Phosphorylation increases α-bungarotoxin binding to acetylcholine receptor-enriched membrane preparations
✍ Scribed by M. E. Carstens; J. J. F. Taljaard; A. C. Neethling
- Publisher
- Springer
- Year
- 1983
- Tongue
- English
- Weight
- 375 KB
- Volume
- 56
- Category
- Article
- ISSN
- 0300-8177
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
When the acetylcholine receptor (AChR) from Torpedo is phosphorylated, ATP is found to bind non-covalently to the preparation. After correction is made for this binding of ATP, the phosphorylation reaction has a Km of 0,16 mM, a pH optimum of 8,6 and reaches maximal activity within 3 min. The intrin
This method involves the irreversible formation of a complex between ?labeled cu-bungarotoxin and the acetylcholine receptor in either its membranebound or purified state. The separation of the labeled toxin-receptor complex from unreacted toxin is accomplished by chromatography on carboxymethylcell
## 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