Abstract
The location of immunodominant regions on bovine αs1-casein (αs1-CN) was compared among three strains of mice ( BALB c , C3H He and C57BL 6 ). Anti-αs1-CN antisera were separated 5 weeks after the first immunization. Thirty-seven kinds of peptides were obtained from αs1-CN by proteolysis, and the segmental 19- to 20-residue peptides overlapping with their adjacent neighbors by 5 residues were synthesized over the entire polypeptide chain of αs1-CN. The ability of the anti-αs1-CN antibody to bind peptides was tested by an enzyme-linked immunosorbent assay, in which the peptides were adsorbed to the solid phase. All the strains responded highly to αs1-CN. The immunodominant antigenic regions of αs1-CN were not common to the three strains of mice, the H-2 haplotypes being different from each other ( BALB c , regions 1, 3, 5, 6 and 7; C3H He , regions 2, 3, 5, 6, 6′, 7 and 7′; and C57BL 6 , regions 2, 4, 5, 6 and 7).
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