Journal article
Kinetics of ligand binding to the type 1 Fc sub( epsilon ) receptor on mast cells
Biochemistry (Easton), Vol.30(14), pp.3473-3481
01 Jan 1991
Abstract
Rates of association and dissociation of several specific monovalent ligands to and from the type I Fc sub( epsilon ) receptor (Fc sub( epsilon )RI) were measured on live mucosal type mast cells of the rat line RBL-2H3. The ligands employed were a monoclonal murine IgE and Fab fragments prepared from three different, Fc sub( epsilon )RI-specific monoclonal IgG class antibodies. These monoclonals (designated H10, J17, and F4) were shown previously to trigger mediator secretion by RBL-2H3 mast cells upon binding to and dimerization of the Fc sub( epsilon )RI. Analysis of the kinetics shows that the minimal mechanism to which all data can be fitted involves two consecutive steps: namely, ligand binding to a low-affinity state of the receptor, followed by a conformational transition into a second, higher affinity state h of the receptor-ligand complex.
Metrics
7 Record Views
Details
- Title
- Kinetics of ligand binding to the type 1 Fc sub( epsilon ) receptor on mast cells
- Creators
- E OrtegaR Schweitzer-StennerI Pecht
- Publication Details
- Biochemistry (Easton), Vol.30(14), pp.3473-3481
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]
- Identifiers
- 991019196806504721