Characterization of complex formation by humanized anti-IgE monoclonal antibody and monoclonal human IgE.
Biochemistry
; 34(33): 10474-82, 1995 Aug 22.
Article
em En
| MEDLINE
| ID: mdl-7654701
ABSTRACT
The interaction of human IgE with high-affinity IgE Fc receptors on cells of the immune system plays an essential role in the type I hypersensitivity reaction. A proposed therapy is to use an anti-IgE monoclonal antibody to block the binding of IgE to its high-affinity receptor on mast cells and basophils, thus preventing subsequent release of the inflammatory agents after exposure to allergen. We report here the solution characteristics of immune complexes formed by a humanized anti-IgE monoclonal antibody (rhuMAb E25) and IgE using sedimentation analysis and size exclusion chromatography. We demonstrate that the rhuMAb E25 is able to form a variety of complexes with IgE at different molar ratios. The largest complex was identified by sedimentation equilibrium analysis as a heterohexamer with very high stability. The intermediate complex formed when one of the interacting components is in large molar excess appears to have a trimeric structure. The high-affinity interaction of rhuMAb E25 and IgE has also been confirmed. Furthermore, by using hydrodynamic modeling, we show that the largest complex may be represented by a cyclic structure.
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Base de dados:
MEDLINE
Assunto principal:
Imunoglobulina E
/
Anticorpos Anti-Idiotípicos
/
Anticorpos Monoclonais
Idioma:
En
Ano de publicação:
1995
Tipo de documento:
Article