메뉴 건너뛰기




Volumn 47, Issue 2, 2007, Pages 127-143

Allergenicity of soybean: New developments in identification of allergenic proteins, cross-reactivities and hypoallergenization technologies

Author keywords

Allergenic proteins; Allergenicity; Allergens; Cross reactivity; Hypoallergenization; Soybean

Indexed keywords

ALLERGEN; PHOSPHATIDYLCHOLINE; SOYBEAN PROTEIN; VEGETABLE PROTEIN;

EID: 33847305451     PISSN: 10408398     EISSN: 15497852     Source Type: Journal    
DOI: 10.1080/10408390600626487     Document Type: Article
Times cited : (143)

References (165)
  • 1
    • 33847306741 scopus 로고    scopus 로고
    • USDA. 2003. United States Department of Agriculture. In: http//www.soystats.com.
    • USDA. 2003. United States Department of Agriculture. In: http//www.soystats.com.
  • 6
    • 0037723037 scopus 로고    scopus 로고
    • Food Allergens of plant origin- their molecular and evolutionary relationships
    • Mills, E.N.C., Madsen, C., Shewry, P.R., and Wichers, H.J. 2003. Food Allergens of plant origin- their molecular and evolutionary relationships. Trends Food Sci. Technol., 14:145-156.
    • (2003) Trends Food Sci. Technol , vol.14 , pp. 145-156
    • Mills, E.N.C.1    Madsen, C.2    Shewry, P.R.3    Wichers, H.J.4
  • 7
    • 2342650734 scopus 로고    scopus 로고
    • Update on food allergy
    • Sampson, H.A. 2004. Update on food allergy. J. Allergy Clin. Immunol., 113(5):805-819.
    • (2004) J. Allergy Clin. Immunol , vol.113 , Issue.5 , pp. 805-819
    • Sampson, H.A.1
  • 8
    • 17844383645 scopus 로고    scopus 로고
    • Opinion of the Scientific Panel on Dietetic Products, Nutrition and Allergies on a request from the Commission relating to the evaluation of allergenic foods for labelling purposes (Request No EFSA-Q-2003-016)
    • Becker, W., Brasseur, D., Bresson, J.L., Flynn, A., Jackson, A.A., Lagiou, P., Mingrone, G., Moseley, B., Palou, A., Przyrembel, H., Salminen, S., Strobel, S., and van Loveren, H. 2004. Opinion of the Scientific Panel on Dietetic Products, Nutrition and Allergies on a request from the Commission relating to the evaluation of allergenic foods for labelling purposes (Request No EFSA-Q-2003-016). EFSA Journal, 32:1-197.
    • (2004) EFSA Journal , vol.32 , pp. 1-197
    • Becker, W.1    Brasseur, D.2    Bresson, J.L.3    Flynn, A.4    Jackson, A.A.5    Lagiou, P.6    Mingrone, G.7    Moseley, B.8    Palou, A.9    Przyrembel, H.10    Salminen, S.11    Strobel, S.12    van Loveren, H.13
  • 10
    • 0033043827 scopus 로고    scopus 로고
    • A study on severe food reactions in Sweden is soy protein an underestimated cause of food anaphylaxis
    • Foucard, T., and Malmheden-Yman, I. 1999. A study on severe food reactions in Sweden is soy protein an underestimated cause of food anaphylaxis. Allergy, 53(3):261-265.
    • (1999) Allergy , vol.53 , Issue.3 , pp. 261-265
    • Foucard, T.1    Malmheden-Yman, I.2
  • 11
    • 0012943358 scopus 로고
    • Anaphylaxis following ingestion of soybean
    • Mortimer, E.Z. 1961. Anaphylaxis following ingestion of soybean. Pediatr., 58:90-92.
    • (1961) Pediatr , vol.58 , pp. 90-92
    • Mortimer, E.Z.1
  • 17
    • 5544322062 scopus 로고    scopus 로고
    • Here, there and everywhere: Allergen detection and labelling-scientific and regulatory issues
    • Popping, B., Waiblinger, H.U., and Holzhauser, T. 2004. Here, there and everywhere: allergen detection and labelling-scientific and regulatory issues. Inform., 15(9):620-621.
    • (2004) Inform , vol.15 , Issue.9 , pp. 620-621
    • Popping, B.1    Waiblinger, H.U.2    Holzhauser, T.3
  • 18
    • 0022181087 scopus 로고
    • Food hypersensitivity and atopic dermatitis evaluation of 113 patients
    • Sampson, H.A., and McCaskill, C.C. 1985. Food hypersensitivity and atopic dermatitis evaluation of 113 patients. J. Pediatrics, 107(5):669-675.
    • (1985) J. Pediatrics , vol.107 , Issue.5 , pp. 669-675
    • Sampson, H.A.1    McCaskill, C.C.2
  • 19
    • 0008584767 scopus 로고
    • Identification and comparison of differences in antigens in two commercially available soybean protein isolates
    • Burks, A.W., Butler, H.L., Brooks, J.R., Hardin, J., and Connaughton, C. 1988. Identification and comparison of differences in antigens in two commercially available soybean protein isolates. J. Food Sci., 53(5): 1456-1459.
    • (1988) J. Food Sci , vol.53 , Issue.5 , pp. 1456-1459
    • Burks, A.W.1    Butler, H.L.2    Brooks, J.R.3    Hardin, J.4    Connaughton, C.5
  • 20
    • 0026310544 scopus 로고
    • Investigation of the Ig binding proteins in soybeans by immunoblotting with the sera of the soybean-sensitive patients with atopic dermatitis
    • Ogawa,T.,Bando,N.,Tsuji,H.,Okajima, K.,Nishikawa, K., and Sasaoka, K. 1991. Investigation of the Ig binding proteins in soybeans by immunoblotting with the sera of the soybean-sensitive patients with atopic dermatitis. J. Nutr. Sci. Vitaminol., 37(6):555-565.
    • (1991) J. Nutr. Sci. Vitaminol , vol.37 , Issue.6 , pp. 555-565
    • Ogawa, T.1    Bando, N.2    Tsuji, H.3    Okajima, K.4    Nishikawa, K.5    Sasaoka, K.6
  • 21
    • 0030035304 scopus 로고    scopus 로고
    • Lalles, J.P., and Peltre, G. 1991. Biochemical features of grain legume allergens in humans and animals. Nutr. Rev., 54(4/Part I):101-107.
    • Lalles, J.P., and Peltre, G. 1991. Biochemical features of grain legume allergens in humans and animals. Nutr. Rev., 54(4/Part I):101-107.
  • 22
    • 0002565175 scopus 로고    scopus 로고
    • Allergen Data collection update: Soybean (glycine max)
    • Besler, M., Helm, R.M., and Ogawa, T. 1999. Allergen Data collection update: soybean (glycine max). Internet Symposium on Food Allergens, 2(suppl 3):1-35.
    • (1999) Internet Symposium on Food Allergens , vol.2 , Issue.SUPPL. 3 , pp. 1-35
    • Besler, M.1    Helm, R.M.2    Ogawa, T.3
  • 23
    • 0034526947 scopus 로고    scopus 로고
    • Soybean allergens and hypoallergenic soybean products
    • Ogawa, T., Samoto, M., and Takahashi, K. 2000. Soybean allergens and hypoallergenic soybean products. J. Nutr. Sci. Vitaminol., 46(6):271-279.
    • (2000) J. Nutr. Sci. Vitaminol , vol.46 , Issue.6 , pp. 271-279
    • Ogawa, T.1    Samoto, M.2    Takahashi, K.3
  • 24
    • 0017019007 scopus 로고
    • Major proteins of soybean seeds: A straight forward fraction and their characterization
    • Thanh, V.H., and Shibasaki, K. 1976. Major proteins of soybean seeds: A straight forward fraction and their characterization. J. Agric. Food. Chem., 24(6):1117-1121.
    • (1976) J. Agric. Food. Chem , vol.24 , Issue.6 , pp. 1117-1121
    • Thanh, V.H.1    Shibasaki, K.2
  • 25
    • 33847266108 scopus 로고    scopus 로고
    • Howard, P.A, Lehnhardt, W.F, and Orthoefer, F.T. 1983. 7S, and 11S vegetable protein traction and isolation. US Patent, No. 4,368,151
    • Howard, P.A., Lehnhardt, W.F., and Orthoefer, F.T. 1983. 7S, and 11S vegetable protein traction and isolation. US Patent, No. 4,368,151.
