Possible modulation of phosphorylation of acetylcholine receptor-enriched membrane preparations
β Scribed by M. E. Carstens; A. C. Neethling; J. J. F. Taljaard
- Publisher
- Springer
- Year
- 1984
- Tongue
- English
- Weight
- 586 KB
- Volume
- 9
- Category
- Article
- ISSN
- 0364-3190
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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
We have found that the acetylcholine receptor (AChR) of Torpedo californica is phosphorylated and dephosphorylated in situ by a membrane-bound protein kinase and phosphatase [1]. There is increasing evidence that other neurotransmitters [2], light [3-6], polypeptide hormones [7], and growth factors
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