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
Protein inhibitors of phosphorylase phosphatase and cyclic AMP-dependent protein kinase from rabbit skeletal muscle
β Scribed by Chiharu Nakai; Walter Glinsmann
- Publisher
- Springer
- Year
- 1977
- Tongue
- English
- Weight
- 514 KB
- Volume
- 15
- Category
- Article
- ISSN
- 0300-8177
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## Abstract A protein kinase that catalyzes the phosphorylation of histone was partially purified from rat thymus, and the rate of histone phosphorylation was stimulated threeβ to fourfold by 1 Γ 10^β6^ M adenosine 3β²,5β²βmonophosphate (cyclic AMP). Thymic protein kinase was more active than the enz
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
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