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Abstract
Antigenic properties of 14 fragments of bovine albumin were measured using antisera to albumin and to two of its fragments. All seven fragments larger than 21,000 daltons formed immune precipitates. Although immune precipitates were not formed with smaller fragments, inhibition tests indicated the presence of antigenic sites on several of these fragments as well. The results predict the occurrence of six or more antigenic determinants and allow assignment of their positions in the parent molecule. These sites are distributed along the entire protein chain, with the sites of greatest antibody affinity situated in the COOH-terminal region. Evidence is presented that some sites are homologous, reacting with the same populations of antibodies, and that other sites are unique, binding to an exclusive population of antibodies.
Highlights
Numerous fragments of bovine albumin have been isolated following cleavage of the interloop peptide strands without rupture of disulfide bonds [2,3,4,5,6,7,8,9]
Teale and Benjamin [9] demonstrated antibody binding ability of three tryptic fragments of bovine albumin, and Habeeb and Atassi [7] and Atassi et al
The latter authors interpreted their observations of strong inhibition of precipitation of bovine albumin by fragments from different regions of the molecule as evidence that the molecule contains a series of repeating antigenic sites
Summary
Numerous fragments of bovine albumin have been isolated following cleavage of the interloop peptide strands without rupture of disulfide bonds [2,3,4,5,6,7,8,9]. Teale and Benjamin [9] demonstrated antibody binding ability of three tryptic fragments of bovine albumin, and Habeeb and Atassi [7] and Atassi et al The latter authors interpreted their observations of strong inhibition of precipitation of bovine albumin by fragments from different regions of the molecule as evidence that the molecule contains a series of repeating antigenic sites. Directed against bovine albumin, against a large COOH-terminal fragment, and against a large NH, terminal fragment
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