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Wyniki nadające się do wykorzystania
Food allergies affect a significant proportion of the population with consequent adverse effects. Food allergies are due not to the whole protein but to a discrete area (peptide) and especially to the reactive sequence (epitope) of amino acids in the peptide. Molecular biology techniques are being used to identify or synthesise the peptide sequences and this information will be used to develop a strategy for making 'allergen-free' food products as well as developing improved immunoassays for the investigation of allergenic reactions. Allergens encourage the production of immunoglobulin E (IgE) antibodies which bind the allergen and trigger the allergic cascade. Experiments have been designed where food allergens will be screened for their ability to induce immune responses, not directly in the body, but in in-vitro culture systems of human lymph cells. This should lead to improved understanding of the mechanism of food allergy thus helping to protect the consumer. Studies have been initiated using a milk protein (beta-lactoglobulin) as the model compound, as its molecular structure has been well documented. For example, a procedure has been developed to isolate `gram' quantities of homogenous beta-lactoglobulin. This preparation is used for the production of beta-lactoglobulin hydrolysates to be tested by screening with human sera as well as in experimental animal studies. A new and improved test procedure has been developed in order to determine that region of the peptide preferentially recognized by IgE antibodies present in sera obtained from cow's milk allergic patients. This test will become a most useful tool in the development of the project. An experimental animal model which provides specific beta-lactoglobulin IgE antibodies has been established using the Brown Norway rat, and is available for screening milk hydrolysates and peptides.
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