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
Phosphorylation of acetylcholine receptor by endogenous membrane protein kinase in receptor-enriched membranes of Torpedo californica
β Scribed by GORDON, ADRIENNE S.; DAVIS, C. GEOFFREY; MILFAY, DALE; DIAMOND, IVAN
- Book ID
- 109705100
- Publisher
- Nature Publishing Group
- Year
- 1977
- Tongue
- English
- Weight
- 335 KB
- Volume
- 267
- Category
- Article
- ISSN
- 0028-0836
- DOI
- 10.1038/267539a0
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Abstract Ion permeation, triggered by ligandβreceptor interaction, is associated with the primary events of membrane depolarization at the neuromuscular junction and synaptic connections. To explore the possible sites of ion permeation, the longβlived fluorescent probe pyrene (fluorescence lifet
## Abstract Purified postsynaptic membranes can be used as a model system to study the regulation of synaptic membrane proteins. These membranes contain protein kinase activity that phosphorylates the acetylcholine receptor (AChR). We find that diphenylhydantoin (DPH) interacts with these membranes