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Assay of IgG and Other Human Plasma Proteins by Quantitative Inhibition of Passive Hemagglutination¹

From the Department of Medicine, Division of Hematology, Mount Sinai School of Medicine, City University of New York, New York, New York

Abstract

Using tanned human red cells coated optimally with isolated plasma proteins, specific agglutination in an AutoAnalyzer was quantitatively inhibited by solutions of the coating protein. IgG, IgM, IgA, IgD, IgE, transferrin, fibrinogen and ceruloplasmin were assayed in this manner. Lowest detectable concentrations varied from 0.2 µg IgE/ml and 0.4 µg IgG/ml to 9 µg IgD/ml. The amount of ¹²⁵I-labeled IgG bound by tanned cells was a linear function of the amount applied when both variables were treated as logarithms, and about 2000 bound molecules per cell were optimal for agglutination. IgG appeared to bind at its Fab region, but less than 5% of the lowest applied concentrations was bound. Assays of cerebrospinal fluid for IgG compared favorably with quantitative precipitin data, but some myeloma proteins were not assayed reliably in reference to normal IgG.

Footnotes

¹ This work was supported by National Institutes of Health Grants HE-05488, HE-03972, AM 12912, PH 43-67-1359 and by Grants from the Albert A. List Foundation, Frederick Machlin Fund, and the Anna Ruth Lowenberg Research Fund.

² Current address: Medical Director, Regional Blood Program, American Red Cross, Rochester, New York and Assistant Professor of Medicine, University of Rochester School of Medicine and Dentistry, Rochester, N. Y.

³ Current address: Director, Blood Bank, New England Medical Center Hospitals, 171 Harrison Ave., Boston, Mass.