  • 26
    • 33847306740 scopus 로고    scopus 로고
    • Nielson, N.C. 1985. Structure of soy proteins. In: Altschul, A.M., and Wilcke, H.L. Eds., New Protein Food, 5. Seed Storage Proteins. Orlando: Academic Press, 27-64.
    • Nielson, N.C. 1985. Structure of soy proteins. In: Altschul, A.M., and Wilcke, H.L. Eds., New Protein Food, Vol. 5. Seed Storage Proteins. Orlando: Academic Press, 27-64.
  • 27
    • 0000997835 scopus 로고
    • Crystalllization of a trypsin inhibitor from soybeans
    • Kunitz, M. 1945. Crystalllization of a trypsin inhibitor from soybeans. Science, 101:668-669.
    • (1945) Science , vol.101 , pp. 668-669
    • Kunitz, M.1
  • 28
    • 0000835443 scopus 로고
    • Degradation of β-conglycinin in early stages of soybean embryogenesis
    • Shattuck-Eidens, D.N., and Beachy, R.N. 1985. Degradation of β-conglycinin in early stages of soybean embryogenesis. Plant Physiol., 78:895.
    • (1985) Plant Physiol , vol.78 , pp. 895
    • Shattuck-Eidens, D.N.1    Beachy, R.N.2
  • 30
    • 0030151307 scopus 로고    scopus 로고
    • Purification, characterization and christallization of single molecular species of β-conglycinin from soybean seeds
    • Morita, S., Fukase, M., Yamaguchi, M., Fukuda, Y., and Morita, Y. 1996. Purification, characterization and christallization of single molecular species of β-conglycinin from soybean seeds. Biosci. Biotechnol. Biochem., 60(5):866-873.
    • (1996) Biosci. Biotechnol. Biochem , vol.60 , Issue.5 , pp. 866-873
    • Morita, S.1    Fukase, M.2    Yamaguchi, M.3    Fukuda, Y.4    Morita, Y.5
  • 31
    • 0002830551 scopus 로고
    • Structure and location of legume and cereal seed storage proteins
    • Daussant, J, Mosse, J, and Vaughan, J, Eds, London: Academic Press
    • Pernollet, J.C., and Mosses, J. 1983. Structure and location of legume and cereal seed storage proteins. In: Daussant, J., Mosse, J., and Vaughan, J., Eds., Seeds Proteins. Annual Proceedings of the Phytochemical Society of Europe. London: Academic Press, 155-190.
    • (1983) Seeds Proteins. Annual Proceedings of the Phytochemical Society of Europe , pp. 155-190
    • Pernollet, J.C.1    Mosses, J.2
  • 32
    • 0001390643 scopus 로고
    • Major proteins of soybean seeds. Reversible and irreversible dissociation of β-conglycinin
    • Thanh, V.H., and Shibasaki, K. 1979. Major proteins of soybean seeds. Reversible and irreversible dissociation of β-conglycinin. J. Agric. Food Chem., 27(4):805-809.
    • (1979) J. Agric. Food Chem , vol.27 , Issue.4 , pp. 805-809
    • Thanh, V.H.1    Shibasaki, K.2
  • 33
    • 0001493386 scopus 로고
    • Varietal and environmental differences in soybean glycinin and β-conglycinin concentration
    • Murphy, P.A., and Resurrection, A.P. 1984. Varietal and environmental differences in soybean glycinin and β-conglycinin concentration. J. Agric. Food. Chem., 32:911.
    • (1984) J. Agric. Food. Chem , vol.32 , pp. 911
    • Murphy, P.A.1    Resurrection, A.P.2
  • 34
    • 0009783937 scopus 로고
    • Two-dimensional electrophoretic analysis of the protein of isolated soybean bodies and of the glycosylation of soybean proteins
    • Lei, M.G., and Reeck, G.R. 1987. Two-dimensional electrophoretic analysis of the protein of isolated soybean bodies and of the glycosylation of soybean proteins. J. Agric, Food. Chem., 35:296-300.
    • (1987) J. Agric, Food. Chem , vol.35 , pp. 296-300
    • Lei, M.G.1    Reeck, G.R.2
  • 35
    • 0018787396 scopus 로고
    • Partial characterization of the acidic and basic polypeptides of glycinin
    • Moreira, M.A., Hermodson, M.A., Larkins, B.A., and Nielson, N.C. 1979. Partial characterization of the acidic and basic polypeptides of glycinin. J. Biol. Chem., 254:9921-9926.
    • (1979) J. Biol. Chem , vol.254 , pp. 9921-9926
    • Moreira, M.A.1    Hermodson, M.A.2    Larkins, B.A.3    Nielson, N.C.4
  • 36
    • 0019888351 scopus 로고
    • Identification of the acidic and basic subunit complexes of glycinin
    • Staswick, P.E., Hermodson, M.A., and Nielson, N.C. 1981. Identification of the acidic and basic subunit complexes of glycinin. J. Biol. Chem., 256:8752-8755.
    • (1981) J. Biol. Chem , vol.256 , pp. 8752-8755
    • Staswick, P.E.1    Hermodson, M.A.2    Nielson, N.C.3
  • 38
    • 0032873808 scopus 로고    scopus 로고
    • Analysis of the distribution of the major soybean seed allergens in a core collection of Glycine max accessions
    • Yaklich, R.W., Helm, R.M., Cockrell, G., and Herman, E.M. 1999. Analysis of the distribution of the major soybean seed allergens in a core collection of Glycine max accessions. Crop Science, 39(5):1444-1447.
    • (1999) Crop Science , vol.39 , Issue.5 , pp. 1444-1447
    • Yaklich, R.W.1    Helm, R.M.2    Cockrell, G.3    Herman, E.M.4
  • 39
    • 0027620748 scopus 로고
    • Identification of the soybean allergenic protein, Gly m Bd 30 K, with the soybean seed 34-kDa oil-body-associated protein Biosci
    • Ogawa, T., Bando, N., Tsuji, H., Nishikawa, K., and Kitamura, K. 1993. Identification of the soybean allergenic protein, Gly m Bd 30 K, with the soybean seed 34-kDa oil-body-associated protein Biosci. Biotechnol. Biochem., 57(6):1030-1033
    • (1993) Biotechnol. Biochem , vol.57 , Issue.6 , pp. 1030-1033
    • Ogawa, T.1    Bando, N.2    Tsuji, H.3    Nishikawa, K.4    Kitamura, K.5
  • 41
    • 0000965330 scopus 로고
    • Apparent processing of a soybean oil body protein accompanies the onset of oil mobilization
    • Herman, E.M., Melroy, D.L., and Buckhout, T.J. 1990. Apparent processing of a soybean oil body protein accompanies the onset of oil mobilization. Plant Physiol., 94:341-349.
    • (1990) Plant Physiol , vol.94 , pp. 341-349
    • Herman, E.M.1    Melroy, D.L.2    Buckhout, T.J.3
  • 42
    • 0026793590 scopus 로고
    • Purification and characterization of major inhalant allergens from soybean hulls
    • Gonzalez, R., Polo, F., Zapatero, L., Caravaca, F., and Carreira, J. 1992. Purification and characterization of major inhalant allergens from soybean hulls. Cli. Exp. Allergy, 22:748-755.
    • (1992) Cli. Exp. Allergy , vol.22 , pp. 748-755
    • Gonzalez, R.1    Polo, F.2    Zapatero, L.3    Caravaca, F.4    Carreira, J.5
  • 43
    • 0029055249 scopus 로고
    • Soybean hydrophobic protein and soybean hull allergy
    • Gonzalez, R., Varela, J., Carreira, J., and Polo, F. 1995. Soybean hydrophobic protein and soybean hull allergy. Lancet, 346:48-49.
    • (1995) Lancet , vol.346 , pp. 48-49
    • Gonzalez, R.1    Varela, J.2    Carreira, J.3    Polo, F.4
  • 44
    • 85007881885 scopus 로고
    • α-Subunit of β-conglycinin, an allergenic protein recognised by IgE antibodies of soybean-sensitive patients with atopic dermatitis
    • Ogawa, T., Bando, N., Tsuji, H., Nishikawa, K., and Kitamura, K. 1995. α-Subunit of β-conglycinin, an allergenic protein recognised by IgE antibodies of soybean-sensitive patients with atopic dermatitis. Biosci. Biotechnol. Biochem., 59(5):831-833.
