Clinical Chemistry
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Clinical Chemistry 34: 1481-1483, 1988;
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Clinical Chemistry, Vol 34, 1481-1483, Copyright © 1988 by American Association for Clinical Chemistry

The potency of immunoglobulin G fragments for inhibition of interference caused by anti-immunoglobulin antibodies in a monoclonal immunoradiometric assay for thyrotropin

G Csako, BD Weintraub and MH Zweig
Clinical Pathology Department, Warren Grant Magnuson Clinical Center, National Institutes of Health, Bethesda, MD 20892.

Heterophile antibodies in patients' serum may produce false increases in apparent analyte concentrations in "sandwich"-type immunoassays. Using three patients with endogenous anti-mouse IgG antibodies and a two-site mouse monoclonal assay for thyrotropin, we studied the ability of IgG fragments to block this positive interference. Mouse whole IgG and IgG Fc fragment blocked the interference virtually completely; IgG F(ab')2 and Fab fragments did not. Rat and horse immunoglobulin fragments gave variable results. We suggest that sandwich assays formulated with IgG Fab or F(ab')2 fragments may be less susceptible to positive interference by heterophile antibodies. Unlike sera from the three patients, simulated human specimens containing heterologous anti- IgG antibodies showed little or no selectivity in inhibition by IgG fragments, and therefore are not useful to study this phenomenon.


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Copyright © 1988 by the American Association for Clinical Chemistry.