Abstract
Summary Several antisera to human γG-globulin obtained from a single horse and isolated γ1- and γ2-antibody fractions prepared from these antisera were compared in complement fixation studies. C′-fixing ability of each successive bleeding progressively increased, paralleling an apparent increase in the proportion of γ2-antibody in the whole serum. Isolated γ2-antibody fractions fixed complement when tested at a level of 1 µg antibody N and greater. There were no significant differences in complement-fixing ability on an antibody N weight basis among γ2 fractions from the same or different bleedings. Isolated γ1-antibody fractions possessed no complement-fixing ability but could inhibit fixation by the γ2-antibody. Both γ2 and γ1 preparations exhibited similar end points (0.04 µg antibody N) when employed as anti-globulin reagents in the Coombs test. In comparison, the γ1-antibody fractions gave a prozone in the antibody excess region, whereas no prozone was noted with the γ2 fractions. The specificity of antisera and antibody fractions from successive bleedings for antigenic determinants on the human γ-globulin molecule was established by reacting these preparations with several antigens related to the heavy and light chains of human γ-globulin.
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