The phosphorylative neuromodulation of the regulatory subunit of protein kinase type II (R-II) in cytosolic fractions from denervated and sham-operated, contralateral soleus muscles of the rat was evaluated. The denervation-induced increase in the 32P-phosphorylation of R-II is not related to an inc
โฆ LIBER โฆ
Temporal relationship between nerve-stump-length-dependent changes in the autophosphorylation of a cyclic AMP-dependent protein kinase and the acetylcholine receptor content in skeletal muscle
โ Scribed by Scott T. Sayers; Hock C. Yeoh; Jerry A. McLane; Irene R. Held
- Publisher
- Springer
- Year
- 1988
- Tongue
- English
- Weight
- 838 KB
- Volume
- 13
- Category
- Article
- ISSN
- 0364-3190
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When soluble proteins in cytosolic fractions of rat soleus muscles are 32P-phosphorylated in vitro by an ATP:protein phosphotransferase reaction, the major substrate is a 56-kilodalton (56K) protein. As we have also reported previously, the onset and development of increased 32P-phosphorylation of t