Fragments of β-lactoglobulin were produced by proteolytic cleavage with trypsin, and chemical cleavage with cyanogen bromide, followed by gel filtration on Sephadex G-50. The antigenicity and allergenicity of the products were studied, before and after reductive cleavage by treatment with 2-mercaptoethanol. The former was determined by inhibition ELISA using IgG anti-β-lactoglobulin raised in rabbits, whilst the latter was determined by inhibition ELISA and mast cell challenge, using respectively the sera and peritoneal cells of rats experimentally sensitised to β-lactoglobulin. The findings raise interesting points about the structural basis of allergenicity in relation to antigenicity.
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