메뉴 건너뛰기




Volumn 46, Issue 5, 2000, Pages 661-669

Purification, biochemical, and immunological characterisation of a major food allergen: Different immunoglobulin E recognition of the apo- and calcium-bound forms of carp parvalbumin

Author keywords

Antibodies; Circular dichroism; Epitopes; Food allergy; Immunochemistry; Parvalbumin

Indexed keywords

CROSS REACTING ANTIGEN; EPITOPE; FOOD ALLERGEN; IMMUNOGLOBULIN E; PARVALBUMIN;

EID: 0004844595     PISSN: 00175749     EISSN: None     Source Type: Journal    
DOI: 10.1136/gut.46.5.661     Document Type: Article
Times cited : (158)

References (52)
  • 3
    • 0033064254 scopus 로고    scopus 로고
    • Food allergy. Part 1 : Immunopathogenesis and clinical disorders
    • 3 Sampson H. Food allergy. Part 1 : Immunopathogenesis and clinical disorders, J Allergy Clin Immunol 1999;103:717-28.
    • (1999) J Allergy Clin Immunol , vol.103 , pp. 717-728
    • Sampson, H.1
  • 4
    • 0032813419 scopus 로고    scopus 로고
    • Food allergy. Part 2: Diagnosis and management
    • 4 Sampson H. Food allergy. Part 2: Diagnosis and management. J Allergy Clin Immunol 1999;103:981-9.
    • (1999) J Allergy Clin Immunol , vol.103 , pp. 981-989
    • Sampson, H.1
  • 5
    • 0029828108 scopus 로고    scopus 로고
    • Prevalence of adverse reactions to food in patients with gastrointestinal diseases
    • 5 Bischoff SC, Herrmann A, Manns MP. Prevalence of adverse reactions to food in patients with gastrointestinal diseases. Allergy 1996;51:811-18.
    • (1996) Allergy , vol.51 , pp. 811-818
    • Bischoff, S.C.1    Herrmann, A.2    Manns, M.P.3
  • 6
    • 0031713908 scopus 로고    scopus 로고
    • IgE-mediated food allergies including oral allergy syndrome in 383 patients
    • 6 Etesamifar M, Wüthrich B. IgE-mediated food allergies including oral allergy syndrome in 383 patients. Allergologic 1998;21:451-7.
    • (1998) Allergologic , vol.21 , pp. 451-457
    • Etesamifar, M.1    Wüthrich, B.2
  • 7
    • 0014641848 scopus 로고
    • Characterization of a major allergen (cod)
    • 7 Aas Kj Elsayed SM. Characterization of a major allergen (cod). J Allergy 1969;44:333-43.
    • (1969) J Allergy , vol.44 , pp. 333-343
    • Aas, K.1    Elsayed, S.M.2
  • 8
    • 0016814965 scopus 로고
    • The primary structure of allergen M from cod
    • 8 Elsayed S, Bennich H. The primary structure of allergen M from cod. Scand J Immunol 1975;4:203-8.
    • (1975) Scand J Immunol , vol.4 , pp. 203-208
    • Elsayed, S.1    Bennich, H.2
  • 11
    • 0025614995 scopus 로고
    • Allergy to different fish species in cod allergic children: In vivo and in vitro studies
    • 11 De Martino M, Novembre E, Galli L, et al. Allergy to different fish species in cod allergic children: in vivo and in vitro studies. J Allergy Clin Immunol 1990;86:909-14.
    • (1990) J Allergy Clin Immunol , vol.86 , pp. 909-914
    • De Martino, M.1    Novembre, E.2    Galli, L.3
  • 12
    • 0026477999 scopus 로고
    • Fish allergy: Evaluation of the importance of cross-reactivity
    • 12 Pascual C, Esteban MM, Crespo JF. Fish allergy: evaluation of the importance of cross-reactivity. J Pediatr 1992;121: 29-34.