    • (1995) Biosci. Biotechnol. Biochem , vol.59 , Issue.5 , pp. 831-833
    • Ogawa, T.1    Bando, N.2    Tsuji, H.3    Nishikawa, K.4    Kitamura, K.5
  • 45
    • 0034501229 scopus 로고    scopus 로고
    • Soybean glycinin Gl acidic chain shares IgE epitopes with peanut allergen Ara h 3
    • Beardslee, T.A., Zeece, M.G., Sarath, G., and Markwell, J.P. 2000. Soybean glycinin Gl acidic chain shares IgE epitopes with peanut allergen Ara h 3. Int. Arch. Allergy Immunol., 123(4):299-307.
    • (2000) Int. Arch. Allergy Immunol , vol.123 , Issue.4 , pp. 299-307
    • Beardslee, T.A.1    Zeece, M.G.2    Sarath, G.3    Markwell, J.P.4
  • 47
    • 0033822839 scopus 로고    scopus 로고
    • Occurrence of IgE antibody-recognizing N-linked glycan moiety of a soybean allergen, Gly m Bd 28 K
    • Hiemori, M., Bando, N., Ogawa, T., Shimada, H., Tsuji, H., Yamanishi, R., and Terao, J. 2000. Occurrence of IgE antibody-recognizing N-linked glycan moiety of a soybean allergen, Gly m Bd 28 K. Int. Arch. Allergy Immunol., 122(4):238-245.
    • (2000) Int. Arch. Allergy Immunol , vol.122 , Issue.4 , pp. 238-245
    • Hiemori, M.1    Bando, N.2    Ogawa, T.3    Shimada, H.4    Tsuji, H.5    Yamanishi, R.6    Terao, J.7
  • 49
    • 0000988512 scopus 로고
    • Antigenic and allergenic properties of acidic and basic peptide chains from glycinin
    • Pedersen, H.S., and Djurtoft, R. 1989. Antigenic and allergenic properties of acidic and basic peptide chains from glycinin. Food Agric. Immunol., 1(2): 101-109.
    • (1989) Food Agric. Immunol , vol.1 , Issue.2 , pp. 101-109
    • Pedersen, H.S.1    Djurtoft, R.2
  • 51
    • 0032901766 scopus 로고    scopus 로고
    • Identification of an IgE-binding region in soybean acidic glycinin G1
    • Zeece, M.G., Beardslee, T.A., Markwell, J.P, and Sarath, G., 1999. Identification of an IgE-binding region in soybean acidic glycinin G1. Food Agric. Immunol., 11(1):83-90.
    • (1999) Food Agric. Immunol , vol.11 , Issue.1 , pp. 83-90
    • Zeece, M.G.1    Beardslee, T.A.2    Markwell, J.P.3    Sarath, G.4
  • 53
    • 0036462292 scopus 로고    scopus 로고
    • Identification and analysis of a conserved immunoglobulin E-binding epitope in soybean G1a and G2a and peanut Ara h 3 glycinins
    • Xiang,P.,Beardslee,T.A.,Zeece,M.G.,Markwell,J., and Sarath,G. 2002. Identification and analysis of a conserved immunoglobulin E-binding epitope in soybean G1a and G2a and peanut Ara h 3 glycinins. Arch. Biochem. Biophys., 408(1):51-57.
    • (2002) Arch. Biochem. Biophys , vol.408 , Issue.1 , pp. 51-57
    • Xiang, P.1    Beardslee, T.A.2    Zeece, M.G.3    Markwell, J.4    Sarath, G.5
  • 55
    • 0001123162 scopus 로고
    • Soybean as a possible important source of allergy
    • Duke, W.W. 1934. Soybean as a possible important source of allergy. J. Allergy, 5:300-305.
    • (1934) J. Allergy , vol.5 , pp. 300-305
    • Duke, W.W.1
  • 56
    • 0018890096 scopus 로고
    • Kunitz soybean trypsin inhibitor: A specific allergen in food anaphylaxis
    • Moroz, L.A., and Yang, W.H. 1980. Kunitz soybean trypsin inhibitor: a specific allergen in food anaphylaxis. N. Engl. J. Med., 302:1126-1128.
    • (1980) N. Engl. J. Med , vol.302 , pp. 1126-1128
    • Moroz, L.A.1    Yang, W.H.2
  • 57
    • 0030035396 scopus 로고    scopus 로고
    • Characterization of soybean allergens causing sensitization of occupationally exposed bakers
    • Baur, X., Pau, M., Czuppon, A., and Fruhmann, G. 1996. Characterization of soybean allergens causing sensitization of occupationally exposed bakers. Allergy, 51(5):326-330.
    • (1996) Allergy , vol.51 , Issue.5 , pp. 326-330
    • Baur, X.1    Pau, M.2    Czuppon, A.3    Fruhmann, G.4
  • 59
    • 0030995891 scopus 로고    scopus 로고
    • Purification and characterization of a soybean hull allergen responsible for the Barcelona asthma outbreaks. II. Purification and sequencing of the Gly m 2 allergen
    • Codina, R., Lockey, R.F., Fernandez-Caldas, E., and Rama, R. 1997. Purification and characterization of a soybean hull allergen responsible for the Barcelona asthma outbreaks. II. Purification and sequencing of the Gly m 2 allergen. Clin. Exp. Allergy, 27(4):424-430.
    • (1997) Clin. Exp. Allergy , vol.27 , Issue.4 , pp. 424-430
    • Codina, R.1    Lockey, R.F.2    Fernandez-Caldas, E.3    Rama, R.4
  • 60
    • 0032911738 scopus 로고    scopus 로고
    • Identification of the soybean hull allergens responsible for the Barcelona asthma outbreaks
    • Codina, R., Lockey, R.F., Fernandez-Caldas, E., and Rama, R. 1999. Identification of the soybean hull allergens responsible for the Barcelona asthma outbreaks. International Arch. Allergy Immunol., 119:69-71.
    • (1999) International Arch. Allergy Immunol , vol.119 , pp. 69-71
    • Codina, R.1    Lockey, R.F.2    Fernandez-Caldas, E.3    Rama, R.4
  • 61
    • 0013083082 scopus 로고    scopus 로고
    • Occupational asthma caused by soybean flour in bakers -difference with soybean-induced epidemic asthma
    • Quirce, S., Polo, F., Figueredo, E., Gonzalez, R., and Sastre, J. 2000. Occupational asthma caused by soybean flour in bakers -difference with soybean-induced epidemic asthma. Clin. Exp. Allergy, 30(6):839- 846.
    • (2000) Clin. Exp. Allergy , vol.30 , Issue.6 , pp. 839-846
    • Quirce, S.1    Polo, F.2    Figueredo, E.3    Gonzalez, R.4    Sastre, J.5
  • 62
    • 0033435099 scopus 로고    scopus 로고
    • IgE binding of the recombinant allergen soybean profilin (rGly m 3) is mediated by conformational epitopes
    • Rihs, H.P., Chen, Z., Rueff, F., Petersen, A., Rozynek, P., Heimann, H., and Baur, X. 1999. IgE binding of the recombinant allergen soybean profilin (rGly m 3) is mediated by conformational epitopes. J. Allergy Clin. Immunol., 104(6):1293-1301.
    • (1999) J. Allergy Clin. Immunol , vol.104 , Issue.6 , pp. 1293-1301
    • Rihs, H.P.1    Chen, Z.2    Rueff, F.3    Petersen, A.4    Rozynek, P.5    Heimann, H.6    Baur, X.7
  • 63
    • 0026810238 scopus 로고
    • Characterization of a stress-induced, developmentally regulated gene family from soybean
    • Crowell, D.N., John, M.E., Russell, D., and Amasino, R.M. 1992. Characterization of a stress-induced, developmentally regulated gene family from soybean. Plant Mol Biol., 18:459-466.
    • (1992) Plant Mol Biol , vol.18 , pp. 459-466
    • Crowell, D.N.1    John, M.E.2    Russell, D.3    Amasino, R.M.4
  • 64
    • 0036858612 scopus 로고    scopus 로고
    • Severe oral allergy syndrome and anaphylactic reactions caused by a Bet v 1- related PR-10 protein in soybean, SAM22
    • Kleine-Tebbe, J., Vogel, L., Crowell, D.N., Haustein, U.F., and Vieths, S. 2002. Severe oral allergy syndrome and anaphylactic reactions caused by a Bet v 1- related PR-10 protein in soybean, SAM22. J. Allergy Clin. Immunol., 110(5):797-804.
