title: Antibody response of three different strains of mice to alpha s1-casein analyzed by using proteolytic and synthetic peptides.
abstract: The location of immunodominant regions on bovine alpha s1-casein (alpha s1-CN) was compared among three strains of mice (BALB/c, C3H/He and C57BL/6). Anti-alpha s1-CN antisera were separated 5 weeks after the first immunization. Thirty-seven kinds of peptides were obtained from alpha s1-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 alpha s1-CN. The ability of the anti-alpha s1-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 alpha s1-CN. The immunodominant antigenic regions of alpha s1-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).
authors.affiliation: Department of Agricultural Chemistry, University of Tokyo, Japan.
authors.forename: A
authors.initials: A
authors.lastname: Ametani
authors.forename: S M
authors.initials: SM
authors.lastname: Kim
authors.forename: S
authors.initials: S
authors.lastname: Kaminogawa
authors.forename: K
authors.initials: K
authors.lastname: Yamauchi
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000917:Antibody Formation; D002364:Caseins / Q000276:immunology*; D002918:Chymotrypsin; D005260:Female; D051379:Mice; D008807:Mice, Inbred BALB C / Q000276:immunology; D008809:Mice, Inbred C3H / Q000276:immunology; D008810:Mice, Inbred C57BL / Q000276:immunology; D008815:Mice, Inbred Strains / Q000276:immunology*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000276:immunology; D013045:Species Specificity; D014357:Trypsin
chemical_list: D002364:Caseins; D010446:Peptide Fragments; D002918:Chymotrypsin; D014357:Trypsin