    • (1992) J Pediatr , vol.121 , pp. 29-34
    • Pascual, C.1    Esteban, M.M.2    Crespo, J.F.3
  • 13
    • 0026553913 scopus 로고
    • Fish hypersensitivity. I. In vitro and oral challange results in fish-allergic patients
    • 13 Bernhisel-Broadbent J, Scanlon SM, Sampson HA. Fish hypersensitivity. I. In vitro and oral challange results in fish-allergic patients. J Allergy Clin Immunol 1992;89:730-7.
    • (1992) J Allergy Clin Immunol , vol.89 , pp. 730-737
    • Bernhisel-Broadbent, J.1    Scanlon, S.M.2    Sampson, H.A.3
  • 15
    • 0024789636 scopus 로고
    • 2+-binding proteins parvalbumin and oncomodulin
    • 2+-binding proteins parvalbumin and oncomodulin. Biochim Biophys Acta 1989;1009:201-15.
    • (1989) Biochim Biophys Acta , vol.1009 , pp. 201-215
    • Berchtold, M.W.1
  • 16
    • 0018539233 scopus 로고
    • Evolutionary diversification of structure and function in the family of intracellular calcium-binding proteins
    • 16 Goodman M, Pechere JF, Haiech J, et al. Evolutionary diversification of structure and function in the family of intracellular calcium-binding proteins. J Mol Evol 1979;13: 331-52.
    • (1979) J Mol Evol , vol.13 , pp. 331-352
    • Goodman, M.1    Pechere, J.F.2    Haiech, J.3
  • 17
    • 0025978546 scopus 로고
    • Intracellular calcium-binding proteins: More sites than insights
    • 17 Heizmann CW, Hunziker W. Intracellular calcium-binding proteins: more sites than insights. Trends Biochem Sci 1991; 16:98-103.
    • (1991) Trends Biochem Sci , vol.16 , pp. 98-103
    • Heizmann, C.W.1    Hunziker, W.2
  • 18
    • 0000596916 scopus 로고
    • Towards an understanding of the effects of calcium on protein structure and function
    • 18 Strynadka N, James M. Towards an understanding of the effects of calcium on protein structure and function. Curr Opin Struct Biol 1991;1:905-14.
    • (1991) Curr Opin Struct Biol , vol.1 , pp. 905-914
    • Strynadka, N.1    James, M.2
  • 19
    • 0030032040 scopus 로고    scopus 로고
    • Calcium-binding and conformation response in EF-hand proteins
    • 19 Ikura M. Calcium-binding and conformation response in EF-hand proteins. Trends Biochem Sci 1996;21:14-17.
    • (1996) Trends Biochem Sci , vol.21 , pp. 14-17
    • Ikura, M.1
  • 20
    • 0015239558 scopus 로고
    • Muscular parvalbumins: Preparative and analytical methods of general applicability
    • 20 Pechere JF, Demaille J, Capony JP Muscular parvalbumins: preparative and analytical methods of general applicability. Biochem Biophys Acta 1971;236:391-408.
    • (1971) Biochem Biophys Acta , vol.236 , pp. 391-408
    • Pechere, J.F.1    Demaille, J.2    Capony, J.P.3
  • 21
    • 0015218997 scopus 로고
    • The primary structure of the major parvalbumin from hake muscle
    • 21 Pechere JF, Capony JP, Ryden L. The primary structure of the major parvalbumin from hake muscle. Eur J Biochem 1971;23:421-8.
    • (1971) Eur J Biochem , vol.23 , pp. 421-428
    • Pechere, J.F.1    Capony, J.P.2    Ryden, L.3
  • 22
    • 0015919789 scopus 로고
    • Carp muscle calcium-binding protein. I. Characterization of the tryptic peptides and the complete amino acid sequence
    • 22 Coffee CJ, Bradshaw RA. Carp muscle calcium-binding protein. I. Characterization of the tryptic peptides and the complete amino acid sequence. J Biol Chem 1973;248: 3305-12.
