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Kinetic analysis of the interaction between recombinant human Fc(epsilon)RIalpha and serum IgEs from allergic patients.

Binding of IgE to the high-affinity IgE receptor (Fc(epsilon)RI) is the essential event for allergic reaction. Although there are many reports on binding kinetics between myeloma IgE and Fc(epsilon)RI, little is known about the kinetics between heterogeneous polyclonal IgE in the serum and Fc(epsilon)RIalpha. To elucidate the binding characteristics of heterogeneous serum IgE, we measured kinetic parameters of binding between IgE from allergic patients and a recombinant ectodomain of the human Fc(epsilon)RIalpha subunit by real-time interaction analysis based on surface plasmon resonance. Purified IgE monomer from the plasma of allergic patients displayed kinetics for the interaction with Fc(epsilon)RIalpha similar to those of myeloma IgE. In the case of crude IgE samples from allergic patients, one of seven specimens showed significantly higher affinity than highly purified IgE, suggesting that it is possible for IgEs in this specimen to form complexes of higher molecular weight.