The analysis of the epitope structures of food allergens by using the synthetic peptides.
| Project/Area Number |
62560115
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
製造化学・食品
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| Research Institution | The University of Tokyo |
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Principal Investigator |
KAMINOGAWA Shuichi Department of Agricultural Chemistry, The University of Tokyo, 農学部, 助教授 (50011945)
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| Project Period (FY) |
1987 – 1988
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| Project Status |
Completed (Fiscal Year 1988)
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| Budget Amount *help |
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1988: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1987: ¥1,600,000 (Direct Cost: ¥1,600,000)
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| Keywords | Antibody / T cell / Casein / エピトープ / モノクローナル抗体 / β-ガゼイン / 抗原抗体反応 / ELISA / NMR / αs_1-カゼイン / 牛乳アレルギー |
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| Research Abstract |
It is important for prevention and cure of food allergy to elucidate the epitope structures of the allergens. In this study, we examined the structures of casein, one of potent allergens in bovine milk.
The full profiles of the sites on bovin s1-casein ( s1-CN) recognized by T and B cells were determined by using synthetic overlapping peptides and enzymatically digested fragments. It was shown that 1) limited sites on s1-CN are recognized by T and B cells; 2) the profiles of these recognition sites on s1-CN are similar in three mouse strains that have independent haplotypes.
The interaction between monoclonal antibody (MAb1C3) to -casein ( -cn) and its fragments was analyzed at the molecular level. As a result, it was shown that the amino acid residues, 194Gln, 200Pro and 202Arg, contributed largely to the binding to MAb1C3 and the contributions of 193Tyr and 201Val were inferior to the formers.
This information on the epitope structure of food allergens may be useful in understandind the antigen recognition in the immune response as well as the hypersensitivity in food allergy .
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Report
(3 results)
Research Products
(9 results)