    • (1973) J Biol Chem , vol.248 , pp. 3305-3312
    • Coffee, C.J.1    Bradshaw, R.A.2
  • 23
    • 0015919772 scopus 로고
    • Carp muscle calcium-binding protein. II. Structure determination and general description
    • 23 Kretsinger RH, Nockold CE. Carp muscle calcium-binding protein. II. Structure determination and general description. J Biol Chem 1973;248:3313-26.
    • (1973) J Biol Chem , vol.248 , pp. 3313-3326
    • Kretsinger, R.H.1    Nockold, C.E.2
  • 24
    • 0025870926 scopus 로고
    • Ionic interactions with parvalbumins. Crystal structure determination of pike 4.10 parvalbumin in four different ionic environments
    • 24 Declercq JP, Tinant B, Parello J, et al. Ionic interactions with parvalbumins. Crystal structure determination of pike 4.10 parvalbumin in four different ionic environments. J Mol Biol 1991;220:1017-39.
    • (1991) J Mol Biol , vol.220 , pp. 1017-1039
    • Declercq, J.P.1    Tinant, B.2    Parello, J.3
  • 25
    • 0016255298 scopus 로고
    • Isolation and characterization of parvalbumin from skeletal muscle of higher vertebrates
    • 25 Lehky P, Blum HE, Stein EA, et al. Isolation and characterization of parvalbumin from skeletal muscle of higher vertebrates. J Biol Chem 1974;249:4332-4.
    • (1974) J Biol Chem , vol.249 , pp. 4332-4334
    • Lehky, P.1    Blum, H.E.2    Stein, E.A.3
  • 26
    • 0017373457 scopus 로고
    • Comparative properties of vertebrate parvalbumins
    • 26 Blum HE, Lehky P, Kohler L, et al. Comparative properties of vertebrate parvalbumins. J Biol Chem 1977;252:2834-8.
    • (1977) J Biol Chem , vol.252 , pp. 2834-2838
    • Blum, H.E.1    Lehky, P.2    Kohler, L.3
  • 27
    • 0017334460 scopus 로고
    • The evolution of muscular parvalbumins investigated by the maximum parsimony method
    • 27 Goodman M, Pechere JF. The evolution of muscular parvalbumins investigated by the maximum parsimony method. J Mol Evol 1977;9:131-58.
    • (1977) J Mol Evol , vol.9 , pp. 131-158
    • Goodman, M.1    Pechere, J.F.2
  • 28
    • 0018380478 scopus 로고
    • Magnesium and calcium binding to parvalbumins: Evidence for differences between parvalbumins and an explanation of their relaxing function
    • 28 Haiech J, Derancourt J, Pechere JF, et al. Magnesium and calcium binding to parvalbumins: evidence for differences between parvalbumins and an explanation of their relaxing function. Biochemistry 1979;8:2752-8.
    • (1979) Biochemistry , vol.8 , pp. 2752-2758
    • Haiech, J.1    Derancourt, J.2    Pechere, J.F.3
  • 29
    • 0020392253 scopus 로고
    • Correlation of parvalbumin concentration with relaxation speed in mammalian muscles
    • 29 Heizmann CW, Berchtold MW, Rowlerson AM. Correlation of parvalbumin concentration with relaxation speed in mammalian muscles. Proc Natl Acad Sci USA 1982;79: 7243-7.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 7243-7247
    • Heizmann, C.W.1    Berchtold, M.W.2    Rowlerson, A.M.3
  • 30
    • 0019480256 scopus 로고
    • Calcium-binding protein parvalbumin as a neuronal marker
    • 30 Celio MR, Heizman CW. Calcium-binding protein parvalbumin as a neuronal marker. Nature 1981;293:300-2.