    • (2002) J. Allergy Clin. Immunol , vol.110 , Issue.5 , pp. 797-804
    • Kleine-Tebbe, J.1    Vogel, L.2    Crowell, D.N.3    Haustein, U.F.4    Vieths, S.5
  • 65
    • 0038663157 scopus 로고    scopus 로고
    • Sequence-specific 1H, 13C and 15N resonance assignments of SAM22, an allergenic stress-induced protein from soy bean
    • Neudecker, P., Lehmann, K., and Rosch, P. 2003. Sequence-specific 1H, 13C and 15N resonance assignments of SAM22, an allergenic stress-induced protein from soy bean. J. biomol. AMR., 26(2):191-192.
    • (2003) J. biomol. AMR , vol.26 , Issue.2 , pp. 191-192
    • Neudecker, P.1    Lehmann, K.2    Rosch, P.3
  • 67
    • 0342813367 scopus 로고    scopus 로고
    • Comparison of human IgE-binding soya bean allergenic protein Gly m 1 with the antigenicity profiles of calf anti-soya protein sera
    • Hessing, M., Bleeker, H., Tsuji, H., Ogawa, T., and Vlooswijk, R.A.A. 1996. Comparison of human IgE-binding soya bean allergenic protein Gly m 1 with the antigenicity profiles of calf anti-soya protein sera. Food Agric. Immunol., 8(1):51-58.
    • (1996) Food Agric. Immunol , vol.8 , Issue.1 , pp. 51-58
    • Hessing, M.1    Bleeker, H.2    Tsuji, H.3    Ogawa, T.4    Vlooswijk, R.A.A.5
  • 68
    • 0035987324 scopus 로고    scopus 로고
    • Identification of the soybean hull allergens involved in sensitization to soybean dust in a rural population from Argentina and N-terminal sequence of a major 50 KD allergen
    • Codina, R., Ardusso, L. Lockey, R.E, Crisci, C.D., Jaen, C., and Bertoya, N.H. 2002. Identification of the soybean hull allergens involved in sensitization to soybean dust in a rural population from Argentina and N-terminal sequence of a major 50 KD allergen. Clin. Exp. Allergy., 32(7):1059-1063.
    • (2002) Clin. Exp. Allergy , vol.32 , Issue.7 , pp. 1059-1063
    • Codina, R.1    Ardusso, L.2    Lockey, R.E.3    Crisci, C.D.4    Jaen, C.5    Bertoya, N.H.6
  • 69
    • 0015510673 scopus 로고
    • Lectins: Cell-agglutinating and sugar-specific proteins
    • Sharon, N., and Lis, H. 1972. Lectins: cell-agglutinating and sugar-specific proteins. Science, 177:949-959.
    • (1972) Science , vol.177 , pp. 949-959
    • Sharon, N.1    Lis, H.2
  • 70
    • 0023627524 scopus 로고
    • Lectins and the radioallergosorbent test
    • Barnett, D., and Howden, M.E. 1987. Lectins and the radioallergosorbent test. J. Allergy Clin Immunol., 80(4):558-561.
    • (1987) J. Allergy Clin Immunol , vol.80 , Issue.4 , pp. 558-561
    • Barnett, D.1    Howden, M.E.2
  • 71
    • 1542580602 scopus 로고    scopus 로고
    • Hessing, M., Bleeker, H., van Biert, R., Sleijsters Selis, H., van Duijn, G., van Westerop.H., and Vlooswijk, R.A.A. 1995. Analysis of proteinaceous antinutritional compounds in soya oilseed products. In: Immunoassays for Residue Analysis: Food Safety: Proceedings of a Symposium. Washington D.C.: ACS Anaheim, April 1995, 219-230.
    • Hessing, M., Bleeker, H., van Biert, R., Sleijsters Selis, H., van Duijn, G., van Westerop.H., and Vlooswijk, R.A.A. 1995. Analysis of proteinaceous antinutritional compounds in soya oilseed products. In: Immunoassays for Residue Analysis: Food Safety: Proceedings of a Symposium. Washington D.C.: ACS Anaheim, April 1995, 219-230.
  • 72
    • 33847253734 scopus 로고    scopus 로고
    • Plant food protein allergens: The role of structure and function in allergenic potential
    • Mills, E.N.C., Madsen, C., Shewry, P.R., and Wichers, H.J. 2001. Plant food protein allergens: the role of structure and function in allergenic potential. Food Allergy and Intolerance, 32:194-209.
    • (2001) Food Allergy and Intolerance , vol.32 , pp. 194-209
    • Mills, E.N.C.1    Madsen, C.2    Shewry, P.R.3    Wichers, H.J.4
  • 73
    • 33847260025 scopus 로고    scopus 로고
    • Dietary lectins and disease
    • 2nd ed, London: Saunders Publishers
    • Freed, D.L.J. 2002. Dietary lectins and disease. In: Food Allergy and Intolerance, 2nd ed., London: Saunders Publishers, 479-495.
    • (2002) Food Allergy and Intolerance , pp. 479-495
    • Freed, D.L.J.1
  • 74
    • 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., and Hatzos, C. 2002. Digestibility of food allergens and nonallergenic proteins in simulated gastric fluid and simulated intestinal fluid-a comparative study. J. Agric. Food Chem., 50(24):7154-7160.
    • (2002) J. Agric. Food Chem , vol.50 , Issue.24 , pp. 7154-7160
    • Fu, T.J.1    Abbott, U.R.2    Hatzos, C.3
  • 75
    • 0026764006 scopus 로고
    • Interaction of lectins with human IgE: IgE binding property and histamine-releasing activity of twelve plant lectins
    • Shibasaki, M., Sumazaki, R., Isoyama, S., and Takita, H. 1992. Interaction of lectins with human IgE: IgE binding property and histamine-releasing activity of twelve plant lectins. Int. Arch. Allergy Immunol., 98:18-25.
    • (1992) Int. Arch. Allergy Immunol , vol.98 , pp. 18-25
    • Shibasaki, M.1    Sumazaki, R.2    Isoyama, S.3    Takita, H.4
  • 80
    • 33847334903 scopus 로고    scopus 로고
    • Unknown. 2005. Soy oil helps shape food allergen labelling rules. In: http://www.newswise.com/articles/view/511384.
    • Unknown. 2005. Soy oil helps shape food allergen labelling rules. In: http://www.newswise.com/articles/view/511384.
  • 83
    • 0025241366 scopus 로고
    • Identification of soybean allergens by immunoblotting with sera from soy-allergic adults
    • Herian, A.M., Taylor, S.L., and Bush, R.K. 1990. Identification of soybean allergens by immunoblotting with sera from soy-allergic adults. Int. Arch. Allergy Appl. Immunol., 92:193-198.
    • (1990) Int. Arch. Allergy Appl. Immunol , vol.92 , pp. 193-198
    • Herian, A.M.1    Taylor, S.L.2    Bush, R.K.3
  • 84
    • 0014970663 scopus 로고
    • Studies on the allergenicity of soy bean
    • Fries, J.H. 1971. Studies on the allergenicity of soy bean. Ann. Allergy, 29:1-7.
    • (1971) Ann. Allergy , vol.29 , pp. 1-7
    • Fries, J.H.1
  • 85
    • 0024549931 scopus 로고
    • Cross-allergenicity in the legume botanical family in children with food hypersensitivity
    • Bernhisel-Broadbent, J., and Sampson, H.A. 1989. Cross-allergenicity in the legume botanical family in children with food hypersensitivity. J. Allergy Clin. Immunol., 83:435-440.
    • (1989) J. Allergy Clin. Immunol , vol.83 , pp. 435-440
    • Bernhisel-Broadbent, J.1    Sampson, H.A.2
  • 86
    • 0029853742 scopus 로고    scopus 로고
    • Identification of unique peanut and soy allergens in sera adsorbed with cross-reacting antibodies
    • Eigenmann., P.A, Burks, A.W., Bannon, G.A., and Sampson, H.A. 1996. Identification of unique peanut and soy allergens in sera adsorbed with cross-reacting antibodies. J. Allergy Clin. Immunol., 98:969-978.
