Clinical & Experimental Allergy

Ligand binding properties of the basophilic IgE receptor of normal and allergic individuals

Authors

  • B. M. WEICHMAN,

    Corresponding author
    1. Department of Pharmacology, Smith Kline and French Laboratories, Philadelphia, Pennsylvania, U.S.A.
      Dr Barry M. Weichman, Department of Pharmacology, Smith Kline and French Laboratories, P.O. Box 7929, Philadelphia, Pennsylvania 19101, U.S.A.
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  • ROSEANNA M. MUCCITELLI

    1. Department of Pharmacology, Smith Kline and French Laboratories, Philadelphia, Pennsylvania, U.S.A.
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Dr Barry M. Weichman, Department of Pharmacology, Smith Kline and French Laboratories, P.O. Box 7929, Philadelphia, Pennsylvania 19101, U.S.A.

Summary

The interaction of [125I]-human myeloma IgE with the human basophilic IgE receptor of normal and allergic individuals was quantitated by direct ligand binding analysis after removal of endogenous IgE. Using a mixed leucocyte preparation containing 2 to 5% basophils, the [125I]-IgE binding was specific for human IgE, paralleled the presence of basophils in the cell preparation, and was described by a time course similar to that reported for passive sensitization experiments. The Kd values were 4.0 to 13.2 nM for the normal individuals with 1.5 to 8.4 × 105 receptors per basophil, while the IgE receptor of allergic individuals was described by Kd values of 4.2 to 11.7 nM and 3.0 to 4.7 × 105 sites per basophil. Based upon the eleven individuals studied, these results suggest that the binding properties of the IgE receptor of normal and allergic individuals are similar.

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