Structural and serological relationships among different antibodies from the same rabbit antiserum. I. Isolation, chemical and allotypic characterization of ten antibody components from one anti-streptococcal serum.
The relationships among antibodies produced by an individual rabbit were examined using multiple antibodies elicited by hyperimmunization with Group C streptococcal vaccine. Immunoadsorbent chromatography followed by agarose block electrophoresis yielded nine different antibody fractions, all directed against Group C carbohydrate, from the immune plasma of rabbit 4295 (allotype a1/b5). Electrophoresis of the antibody light chains gave single bands for most of the antibodies. Amino acid sequence analyses carried out on several of the antibody L-chains revealed that five of these had aspartic acid at the amino terminus. By quantitative allotypic analyses all antibodies were allotype a1/b5. One antibody fraction, homogeneous by all other criteria, contained antibodies with two distinct group a allotypic subspecificities. The two antibodies in this fraction could be separated on an anti-a1 column. The ten antibodies were placed into a minimum of three groups based on differences in a1 allotype subspecificity.
D000595:Amino Acid Sequence; D000818:Animals; D000907:Antibodies, Bacterial / Q000302:isolation & purification; D001666:Binding Sites, Antibody; D007106:Immune Sera / Q000032:analysis; D007126:Immunoglobulin Allotypes; D007147:Immunoglobulin Light Chains / Q000032:analysis; D011817:Rabbits / Q000276:immunology*; D013291:Streptococcus / Q000276:immunology*
D000907:Antibodies, Bacterial; D007106:Immune Sera; D007126:Immunoglobulin Allotypes; D007147:Immunoglobulin Light Chains