Abstract
The interaction of immunoglobulin G fractions from the sera and thymus glands of patients with myasthenia gravis with acetylcholine receptors from denervated rat muscle was studied using a combination of immunoprecipitation and an assay for binding to concanavalin A-Sepharose. Results showed that myasthenic IgG distinguishes two different α-bungarotoxin-binding components, each associated with approximately half the total receptor toxin binding capacity. The receptor components can be separated as immune complexes by different properties of binding to concanavalin A and are characterized by different kinetics of toxin binding. The majority of myasthenia gravis sera contain at least two antibodies, directed against determinants on one or both components of the receptor, which do not affect the total binding capacity for α-bungarotoxin. A few sera contain a third antibody type, which prevents the binding of α-bungarotoxin to receptors.
ACKNOWLEDGMENTS We are grateful to G. Genkins, P. Kornfeld, and A. Papatestas for making sera and thymus available for these studies.
- Copyright © 1978 by Academic Press, Inc.
MolPharm articles become freely available 12 months after publication, and remain freely available for 5 years.Non-open access articles that fall outside this five year window are available only to institutional subscribers and current ASPET members, or through the article purchase feature at the bottom of the page.
|
Log in using your username and password
Purchase access
In this issue
Heterogeneity of Acetylcholine Receptors in Denervated Muscle: Interactions of Receptors with immunoglobulin from Patients with Myasthenia Gravis