    • (1996) J. Allergy Clin. Immunol , vol.98 , pp. 969-978
    • Eigenmann, P.A.1    Burks, A.W.2    Bannon, G.A.3    Sampson, H.A.4
  • 87
    • 0034067401 scopus 로고    scopus 로고
    • Peanut and soy allergy: A clinical and therapeutic dilemma
    • Sicherer, S.H., Sampson, H.A., and Burks, A.W. 2000. Peanut and soy allergy: a clinical and therapeutic dilemma. Allergy, 55:515-521.
    • (2000) Allergy , vol.55 , pp. 515-521
    • Sicherer, S.H.1    Sampson, H.A.2    Burks, A.W.3
  • 88
    • 0023891803 scopus 로고
    • Allergenicity of major component proteins of soybean determined by enzyme-linked immunosorbent assay (ELISA) and immunoblotting in children with atopic dermatitis and positive soy challenges
    • Burks, A.W., Brooks, J.R., and Sampson, H.A. 1988. Allergenicity of major component proteins of soybean determined by enzyme-linked immunosorbent assay (ELISA) and immunoblotting in children with atopic dermatitis and positive soy challenges. J. Allergy Clin. Immunol., 11:1135-1142.
    • (1988) J. Allergy Clin. Immunol , vol.11 , pp. 1135-1142
    • Burks, A.W.1    Brooks, J.R.2    Sampson, H.A.3
  • 90
    • 0025085949 scopus 로고
    • A prospective study of cow milk allergy in Danish infants during the first 3 years of life. Clinical course in relation to clinical and immunological type of hypersensitivity reaction
    • Host, A., and Halken, S. 1990. A prospective study of cow milk allergy in Danish infants during the first 3 years of life. Clinical course in relation to clinical and immunological type of hypersensitivity reaction. Allergy, 45:587-596.
    • (1990) Allergy , vol.45 , pp. 587-596
    • Host, A.1    Halken, S.2
  • 91
    • 0028324453 scopus 로고
    • Prospective oral food challenge study of two soybean protein isolates in patients with possible milk or soy protein enterocolitis
    • Burks, A.W., Casteel, H.B., Fiedorek, S.C., Williams, L.W., and Pumphrey, C.L. 1994. Prospective oral food challenge study of two soybean protein isolates in patients with possible milk or soy protein enterocolitis. Pediatr. Allergy Immunol., 5:40-45.
    • (1994) Pediatr. Allergy Immunol , vol.5 , pp. 40-45
    • Burks, A.W.1    Casteel, H.B.2    Fiedorek, S.C.3    Williams, L.W.4    Pumphrey, C.L.5
  • 92
    • 0030731390 scopus 로고    scopus 로고
    • Natural history of soy allergy and/or intolerance in children, and clinical use of soy-protein formulas
    • Cantani, A., and Lucenti, P. 1997. Natural history of soy allergy and/or intolerance in children, and clinical use of soy-protein formulas. Pediatr. Allergy Immunol., 8:59-74.
    • (1997) Pediatr. Allergy Immunol , vol.8 , pp. 59-74
    • Cantani, A.1    Lucenti, P.2
  • 93
    • 0036378387 scopus 로고    scopus 로고
    • Detection and identification of a soy protein component that cross-reacts with caseins from cow's milk
    • Rozenfeld, P., Docena, G.H., Anon, M.C., and Fossati, C.A. 2002. Detection and identification of a soy protein component that cross-reacts with caseins from cow's milk. Clin. Exp. Immunol., 130:49-58.
    • (2002) Clin. Exp. Immunol , vol.130 , pp. 49-58
    • Rozenfeld, P.1    Docena, G.H.2    Anon, M.C.3    Fossati, C.A.4
  • 94
    • 0033484339 scopus 로고    scopus 로고
    • Recognition of allergenic structures in 'novel' food
    • Wal, J.M. 1999. Recognition of allergenic structures in 'novel' food. Sciences des Aliments, 19(3/4):409-22.
    • (1999) Sciences des Aliments , vol.19 , Issue.3-4 , pp. 409-422
    • Wal, J.M.1
  • 95
    • 2342525840 scopus 로고    scopus 로고
    • Classification of plant food allergens
    • Breiteneder, H., and Radauer, C.A. 2004. Classification of plant food allergens. J. Allergy Clin. Immunol., 113(5):821-830.
    • (2004) J. Allergy Clin. Immunol , vol.113 , Issue.5 , pp. 821-830
    • Breiteneder, H.1    Radauer, C.A.2
  • 96
    • 85007940400 scopus 로고
    • Crystallization and preliminary X-ray analysis of soybean proglycinins modified by protein engineering
    • Gidamis, A.B., Mikami, B., Katsube, T., Utsumi, S., and Kito, M. 1994. Crystallization and preliminary X-ray analysis of soybean proglycinins modified by protein engineering. Biosci. Biotechnol Biochem., 58(4):703- 706.
    • (1994) Biosci. Biotechnol Biochem , vol.58 , Issue.4 , pp. 703-706
    • Gidamis, A.B.1    Mikami, B.2    Katsube, T.3    Utsumi, S.4    Kito, M.5
  • 97
    • 0027507539 scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of the soybean proglycinin expressed in Escherichia coli
    • Utsumi, S., Gidamis, A.B., Mikami, B., and Kito, M. 1993. Crystallization and preliminary X-ray crystallographic analysis of the soybean proglycinin expressed in Escherichia coli J. Mol. Biol., 233(1):177-178.
    • (1993) J. Mol. Biol , vol.233 , Issue.1 , pp. 177-178
    • Utsumi, S.1    Gidamis, A.B.2    Mikami, B.3    Kito, M.4
  • 98
    • 0035847055 scopus 로고    scopus 로고
    • Crystal structure of soybean proglycinin A1aB1b homotrimer
    • Adachi, M., Takenaka, Y., Gidamis, A.B., Mikami, B., and Utsumi, S. 2001. Crystal structure of soybean proglycinin A1aB1b homotrimer. J. Mol. Biol., 305(2):291-305.
    • (2001) J. Mol. Biol , vol.305 , Issue.2 , pp. 291-305
    • Adachi, M.1    Takenaka, Y.2    Gidamis, A.B.3    Mikami, B.4    Utsumi, S.5
  • 100
    • 0033928258 scopus 로고    scopus 로고
    • Molecular and biochemical classification of plant-derived food allergens
    • Breiteneder, H., and Ebner, C. 2000. Molecular and biochemical classification of plant-derived food allergens. J. Allergy Clin. Immunol., 106:27-36.
    • (2000) J. Allergy Clin. Immunol , vol.106 , pp. 27-36
    • Breiteneder, H.1    Ebner, C.2
  • 101
    • 0027507001 scopus 로고
    • Lipid transfer proteins (LTPs) from barley and maize leaves are potent inhibitors of bacterial and fungal plant pathogens
    • Molina, A., Segura, A., and Garcia-Olmedo, F. 1993. Lipid transfer proteins (LTPs) from barley and maize leaves are potent inhibitors of bacterial and fungal plant pathogens. FEBS Lett., 316:119-122.
    • (1993) FEBS Lett , vol.316 , pp. 119-122
    • Molina, A.1    Segura, A.2    Garcia-Olmedo, F.3
  • 102
    • 0027202271 scopus 로고
    • Crystal structure of hydrophobic protein from soybean; a member of a new cysteine-rich family
    • Baud, F., Pebay-Peyroula, E., Cohen-Addad, C., Odani, S., and Lehmann, M.S. 1993. Crystal structure of hydrophobic protein from soybean; a member of a new cysteine-rich family. J. Mol. Biol., 231(3):877-887.
    • (1993) J. Mol. Biol , vol.231 , Issue.3 , pp. 877-887
    • Baud, F.1    Pebay-Peyroula, E.2    Cohen-Addad, C.3    Odani, S.4    Lehmann, M.S.5
  • 105
    • 0034991489 scopus 로고    scopus 로고
    • Identification of four novel potato (Solanum tuberosum) allergens belonging to the family of soybean trypsin inhibitors
    • Seppala, U., Majamaa, H., Turjanmaa, K., Helin, J.,Reunal,T., Kalkkinen, N., and Palosuo, T. 2001. Identification of four novel potato (Solanum tuberosum) allergens belonging to the family of soybean trypsin inhibitors. Allergy, 56(7):619-626.
