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The Journal of Immunology, 1968, 100: 955-963.
Copyright © 1968 by The American Association of Immunologists, Inc.
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Equine Antibodies to Human {gamma}G-Globulin

III. Immunochemical Behavior and Specificity of {gamma}2- and {gamma}1-Antibody Fractions Isolated from Equine Antisera to Human {gamma}G-Globulin1

Sarah L. Johnston and Peter Z. Allen

From the Department of Microbiology, University of Rochester School of Medicine and Dentistry, Rochester, New York 14620

Abstract

Several antisera to human {gamma}G-globulin obtained from a single horse and isolated {gamma}1- and {gamma}2-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 {gamma}2-antibody in the whole serum. Isolated {gamma}2-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 {gamma}2 fractions from the same or different bleedings. Isolated {gamma}1-antibody fractions possessed no complement-fixing ability but could inhibit fixation by the {gamma}2-antibody.

Both {gamma}2 and {gamma}1 preparations exhibited similar end points (0.04 µg antibody N) when employed as anti-globulin reagents in the Coombs test. In comparison, the {gamma}1-antibody fractions gave a prozone in the antibody excess region, whereas no prozone was noted with the {gamma}2 fractions. The specificity of antisera and antibody fractions from successive bleedings for antigenic determinants on the human {gamma}-globulin molecule was established by reacting these preparations with several antigens related to the heavy and light chains of human {gamma}-globulin.

Footnotes

Supported by United States Public Health Service Research Grant A1-06534.






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