    • (1981) Nature , vol.293 , pp. 300-302
    • Celio, M.R.1    Heizman, C.W.2
  • 31
    • 0022363120 scopus 로고
    • Parvalbumin exists in endocrine glands
    • 31 Endo T, Takazawa K, Onaya T. Parvalbumin exists in endocrine glands. Endocrinology 1985;117:527-31.
    • (1985) Endocrinology , vol.117 , pp. 527-531
    • Endo, T.1    Takazawa, K.2    Onaya, T.3
  • 32
    • 0031437075 scopus 로고    scopus 로고
    • Food allergy
    • 32 Sampson HA. Food allergy. JAMA 1997;278:1888-94.
    • (1997) JAMA , vol.278 , pp. 1888-1894
    • Sampson, H.A.1
  • 33
    • 0031759455 scopus 로고    scopus 로고
    • Accuracy of in vivo and in vitro tests
    • 33 Bindslev JC, Poulsen LK. Accuracy of in vivo and in vitro tests. Allergy 1998;53:72-4
    • (1998) Allergy , vol.53 , pp. 72-74
    • Bindslev, J.C.1    Poulsen, L.K.2
  • 34
    • 8544246419 scopus 로고    scopus 로고
    • Colonoscopic allergen provocation (COLAP): A new diagnostic approach for gastrointestinal food allergy
    • 34 Bischoff SC, Mayer J, Wedemeyer J, et al. Colonoscopic allergen provocation (COLAP): a new diagnostic approach for gastrointestinal food allergy. Gut 1997;40:745-53.
    • (1997) Gut , vol.40 , pp. 745-753
    • Bischoff, S.C.1    Mayer, J.2    Wedemeyer, J.3
  • 35
    • 0023987712 scopus 로고
    • Monoclonal antibodies directed against the calcium binding protein parvalbumin
    • 35 Celio MR, Baier W, Scharer L, et al. Monoclonal antibodies directed against the calcium binding protein parvalbumin. Cell Calcium 1988;9:81-6.
    • (1988) Cell Calcium , vol.9 , pp. 81-86
    • Celio, M.R.1    Baier, W.2    Scharer, L.3
  • 36
    • 0022392683 scopus 로고
    • Modification of nuclear matrix proteins by ADP-ribosylation. Association of nuclear ADP-ribosyltransferase with the nuclear matrix
    • 36 Wesierska-Gadek J, Sauermann G. Modification of nuclear matrix proteins by ADP-ribosylation. Association of nuclear ADP-ribosyltransferase with the nuclear matrix. Eur J Biochem 1985;153:421-8.
    • (1985) Eur J Biochem , vol.153 , pp. 421-428
    • Wesierska-Gadek, J.1    Sauermann, G.2
  • 37
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 37 Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 38
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some apllications
    • 38 Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some apllications. Proc Natl Acad Sci USA 1979;76:4350-4.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 40
    • 0024443144 scopus 로고
    • The gene coding for the major birch pollen allergen Betv1 is highly homologous to a pea disease resistance response gene
    • 40 Breiteneder H, Pettenburger K, Bito A, et al. The gene coding for the major birch pollen allergen Betv1 is highly homologous to a pea disease resistance response gene. EMBO J 1989;8:1935-8.
    • (1989) EMBO J , vol.8 , pp. 1935-1938
    • Breiteneder, H.1    Pettenburger, K.2    Bito, A.3
  • 41
    • 0024399296 scopus 로고
    • Interleukin 3 activates human blood basophils via high-affinity binding sites
    • 41 Valent P, Besmer L, Muhm M, et al. Interleukin 3 activates human blood basophils via high-affinity binding sites. Proc Natl Acad Sci USA 1989;86:5542-7.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 5542-5547
    • Valent, P.1    Besmer, L.2    Muhm, M.3
  • 42
    • 0030973268 scopus 로고
    • Conformational effects of calcium release from parvalbumins: Comparison of computational simulations with spectroscopic investigations
    • 42 Laberge M, Wright WW, Sudhakar K, et al. Conformational effects of calcium release from parvalbumins: comparison of computational simulations with spectroscopic investigations. Biochemistry 1995;36:5363-71.