    • (2001) Allergy , vol.56 , Issue.7 , pp. 619-626
    • Seppala, U.1    Majamaa, H.2    Turjanmaa, K.3    Helin, J.4    Reunal, T.5    Kalkkinen, N.6    Palosuo, T.7
  • 106
    • 0022004555 scopus 로고
    • Comparative study on amino-acid sequences of Kunitz-type soybean trypsin inhibitors TI-A TI-3 and TI-C
    • Kim, S.H., Hara, S., Hase, S., Ikenaka, T., Toda, H., Kitamura, K., and Kaizuma, N. 1985. Comparative study on amino-acid sequences of Kunitz-type soybean trypsin inhibitors TI-A TI-3 and TI-C. J. Biochem.(Tokyo), 98(2):435-448.
    • (1985) J. Biochem.(Tokyo) , vol.98 , Issue.2 , pp. 435-448
    • Kim, S.H.1    Hara, S.2    Hase, S.3    Ikenaka, T.4    Toda, H.5    Kitamura, K.6    Kaizuma, N.7
  • 107
    • 0032536108 scopus 로고    scopus 로고
    • Kunitz-type soybean trypsin inhibitorre-visited: Refined structure of its complex with porcine trypsin reveals an insight into the interaction between a homologous inhibitor from Erythrina caffra and tissue-type plasminogen activator
    • Song, H.K., and Suh, S.W. 1998. Kunitz-type soybean trypsin inhibitorre-visited: refined structure of its complex with porcine trypsin reveals an insight into the interaction between a homologous inhibitor from Erythrina caffra and tissue-type plasminogen activator. J. Mol. Biol., 275:347-363.
    • (1998) J. Mol. Biol , vol.275 , pp. 347-363
    • Song, H.K.1    Suh, S.W.2
  • 108
  • 111
    • 0033909638 scopus 로고    scopus 로고
    • Plant allergens and pathogenesis-related proteins. What do they have in common?
    • Hoffmann-Sommergruber, K. 2000. Plant allergens and pathogenesis-related proteins. What do they have in common? Int. Arch. Allergy Immunol., 122:155-166.
    • (2000) Int. Arch. Allergy Immunol , vol.122 , pp. 155-166
    • Hoffmann-Sommergruber, K.1
  • 112
    • 0036864268 scopus 로고    scopus 로고
    • Pathogenesis-related (PR)-proteins identified as allergens
    • Hoffmann-Sommergruber, K. 2002. Pathogenesis-related (PR)-proteins identified as allergens. Biochem. Soc. Trans., 30:930-935.
    • (2002) Biochem. Soc. Trans , vol.30 , pp. 930-935
    • Hoffmann-Sommergruber, K.1
  • 113
    • 0024443144 scopus 로고
    • The gene coding for the major birch pollen allergen Bet v 1, is highly homologous to a pea disease resistance response gene
    • Breiteneder, H., Pettenburger, K., Bito, A., Valenta, R., Kraft, D., Rumpold, H., Scheiner, O., and Breitenebach, M. 1989. The gene coding for the major birch pollen allergen Bet v 1, is highly homologous to a pea disease resistance response gene. EMBO J., 8(7):1938-1938.
    • (1989) EMBO J , vol.8 , Issue.7 , pp. 1938-1938
    • Breiteneder, H.1    Pettenburger, K.2    Bito, A.3    Valenta, R.4    Kraft, D.5    Rumpold, H.6    Scheiner, O.7    Breitenebach, M.8
  • 118
    • 84985376691 scopus 로고
    • Determination of soy proteins in food using an enzyme-linked immunosorbent assay procedure
    • Hitchcock, C.H.S., Bailey, F.J., Crimes, A.A., Dean, D.A.G., and Davis, P.J. 1981. Determination of soy proteins in food using an enzyme-linked immunosorbent assay procedure. J. Sci. Food Agric., 32:157-165.
    • (1981) J. Sci. Food Agric , vol.32 , pp. 157-165
    • Hitchcock, C.H.S.1    Bailey, F.J.2    Crimes, A.A.3    Dean, D.A.G.4    Davis, P.J.5
  • 119
    • 84986815060 scopus 로고
    • An assessment of commercially available reagents for an enzyme-linked immunosorbent assay (ELISA) of soy protein in meat products
    • Griffiths, N.M., Billington, M.J., Crimes, A.A., and Hitchcock, C.H.S. 1984. An assessment of commercially available reagents for an enzyme-linked immunosorbent assay (ELISA) of soy protein in meat products. J. Sci. Food Agric., 35:1255-1260.
    • (1984) J. Sci. Food Agric , vol.35 , pp. 1255-1260
    • Griffiths, N.M.1    Billington, M.J.2    Crimes, A.A.3    Hitchcock, C.H.S.4
  • 120
    • 0023334249 scopus 로고
    • Improved enzyme-linked immunosorbent assay for determination of soy protein in meat products
    • Rittenburg, J.H., Adams, A., Palmer, J., and Allen, J.C. 1987. Improved enzyme-linked immunosorbent assay for determination of soy protein in meat products. J. Assoc. Off, Anal. Chem, 70:582-587.
    • (1987) J. Assoc. Off, Anal. Chem , vol.70 , pp. 582-587
    • Rittenburg, J.H.1    Adams, A.2    Palmer, J.3    Allen, J.C.4
  • 121
    • 33847319025 scopus 로고
    • Quantitation of soya protein by enzyme linked immunosorbent assay of its characteristic peptide
    • Yasumuto, K., Sudo, M., and Suzuki, T. 1990. Quantitation of soya protein by enzyme linked immunosorbent assay of its characteristic peptide. J. Sci. Food Agri., 61:19-23.
    • (1990) J. Sci. Food Agri , vol.61 , pp. 19-23
    • Yasumuto, K.1    Sudo, M.2    Suzuki, T.3
  • 122
    • 0023601937 scopus 로고
    • A comparison of the antigenicity of soybean-based infant formulas
    • Heppell, L.M., Sissons, J.W., and Pedersen, H.E. 1987. A comparison of the antigenicity of soybean-based infant formulas. Br. J. Nutr., 58:393-403.
    • (1987) Br. J. Nutr , vol.58 , pp. 393-403
    • Heppell, L.M.1    Sissons, J.W.2    Pedersen, H.E.3
  • 123
    • 0025770572 scopus 로고
    • ELISA analysis of soybean trypsin inhibitors in processed foods
    • Brandon, D.L., Bates, A.H., and Friedman, M. 1991. ELISA analysis of soybean trypsin inhibitors in processed foods. Adv. Exp. Med. Biol., 289:321-337.
    • (1991) Adv. Exp. Med. Biol , vol.289 , pp. 321-337
    • Brandon, D.L.1    Bates, A.H.2    Friedman, M.3
  • 124
    • 0029202586 scopus 로고
    • Measurement of Gly m Bd 30 K, a major soybean allergen, in soybean products by a sandwich enzyme-linked immunosorbent assay
    • Tsuji, H., Okada, N., Yamanishi, R., Bando, N., Kimoto, M., and Ogawa, T. 1995. Measurement of Gly m Bd 30 K, a major soybean allergen, in soybean products by a sandwich enzyme-linked immunosorbent assay. Biosci. Biotechnol. Biochem., 59(1):150-151.
    • (1995) Biosci. Biotechnol. Biochem , vol.59 , Issue.1 , pp. 150-151
    • Tsuji, H.1    Okada, N.2    Yamanishi, R.3    Bando, N.4    Kimoto, M.5    Ogawa, T.6
  • 125
    • 0012104136 scopus 로고    scopus 로고
    • Determination of soy proteins in food products by enzyme immunoassay
    • Yeung, J.M., and Collins, P.G. 1997. Determination of soy proteins in food products by enzyme immunoassay. Food Technol. Biotechnol., 35(3):209-214.
    • (1997) Food Technol. Biotechnol , vol.35 , Issue.3 , pp. 209-214
    • Yeung, J.M.1    Collins, P.G.2
  • 126
    • 0032446544 scopus 로고    scopus 로고
    • Quantitative analysis of Gly m Bd 28 K in soybean products by a sandwich enzyme-linked immunosorbent assay
    • Bando, N., Tsuji,H., Hiemori, M., Yoshizumi, K., Yamanishi, R., Kimoto, M., and Ogawa, T. 1998. Quantitative analysis of Gly m Bd 28 K in soybean products by a sandwich enzyme-linked immunosorbent assay. J. Nutr. Sci. Vitaminol., 44(5):655-664.
