stilbenes and Milk-Hypersensitivity

stilbenes has been researched along with Milk-Hypersensitivity* in 1 studies

Other Studies

1 other study(ies) available for stilbenes and Milk-Hypersensitivity

ArticleYear
β-Lactoglobulin mutant Lys69Asn has attenuated IgE and increased retinol binding activity.
    Journal of biotechnology, 2015, Oct-20, Volume: 212

    β-Lactoglobulin (β-LG) is a member of lipocalin superfamily of transporters for small hydrophobic molecules such as retinoids, fatty acids, drugs, and vitamins. β-LG also is one of the major allergens in milk. Despite a lot of research on decreasing cow's milk allergenicity, the effects of mutations of β-LG on recognition by IgE from cow's milk allergy (CMA) patients have not been investigated. We describe here the expression in the yeast Pichia pastoris of a mutant bovine β-LG, in which lysine at position 69, in the main epitopes of the protein, was changed into asparagine (Lys69Asn). The purity and native like folded structure of the recombinant Lys69Asn β-LG was confirmed by HPLC, SDS-PAGE, mass spectrometry and circular dichroism. Lys69Asn β-LG has a fourfold stronger affinity than the wild-type protein for retinol, palmitic acid, and resveratrol, as determined by quenching of the intrinsic tryptophan fluorescence. At the same time the Lys69Asn mutant had a 9 fold attenuated, compared with the wild-type, affinity for IgE of sera from patients suffering from cow's milk allergy, whereas no difference could be detected between mutant and wild-type for binding of the IgGs of four monoclonal antibodies. The results of this study demonstrated the significant role of Lys69 residue on the binding and immuoreactivity properties of β-LG.

    Topics: Antibodies, Monoclonal; Asparagine; Humans; Immunoglobulin E; Immunoglobulin G; Lactoglobulins; Lysine; Milk Hypersensitivity; Mutation; Palmitic Acid; Pichia; Protein Binding; Resveratrol; Stilbenes; Vitamin A

2015