    • (1995) Biochemistry , vol.36 , pp. 5363-5371
    • Laberge, M.1    Wright, W.W.2    Sudhakar, K.3
  • 43
    • 0028904064 scopus 로고
    • Dynamics of parvalbumin studied by fluorescence emission and triplet absorption spectroscopy of tryptophan
    • 43 Sudhakar K, Philips CM, Owen CS, et al. Dynamics of parvalbumin studied by fluorescence emission and triplet absorption spectroscopy of tryptophan. Biochemistry 1995; 34:1355-63.
    • (1995) Biochemistry , vol.34 , pp. 1355-1363
    • Sudhakar, K.1    Philips, C.M.2    Owen, C.S.3
  • 44
    • 0026722948 scopus 로고
    • Fish hypersensitivity. II: Clinical relevance of altered fish allergenicity caused by various preparation methods
    • 44 Bernhisl-Broadbent J, Strause D, Sampson HA. Fish hypersensitivity. II: Clinical relevance of altered fish allergenicity caused by various preparation methods. J Allergy Clin Immunol 1992;90:622-9.
    • (1992) J Allergy Clin Immunol , vol.90 , pp. 622-629
    • Bernhisl-Broadbent, J.1    Strause, D.2    Sampson, H.A.3
  • 45
    • 0021883909 scopus 로고
    • Evaluation of immediated adverse reactions to foods in adult patients. II. A detailed analysis of reaction patterns during oral food challenge
    • 45 Atkins FM, Steinberg SS, Metcalfe DD. Evaluation of immediated adverse reactions to foods in adult patients. II. A detailed analysis of reaction patterns during oral food challenge. J Allergy Clin Immunol 1985;75:348-55.
    • (1985) J Allergy Clin Immunol , vol.75 , pp. 348-355
    • Atkins, F.M.1    Steinberg, S.S.2    Metcalfe, D.D.3
  • 46
    • 0027257525 scopus 로고
    • Introduction: Basophil histamine release and the diagnosis of food allergy
    • 46 Du Buske LM. Introduction: basophil histamine release and the diagnosis of food allergy. Allergy Proc 1993;14:243-9.
    • (1993) Allergy Proc , vol.14 , pp. 243-249
    • Du Buske, L.M.1
  • 49
  • 50
    • 0032826306 scopus 로고    scopus 로고
    • Genetically engineered and synthetic allergen derivatives: Candidates for vaccination against type I allergy
    • 50 Valenta R, Vrtala S, Focke-Tejkl M, et al. Genetically engineered and synthetic allergen derivatives: Candidates for vaccination against type I allergy. Biol Chem 1999;380: 815-24.
    • (1999) Biol Chem , vol.380 , pp. 815-824
    • Valenta, R.1    Vrtala, S.2    Focke-Tejkl, M.3
  • 51
    • 0028167950 scopus 로고
    • 2+-binding sites in the paired EF-hand sites of parvalbumin reveals asymmetrical metal-binding properties
    • 2+-binding sites in the paired EF-hand sites of parvalbumin reveals asymmetrical metal-binding properties. Biochemistry 1994;33:10393-400.
    • (1994) Biochemistry , vol.33 , pp. 10393-10400
    • Pauls, T.L.1    Durussel, I.2    Berchtold, M.W.3
  • 52
    • 0029665077 scopus 로고    scopus 로고
    • 2+-induced conformational transitions in calmodulin with disulfide bonds
    • 2+-induced conformational transitions in calmodulin with disulfide bonds. J Biol Chem 1996;271:7479-83.
    • (1996) J Biol Chem , vol.271 , pp. 7479-7483
    • Tan, R.Y.1    Mabuchi, Y.2    Grabarck, Z.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.