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From the Center for Disease Control, Health Service and Mental Health Administration, Public Health Service, United States Department of Health, Education, and Welfare, Atlanta, Georgia 30333
Abstract
A virus immunoprecipitin radioassay (VIR) was developed to quantitate influenza virus interaction with specific antibody. After the initial virus-antibody reaction, quantitative binding of isotopically labeled anti-IgG resulted in the final formation of a virus immunoprecipitate. The anti-IgG radioactivity incorporated in this virus immunoprecipitate was a measure of the variation in any one of the reactants. This finding confirmed that the immunologic specificity of the VIR procedure was directly dependent upon virus antigen concentration and virus antibody dilution for proportional binding of the 125I-labeled anti-IgG with no prozone activity. Competitive inhibition of labeled anti-IgG antibody by unlabeled anti-IgG for detecting specifically bound virus antibody indicates the sensitivity of the virus immunoprecipitin reaction. Alternate methods for eliminating unbound anti-IgG from the virus immunoprecipitin complex, the carrier precipitate and the sucrose gradient methods were used. In the sucrose gradient method, the changes in the reactants, as evidenced by sedimentation behavior, were quantitative and proportional to the dilution of influenza antibody. Hemagglutination inhibition is no more reproducible and is not as sensitive or precise as the VIR for quantitating influenza-specific antibody. Correlation between the two tests indicates that they probably measure the same factor of influenza-specific antibody.
Footnotes
1 The research described in this report involved animals maintained in animal care facilities fully accredited by the American Association for Accreditation of Laboratory Animal Care. Use of trade names is for identification only and does not constitute endorsement by the Public Health Service or by the United States Department of Health, Education, and Welfare.
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