    • (1998) J. Nutr. Sci. Vitaminol , vol.44 , Issue.5 , pp. 655-664
    • Bando, N.1    Tsuji, H.2    Hiemori, M.3    Yoshizumi, K.4    Yamanishi, R.5    Kimoto, M.6    Ogawa, T.7
  • 128
    • 0032906962 scopus 로고    scopus 로고
    • Quantification of soy proteins by association of immunochemistry and video image analysis
    • Boutten, B., Humbert, C., Chelbi, M., Durand, P., and Peyraud, D. 1999. Quantification of soy proteins by association of immunochemistry and video image analysis. Food Agric, Immunol., 11:51-59.
    • (1999) Food Agric, Immunol , vol.11 , pp. 51-59
    • Boutten, B.1    Humbert, C.2    Chelbi, M.3    Durand, P.4    Peyraud, D.5
  • 129
    • 0033849340 scopus 로고    scopus 로고
    • Identification of peanut and hazelnut allergens by native two-dimensional gel electrophoresis
    • Hird, H., Pumphrey, R., Wilson, P., Sunderland, J., and Reece, P. 2000. Identification of peanut and hazelnut allergens by native two-dimensional gel electrophoresis. Electrophoresis, 21:2678-2683.
    • (2000) Electrophoresis , vol.21 , pp. 2678-2683
    • Hird, H.1    Pumphrey, R.2    Wilson, P.3    Sunderland, J.4    Reece, P.5
  • 131
    • 33847331457 scopus 로고    scopus 로고
    • Hypoallergenic Foods-Soybeans and peanuts
    • October Issue, 3-5
    • Helm, R.M., Burks, W., and Herman, E. 2002. Hypoallergenic Foods-Soybeans and peanuts. ISB News Report, October Issue, 3-5.
    • (2002) ISB News Report
    • Helm, R.M.1    Burks, W.2    Herman, E.3
  • 133
    • 0027499581 scopus 로고
    • Comment on antigen-reduced infant formulae
    • ESPAGN Committee on Nutrition
    • ESPAGN Committee on Nutrition. 1993. Comment on antigen-reduced infant formulae. Acta Paediatr., 82:314-319.
    • (1993) Acta Paediatr , vol.82 , pp. 314-319
  • 134
    • 0003115052 scopus 로고    scopus 로고
    • Host, A., Koletzko, B., Dreborg, S., Muraro, A., Wahn, U., Aggett, P., Bresson, J.L., Hernell, O., Lafeber, H., Michaelsen, K.F., Micheli, J.L., Rigo, J., Weaver, L., Heymans, H., Strobel, S., and Vandenplas, Y. 1999. Dietary products used in infants for treatment and prevention of food allergy. Joint Statement of the European Society for Paediatric Allergology and Clinical Immunology (ESPACI) Committee on Hypoallergenic Formulas and the European Society for Paediatric Gastroenterology, Hepatology and Nutrition (ESPGHAN) Committee on Nutrition. Arch. Dis. Child, 81(1):80-84.
    • Host, A., Koletzko, B., Dreborg, S., Muraro, A., Wahn, U., Aggett, P., Bresson, J.L., Hernell, O., Lafeber, H., Michaelsen, K.F., Micheli, J.L., Rigo, J., Weaver, L., Heymans, H., Strobel, S., and Vandenplas, Y. 1999. Dietary products used in infants for treatment and prevention of food allergy. Joint Statement of the European Society for Paediatric Allergology and Clinical Immunology (ESPACI) Committee on Hypoallergenic Formulas and the European Society for Paediatric Gastroenterology, Hepatology and Nutrition (ESPGHAN) Committee on Nutrition. Arch. Dis. Child, 81(1):80-84.
  • 137
    • 0027052241 scopus 로고
    • Allergenicity of peanut and soybean extracts altered by chemical or thermal denaturation in patients with atopic der-matitis and positive food challenges
    • Burks, A.W., Williams, L.W., Thresher, W., Connaughton, C., Cockrell, G., and Helm, R.M. 1992. Allergenicity of peanut and soybean extracts altered by chemical or thermal denaturation in patients with atopic der-matitis and positive food challenges. J. Allergy Clin Immunol., 90:889-897.
    • (1992) J. Allergy Clin Immunol , vol.90 , pp. 889-897
    • Burks, A.W.1    Williams, L.W.2    Thresher, W.3    Connaughton, C.4    Cockrell, G.5    Helm, R.M.6
  • 138
    • 0031758168 scopus 로고    scopus 로고
    • Protein modification by thermal processing
    • Davis, P.J., and Williams, S.C. 1998. Protein modification by thermal processing. Allergy, 53(Suppl. 46): 102-105
    • (1998) Allergy , vol.53 , Issue.SUPPL. 46 , pp. 102-105
    • Davis, P.J.1    Williams, S.C.2
  • 139
    • 0033934051 scopus 로고    scopus 로고
    • Heat denaturation of soy glycinin: Influence of pH and ionic strenght on molecular structure
    • Lakemond, C.M.M., De jongh, H.H., Hessing, M., Gruppen, H., and Voragen, A.G.J. 2000. Heat denaturation of soy glycinin: Influence of pH and ionic strenght on molecular structure. J. Agric. Food Chem., 48:1991-1995.
    • (2000) J. Agric. Food Chem , vol.48 , pp. 1991-1995
    • Lakemond, C.M.M.1    De jongh, H.H.2    Hessing, M.3    Gruppen, H.4    Voragen, A.G.J.5
  • 142
    • 0000958919 scopus 로고
    • Allergenic reactivity of various soybean products as determined by RAST inhibition
    • Herian, A.M., Taylor, S.L., and Bush, R.K. 1993. Allergenic reactivity of various soybean products as determined by RAST inhibition. J. Food Sci., 58(2):385-388.
    • (1993) J. Food Sci , vol.58 , Issue.2 , pp. 385-388
    • Herian, A.M.1    Taylor, S.L.2    Bush, R.K.3
  • 143
    • 0001589098 scopus 로고    scopus 로고
    • Fate of major soybean allergen, Gly m Bd 30 K, in rice-, barley-, and soybean-koji miso (fermented soybean paste) during fermentation
    • Tsuji, H., Okada, N., Yamanashi, R., Bando, N., Ebine, H., and Ogawa, T. 1997. Fate of major soybean allergen, Gly m Bd 30 K, in rice-, barley-, and soybean-koji miso (fermented soybean paste) during fermentation. Food Sci. Technol. Int. Tokyo, 3:145-149.
    • (1997) Food Sci. Technol. Int. Tokyo , vol.3 , pp. 145-149
    • Tsuji, H.1    Okada, N.2    Yamanashi, R.3    Bando, N.4    Ebine, H.5    Ogawa, T.6
  • 146
    • 0006597308 scopus 로고    scopus 로고
    • Preparation of hypoallergenic soybean protein with processing functionality by selective enzymatic hydrolysis
    • Tumura, K., Kugimiya, W., Bando, N., Hiemori, M., and Ogawa, T. 1999. Preparation of hypoallergenic soybean protein with processing functionality by selective enzymatic hydrolysis. Food. Sci. Technol. Res., 5:171-175.
    • (1999) Food. Sci. Technol. Res , vol.5 , pp. 171-175
    • Tumura, K.1    Kugimiya, W.2    Bando, N.3    Hiemori, M.4    Ogawa, T.5
  • 147
    • 33847273431 scopus 로고    scopus 로고
    • A new technique to produce hypoallergenic soybean proteins using three differentfermentating microorganisms
    • Lee, J.O., Lee, S.I., Cho, S.H., Oh, C.K., and Ryu, C.H. 2004. A new technique to produce hypoallergenic soybean proteins using three differentfermentating microorganisms. J. Allergy Clin. Immunol., 113(2):S239.
    • (2004) J. Allergy Clin. Immunol , vol.113 , Issue.2
    • Lee, J.O.1    Lee, S.I.2    Cho, S.H.3    Oh, C.K.4    Ryu, C.H.5
  • 148
    • 0036977345 scopus 로고    scopus 로고
    • Cow's milk proteins/Allergens
    • Wal, J.M. 2002. Cow's milk proteins/Allergens. Ann. Allergy Asthma Immunol., 89:3-10.
