caa a22 4500 477127096 CHVBK 20180405111653.0 cr unu---uuuuu 170330e19971001xx s 000 0 eng 10.1023/A:1012116604499 doi (NATIONALLICENCE)springer-10.1023/A:1012116604499 Interaction of Human IgE with Soluble Forms of IgE High Affinity Receptors [Elektronische Daten] [Jim Liu, Jane Ruppel, Steven Shire] Purpose. Interaction of human IgE with its high affinity receptor (FcεRI) on mast cells and basophils is an important step for initiating IgE mediated immune responses. To characterize the IgE and FcεRI interaction, we investigated this interaction in terms of stoichiometry and binding affinity in solution. The binding of IgE and IgE FcεRI α chain, the extracellular portion of IgE high affinity receptor (sFcεRIα) was compared with the binding of IgE and IgE immunoadhesin (FcεRIα-IgG). Methods. The interaction was characterized by analytical ultracentrifugation, size exclusion chromatography, light scattering and ELISA. Results. We show that the sFcεRIα is only able to bind to one IgE, while the immunoadhesin can bind to two IgE. The interaction between IgE and FcεRI is very strong. Both forms of soluble receptors have similar intrinsic binding affinity with IgE. Conclusions. Both soluble receptors (FcεRIα-IgG and sFcεRIα) can block the binding of IgE to its high affinity receptors on cell surface. The FcεRIα-IgG is a better IgE binding protein than sFcεRIα at physiological relevant conditions. A humanized anti-IgE monoclonal antibody, rhuMAb E25 that also can block the binding of IgE to its high affinity receptors appears to bind to IgE at slightly different regions or in a different manner as the soluble forms of IgE receptors. Plenum Publishing Corporation, 1997 analytical ultracentrifuge nationallicence anti-IgE monoclonal antibody nationallicence IgE Fc high affinity receptor nationallicence light scattering nationallicence complex nationallicence Liu Jim Department of Pharmaceutical Research & Development, Genentech, Inc., 94080, South San Francisco, California aut Ruppel Jane Bioanalytical Method Development, Genentech, Inc., 94080, South San Francisco, California aut Shire Steven Department of Pharmaceutical Research & Development, Genentech, Inc., 94080, South San Francisco, California aut Pharmaceutical Research Kluwer Academic Publishers-Plenum Publishers 14/10(1997-10-01), 1388-1393 0724-8741 14:10<1388 1997 14 11095 https://doi.org/10.1023/A:1012116604499 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1012116604499 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Liu Jim Department of Pharmaceutical Research & Development, Genentech, Inc., 94080, South San Francisco, California aut NATIONALLICENCE 700 1- Ruppel Jane Bioanalytical Method Development, Genentech, Inc., 94080, South San Francisco, California aut NATIONALLICENCE 700 1- Shire Steven Department of Pharmaceutical Research & Development, Genentech, Inc., 94080, South San Francisco, California aut NATIONALLICENCE 773 0- Pharmaceutical Research Kluwer Academic Publishers-Plenum Publishers 14/10(1997-10-01), 1388-1393 0724-8741 14:10<1388 1997 14 11095 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer