Bovine serum albumin (BSA) is one of the most widely studied proteins; its structure is well known and its antigenic properties have been described in animal models. The aim of our work was to evaluate the role of conformation on antigenicity of serum albumins. This study was performed using electrophoresis associated with the immunoblotting technique, where sera from children allergic to BSA were used. Data obtained in this research indicate that serum albumin antigenicity is only partially correlated to its native three-dimensional structure. Heat treatment and chemical denaturation (SDS treatment) are not able to significantly decrease its capability to bind circulating IgEs. Only the reducing treatment is able to modify the antigenicity of this protein. Moreover, a direct correlation between the cross-reactivity observed in immunoblotting between different serum albumins and the percentage of their sequence identity (phylogenetic similarity of the species) was shown.
|Number of pages||5|
|Journal||Letters in Peptide Science|
|Publication status||Published - 1997|
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