![]() |
|
|
Molecular Pharmacology, Vol 14, 60-68, Copyright © 1978 by the American Society for Pharmacology and Experimental Therapeutics
1 Department of Pharmacology, Mount Sinai School of Medicine, City University of New York, New York,
New York 10029
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
-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
-bungarotoxin. A few sera contain a third antibody type, which prevents the binding of
-bungarotoxin to receptors.
Note:
ACKNOWLEDGMENTS
We are grateful to G. Genkins, P. Kornfeld, and
A. Papatestas for making sera and thymus available
for these studies.