## Abstract Conditions are described for an assay that allows the percent inhibition of α‐bungarotoxin binding to acetylcholine receptors by antisera and monovalent antigen‐binding fragments of antibody molecules (Fab) to be determined. Anti‐Torpedo californica acetylcholine‐receptor antisera, prep
A possible modulation of acetylcholine receptors of embryonic chick muscle cells by α-bungarotoxin
✍ Scribed by Elson, Hannah Friedman
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1979
- Tongue
- English
- Weight
- 631 KB
- Volume
- 10
- Category
- Article
- ISSN
- 0091-7419
No coin nor oath required. For personal study only.
✦ Synopsis
Acetylcholine receptors were assayed with a-bugarotoxin o n embryonic chick skeletal muscle growing in primary cell culture. Toxin was bound specifically to muscle cells and could be competed with D-tubocurarine. Two dissociation constants were obtained by equilibrium binding: 7.2 X 10-9M and 2.7 x 10W7M at 25OC. Two sets of rate constants were also obtained from dissociation kinetics. There are five times more low affinity sites o n cells than high affinity sites. The average density of high-affinity receptors is about 200/pmz.
A time course of toxin binding to receptors at 37°C vs 25°C in growth medium revealed that under conditions permitting growth and metabolism, toxin bound t o cells was lost. The possibility that the growth medium was inactivating toxin molecules was ruled out by showing that unbound toxin molecules in the medium were fully capable of binding to fresh cultures.
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