chemistry , vol.122 , pp. 539-545
    • Svetli, D.1    Guy, S.2    Heidar-Ali, T.3
  • 26
    • 0028063528 scopus 로고
    • Determination of protein tertiary structure class from circular dichroism spectra
    • Venyaminov, S.Y., & Vesilenko, K.S. (1994). Determination of protein tertiary structure class from circular dichroism spectra. Analytical Biochemistry, 222, 176-184.
    • (1994) Analytical Biochemistry , vol.222 , pp. 176-184
    • Venyaminov, S.Y.1    Vesilenko, K.S.2
  • 27
    • 85008124098 scopus 로고
    • Controlled enzymatic treatment of wheat proteins for production of hypoallergenic flour
    • Watanabe, M., Suzuki, T., Ikezawa, Z., & Arai, S. (1994). Controlled enzymatic treatment of wheat proteins for production of hypoallergenic flour. Bioscience Biotechnology & Biochemistry, 58, 388-390.
    • (1994) Bioscience Biotechnology & Biochemistry , vol.58 , pp. 388-390
    • Watanabe, M.1    Suzuki, T.2    Ikezawa, Z.3    Arai, S.4
  • 28
    • 76749084741 scopus 로고    scopus 로고
    • Characterization of binding interactions between green tea flavanoids and milk proteins
    • Zerrin, Y., Elif, A., & Yasar, K.E. (2010). Characterization of binding interactions between green tea flavanoids and milk proteins. Food Chemistry, 121, 450-456.
    • (2010) Food Chemistry , vol.121 , pp. 450-456
    • Zerrin, Y.1    Elif, A.2    Yasar, K.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.