Oct 1, 1989

A monoclonal antibody directed against the beta 1-adrenergic receptor from turkey erythrocyte membranes

Hybridoma
M P ChapotO Durieu-Trautmann

Abstract

A monoclonal antibody was raised against the affinity purified beta 1-adrenergic receptor from turkey erythrocytes. This antibody, B120, of the IgG1 isotype, precipitates the photoaffinity-labeled purified receptor and the corresponding binding activity. The antibody recognizes the 42 kDa component of the receptor of erythrocyte membranes, after electrotransfer on nitrocellulose. B120 does not inhibit binding of dihydroalprenolol on membranes and has no effect on the activity of adenylate cyclase. Since specific immunofluorescence was detected only after ethanol treatment of the erythrocytes, the epitope recognized by B120 appears not to be accessible at the cell surface.

Mentioned in this Paper

Monoclonal Antibodies
Immunofluorescence Assay
Ethanol
Tissue Membrane
Ethanol Measurement
ARID1A
Antigenic Specificity
Immunoglobulin Isotypes
IgG1
Adrenergic Receptor

About this Paper

Related Feeds

Adrenergic Receptors: Trafficking

Adrenergic receptor trafficking is an active physiological process where adrenergic receptors are relocated from one region of the cell to another or from one type of cell to another. Discover the latest research on adrenergic receptor trafficking here.