Identification of Allergens in Pork Meat

돼지고기 중 알레르기 유발성분의 동정

  • 정혜주 (국립독성연구소 독성부 면역독성과, 식품의약품안전청) ;
  • 박재현 (국립독성연구소 독성부 면역독성과, 식품의약품안전청) ;
  • 김재희 (국립독성연구소 독성부 면역독성과, 식품의약품안전청) ;
  • 김영옥 (국립독성연구소 독성부 면역독성과, 식품의약품안전청) ;
  • 정승태 (국립독성연구소 독성부 면역독성과, 식품의약품안전청) ;
  • 김진호 (국립독성연구소 독성부 면역독성과, 식품의약품안전청) ;
  • 조은득 (국립독성연구소 독성부 면역독성과, 식품의약품안전청) ;
  • 조대현 (국립독성연구소 독성부 면역독성과, 식품의약품안전청) ;
  • 노건웅 (성균관대학교 의과대학 소아과)
  • Published : 2001.02.01

Abstract

The pork meat has been reported as one of the food occurring allergic reactions predominantly to korean. To identify the potential food allergens in pork meat, sera were collected from 25 allergic patients to the pork meat and 10 allergic patients not to pork meat as well as 5 normal subjects after skin prick test and open food challenge test. Crude extracts were prepared by blending raw pork meat in phosphate buffered saline (pH 7.0) and the heat treatment on crude extracts was carried to characterize sensibility of the allergens to heat. ELISA was performed to determine specific IgE antibody levels of allergic patients to pork meat, and resulted in twofold higher mean value than that of tolerated patients. Extracted proteins from pork meat was separated with SDS-PAGE followed by immunoblotting using sera from pork sensitive patients and control subjects, respectively. The IgE binding response to pork meat by immunobots correlated with quantitative specific IgE value of each person. Immunoblots showed four prominent IgE-binding bands (66, 60, 50, 44 kDa) in crude extract, but two bands of those (60, 44 kDa) were heat-labile. These results suggest that most prominent allergens from pork meat are four components(66, 60, 50, 44 kDa) in korean and the heat treatment on allergen is additional parameter to characterize allergen.

Keywords

References

  1. Ameriacn Family Physician v.59 Evaluation and Management Sicherer, S. H
  2. Clin. Exp. Allergy v.21 Immune mechanisms in food allergy Metcalfe. D. D
  3. JAMA v.260 Fatal food-induced anaphylaxis Yunginger, J. W., Sweeney, K. G;Sturner, W. Q
  4. Food Allergy JAMA v.248 no.20 Buckley, R. H;Metcalf, D
  5. Biochem. Biophys. Acta v.882 Partial characterization of an allergenic glycoprotein from peanut(Arachis kypogaea L) Barnett, D;Howden, M. E. H
  6. J. Allergy Clin. Immunol v.88 Identification of a major peanut allergen, Ara h 1, in patients with atopic dermatitis and positive peanut challenge Burks, A. W., Williams, L. W., Heim. R. W., Connaughton, C. Cockrell, G;O'Brein T
  7. J. Allergy. Clin. Immunol v.90 Indetification and characterization of a second major peanut allergen, Ara h II, with use of the sera of patients with atopic dermatitis and positive peanut challege Burks, A. W., Williams, L. W., Connaughton, C., Cockrell, G., O'Brein T. J;Helm, R. M
  8. Int. Arch. Allergy Appl. Immunol v.32 Studies of hypersensitivity to fish: Partial purification and crystallization of a major allergenic component of codl Asa, K;Jebsen, J. W
  9. J. Allergy Clin. Immunol v.103 Food allergy: Immunopathogenesis and clinical disorders Sampson, H. A
  10. J. Pediatr v.107 Food hypersensitivity and atopic dermatitis: evaluation of 113 patients Sampson, H. A;McCaskil, I. C. C
  11. J. Allergy Clin. Immunol v.100 Relationship between food-specific IgE concentration and the risk of positive food challenges in children and adolescents Sampson, H. A;Ho, D. G
  12. 소아알레르기 및 호흡기 v.5 소아 천식환자에서 식품알레르기의 빈도 및 원인 식품 김규언;정병주;이기영
  13. Ann. Allergy Asthma Immunol v.79 Comparison of pediatric and adult IgE antivbody binding to fish proteins James, J. M., Helm, R. M., Burks, A. W;Lehrer, S. B
  14. Nature Biotech v.14 Stability of food allergens to digestion in vitro Astwood, J. D., Leach, J. N;Fuchs, R. L
  15. Nature v.227 Cleavage of structural proteins during the assembly of the head of bacterophage T4 Laemmli, U. K
  16. Proc. Natl. Acad. Sci v.76 Electrophoretic transfers of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications Towbin, H. T., Staehelin, T;Gordon, J
  17. Critical Reciews in Food Science and Nutrition v.36 Why are some proteins allergenic? Implications for biotechnology Lehrer, S. B., Horner, W. E;Reese, G. Lehrer, S. B., Horner, W. E;Reese, G
  18. J. Am. Coll. Nutr v.14 Meat allergy. I. Specific IgE to BSA and OSA in atopic beef sensitive children Fiocchi, A., Restani, P., Riva, E., Qualizza, R., Bruni, P., Resteli, Ar;Galli, C. L
  19. J. Am. Coll. Nutr v.14 Meat allergy. II. Effects of food processing and enzymatic digestion on the aller-genecity of bovine and ovine meats Fiocchi, A., Restani, P., Riva, E., Qualizza, R., Bruni, P. Resteli, Ar., Biasucci, G., Galli, C. L;Giovannini, M
  20. Allerg. Immunol v.31 Pork-cat syndrome in a 16-month-old child Couturier, P., Basset-Stheme, S;Sainte-Laudy, J
  21. J. Allergy Clin. Immunol v.98 Oral allergy syndrome after ingestion of salami in a subject with monosensitization to mite allergens Liccardi, G., D'Amato, G
  22. Clin. Chem v.26 Two-dimensional gel electrophoresis of cerebrospinal fluid proteins Goldman, D. Merril, c. R;Ebert, M. H
  23. Clinical and Experimental Allergy v.28 Alimentary allergy to pork. Crossreactivity among pork kidney and pork and lamb gut Llatser, R., Polo, F., Delahoz, F;Guillaumet, B
  24. Allergy v.52 Allergic cross-reactions between cat and pig serum albumin:Study at the protein and DNA levels Hilger, C., Kohnen, Grigioni, F., Lehners, C;Hentges, F
  25. Allergy v.52 Oral allergy syndrome from pork Asero, R., Mistrello, G;Falagiani, P