Ligand binding properties of the basophilic IgE receptor of normal and allergic individuals.
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 x 10(5) 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 x 10(5) 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.
D000918:Antibody Specificity; D001491:Basophils / Q000378:metabolism*; D006801:Humans; D006967:Hypersensitivity / Q000276:immunology*; D008214:Lymphocytes / Q000378:metabolism; D009194:Myeloma Proteins / Q000378:metabolism; D017455:Receptors, IgE; D011971:Receptors, Immunologic / Q000502:physiology; D013997:Time Factors
D009194:Myeloma Proteins; D017455:Receptors, IgE; D011971:Receptors, Immunologic