    • (2002) Ann. Allergy Asthma Immunol , vol.89 , pp. 3-10
    • Wal, J.M.1
  • 149
    • 0032926498 scopus 로고    scopus 로고
    • Outcome of double blind placebo controlled food challenge test in 107 children with atopic dermatitis
    • Niggemann, B., Sielaff, B., Beyer, K., Binder, C., and Wahn, U. 1999. Outcome of double blind placebo controlled food challenge test in 107 children with atopic dermatitis. Clin. Exp. Allergy, 29:91-96.
    • (1999) Clin. Exp. Allergy , vol.29 , pp. 91-96
    • Niggemann, B.1    Sielaff, B.2    Beyer, K.3    Binder, C.4    Wahn, U.5
  • 150
    • 0000016467 scopus 로고    scopus 로고
    • Effect of polysaccharide conjugation or transglutaminase treatment on the allergenicity and functional properties of soy protein
    • Babiker, E.F.E., Hiroyuki, A., Matsudomi, N., Iwata, H., Ogawa, T., Bando, N., and Kato, A. 1998 Effect of polysaccharide conjugation or transglutaminase treatment on the allergenicity and functional properties of soy protein. J. Agric. Food Chem., 46(3):866-871.
    • (1998) J. Agric. Food Chem , vol.46 , Issue.3 , pp. 866-871
    • Babiker, E.F.E.1    Hiroyuki, A.2    Matsudomi, N.3    Iwata, H.4    Ogawa, T.5    Bando, N.6    Kato, A.7
  • 151
    • 1542472256 scopus 로고    scopus 로고
    • Masking of antigen structure of soybean protein by conjugation with polysaccharide and cross-linkage with microbial transglutaminase
    • Babiker, E.F.E, Matsudomi, N., and Kato, A. 1998. Masking of antigen structure of soybean protein by conjugation with polysaccharide and cross-linkage with microbial transglutaminase. Nahrung, 42(3-4):158-159.
    • (1998) Nahrung , vol.42 , Issue.3-4 , pp. 158-159
    • Babiker, E.F.E.1    Matsudomi, N.2    Kato, A.3
  • 152
    • 0034877014 scopus 로고    scopus 로고
    • Effect of chemical and genetic attachment of polysaccharides to proteins on the production of IgG and IgE
    • Arita, K., Babiker, E.E., Azakami, H., and Kato, A. 2001. Effect of chemical and genetic attachment of polysaccharides to proteins on the production of IgG and IgE. J. Agric. Food Chem., 49(4):2030-2036.
    • (2001) J. Agric. Food Chem , vol.49 , Issue.4 , pp. 2030-2036
    • Arita, K.1    Babiker, E.E.2    Azakami, H.3    Kato, A.4
  • 153
    • 1642338134 scopus 로고    scopus 로고
    • Enhanced bactericidal action and masking of allergen structure of soy protein by attachment of chitosan through Maillard-type protein-polysaccharide conjugation
    • Usui, M., Tamura, H., Nakamura, K., Ogawa, T., Muroshita, M., Akazami, H., Kanuma, S., and Kato, A. 2004. Enhanced bactericidal action and masking of allergen structure of soy protein by attachment of chitosan through Maillard-type protein-polysaccharide conjugation. Nahrung/Food, 48(1):69-72.
    • (2004) Nahrung/Food , vol.48 , Issue.1 , pp. 69-72
    • Usui, M.1    Tamura, H.2    Nakamura, K.3    Ogawa, T.4    Muroshita, M.5    Akazami, H.6    Kanuma, S.7    Kato, A.8
  • 154
    • 0029608871 scopus 로고
    • Microbial transglutaminase - A review of its production and application in food processing
    • Zhu, Y., Rinzema, A., Tramper, J., and Bol, J. 1995. Microbial transglutaminase - A review of its production and application in food processing. Appl. Microbiol. Biotechnol., 44(3/4):277-282.
    • (1995) Appl. Microbiol. Biotechnol , vol.44 , Issue.3-4 , pp. 277-282
    • Zhu, Y.1    Rinzema, A.2    Tramper, J.3    Bol, J.4
  • 155
    • 0041744860 scopus 로고    scopus 로고
    • Recent progress in research and technology on soybeans
    • Fukishima, D. 2001. Recent progress in research and technology on soybeans. Food Sci. Technol. Res., 7(1):8-16.
    • (2001) Food Sci. Technol. Res , vol.7 , Issue.1 , pp. 8-16
    • Fukishima, D.1
  • 156
    • 0001446899 scopus 로고
    • Registration of 'Kunitz' soybean
    • Bernard, R., Hymowitz, T., and Cremeens, C.R. 1991. Registration of 'Kunitz' soybean. Crop Sci., 31:232-233.
    • (1991) Crop Sci , vol.31 , pp. 232-233
    • Bernard, R.1    Hymowitz, T.2    Cremeens, C.R.3
  • 157
    • 0027951481 scopus 로고
    • An induced mutant line lacking the a-subunit of β-conglycinin in soybean (Glycine max (L) Merrill)
    • Takahashi, K., Banba, H., Kikuchi, A., Ito, M., and Nakamura, S. 1994. An induced mutant line lacking the a-subunit of β-conglycinin in soybean (Glycine max (L) Merrill). Breeding Sci., 44:65-66.
    • (1994) Breeding Sci , vol.44 , pp. 65-66
    • Takahashi, K.1    Banba, H.2    Kikuchi, A.3    Ito, M.4    Nakamura, S.5
  • 158
    • 0000980420 scopus 로고    scopus 로고
    • Substantially complete removal of three major allergenic soybean proteins (Gly m Bd 30 K, Gly m Bd 28 K, and the α-subunit of conglycinin) from soy protein by using a mutant soybean, Tohoku 124
    • Samoto, M., Fukuda, Y., Takahashi, K., Tabuchi, K., Hiemori, M., Tsuji, H., Ogawa, T., and Kawamura, Y. 1997. Substantially complete removal of three major allergenic soybean proteins (Gly m Bd 30 K, Gly m Bd 28 K, and the α-subunit of conglycinin) from soy protein by using a mutant soybean, Tohoku 124.Biosci. Biotechnol. Biochem., 61(12):2148- 2150.
    • (1997) Biosci. Biotechnol. Biochem , vol.61 , Issue.12 , pp. 2148-2150
    • Samoto, M.1    Fukuda, Y.2    Takahashi, K.3    Tabuchi, K.4    Hiemori, M.5    Tsuji, H.6    Ogawa, T.7    Kawamura, Y.8
  • 159
    • 0032415472 scopus 로고    scopus 로고
    • Dominant inheritance of a trait lacking β-conglycinin detected in wild soybean line
    • Hajika, M., Takahashi, M., Sakai, S., and Matsunaga, R. 1998. Dominant inheritance of a trait lacking β-conglycinin detected in wild soybean line. Breeding Sci., 48:386-386.
    • (1998) Breeding Sci , vol.48 , pp. 386-386
    • Hajika, M.1    Takahashi, M.2    Sakai, S.3    Matsunaga, R.4
  • 162
    • 0038523728 scopus 로고    scopus 로고
    • Genetic modification removes an immunodominant allergen from soybean
    • Herman, E.M., Helm, R.M., Jung, R., and Kinney, A.J. 2003. Genetic modification removes an immunodominant allergen from soybean. Plant Physiol., 132(1):36-43.
    • (2003) Plant Physiol , vol.132 , Issue.1 , pp. 36-43
    • Herman, E.M.1    Helm, R.M.2    Jung, R.3    Kinney, A.J.4
  • 163
    • 33847294540 scopus 로고    scopus 로고
    • Hypoallergenic transgenic soybeans.
    • US Patent, No. US2003/0041350 A1
    • Kinney, A.J., and Jung, R. 2003. Hypoallergenic transgenic soybeans. US Patent, No. US2003/0041350 A1.
    • (2003)
    • Kinney, A.J.1    Jung, R.2
  • 165
    • 0043196945 scopus 로고    scopus 로고
    • A novel brassinolide-enhanced gene identified by cDNA microarray is involved in the growth of rice
    • Yang, G., Matsuoka, M., Iwasaki, Y., and Komatsu, S. 2003. A novel brassinolide-enhanced gene identified by cDNA microarray is involved in the growth of rice. Plant Mol. Biol., 52:843-854.
    • (2003) Plant Mol. Biol , vol.52 , pp. 843-854
    • Yang, G.1    Matsuoka, M.2    Iwasaki, Y.3    Komatsu, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.