Electrophoretic Analysis of Polypeptide Chains Isolated from Antibodies in the Serum of Immunized Rabbits

Abstract

The electrophoretic patterns of the sera from rabbits hyperimmunized with group A-variant and group C streptococcal vaccines exhibit a prominent narrow band in the γ-globulin region. This electrophoretically homogeneous γ-globulin was identified as antibody. L chains isolated from purified antibody preparations were shown to migrate as a narrow band on acid urea starch gel electrophoresis, whereas L chains from normal γ-globulin traveled as a diffuse smear. A limited number of L chain bands was also demonstrable using alkaline urea starch gel. All of the rabbits exhibiting this unusual antibody response were allotypically homozygous at both the a and b loci. Precipitin gel diffusion experiments suggest that the purified antibodies represent a limited population of the antigenic spectrum of normal rabbit γ-globulin. Thus, the immunologic and physicochemical properties of the γ-globulin isolated from these rabbits suggest a selective manufacture of an unusually homogeneous population of group specific carbohydrate antibodies.