Structurally inherent antigenic sites. Localization of the antigenic sites of the α-chain of human haemoglobin in three host species by a comprehensive synthetic approach

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Abstract
The antigenic structure of the .alpha.-chain of human hemoglobin was studied by a synthetic approach consisting of the synthesis of a series of consecutive overlapping peptides that together systematically represent the entire primary structure of the protein. This approach enabled the identification of a full profile of immunochemically active .alpha.-chain peptides and the localization of its major continuous antigenic sites. Antibodies to hemoglobin raised in each of 3 different species (goat, rabbit and mouse) recognize similar sites on the .alpha.-chain. The molecular locations of these sites coincide with .alpha.-chain regions extrapolated from antigenic sites of the conformationally similar myoglobin molecule. The findings support the concept of structurally inherent antigenic sites, namely that antigenicity is conferred on certain surface regions of proteins by virtue of their 3-dimensional locations. The antigenic sites of conformationally related proteins are likely to have similar molecular locations.