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
A cyclic AMP-mediated intersubunit disulfide crosslinking reaction of the regulatory subunit of type II cyclic AMP-dependent protein kinase
โ Scribed by Chi-Kuang Huang
- Book ID
- 115913044
- Publisher
- Elsevier Science
- Year
- 1982
- Tongue
- English
- Weight
- 1012 KB
- Volume
- 143
- Category
- Article
- ISSN
- 0014-5793
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๐ SIMILAR VOLUMES
Intact S49 mouse lymphoma cells were used as a model system to study the effects of cyclic AMP (CAMP) and its analogs on the phosphorylation of regulatory (R) subunit of type I CAMP-dependent protein kinase. Phosphorylation of R subunit was negligible in mutants deficient in adenylate cyclase; low l
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