Anti-Human IgE Monoclonal Antibodies Recognizing Epitopes Related to the Binding Sites of High and Low Affinity IgE Receptors

Author:

Takemoto Hiroshi1,Nishimura Shinji2,Kosada Yumi3,Hata Satoshi3,Takagi Shin3,Hosoi Susumu4,Ezumi Kiyoshi1,Ide Misao1,Harada Shigenori3

Affiliation:

1. Shionogi Research Laboratories; Shionogi and Co., Ltd.; Settsu Osaka 566 Japan

2. Department of Diagnostics; Shionogi and Co., Ltd.; Settsu Osaka 566 Japan

3. Shionogi Institute for Medical Science; Shionogi and Co., Ltd.; Settsu Osaka 566 Japan

4. Ohtsu Red Cross Hospital; Ohtsu Shiga 520 Japan

Publisher

Wiley

Subject

Virology,Immunology,Microbiology

Reference33 articles.

1. Conformational differences of human IgE on hydrophobic and hydrophilic solid phases detected by monoclonal antibodies;Anfosso;Mol. Immunol.,1987

2. Interaction of IgE with its high-affinity receptor;Baird;Structural basis and requirements for effective cross-linking. Int. Arch. Allergy Sppl. Immunol.,1989

3. IgE has a bent conformation before and after binding to its high affinity receptor (FcεRI) on RBL cells;Baird;FASEB J.,1990

4. Characterization of truncated alpha chain products from human, rat, and mouse high affinity receptor for immunoglobulin E;Blank;J. Biol. Chem.,1991

5. Inhibition of mast cell sensitization in vitro by a human immunoglobulin epsilon-chain fragment synthesized in Escherichia coli.;Coleman;Eur. J. Immunol.,1985

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