| Autor: |
Squinto, Stephen, McLane, Jerry, Held, Irene |
| Zdroj: |
Neurochemical Research; Feb1981, Vol. 6 Issue 2, p203-211, 9p |
| Abstrakt: |
The in vitro phosphorylation of a 40,400-dalton, cytosolic polypeptide from the soleus muscle of the rat is increased twofold within 24 hr after cutting the motor nerve fibers to this muscle. This involves an ATP:phosphotransferase reaction which we have reported to be inhibited by a specific cyclic AMP-dependent protein kinase inhibitor. The phosphorylated polypeptide does not electrophoretically comigrate on SDS-polyacrylamide gels with the 38,000-dalton catalytic subunit of cyclic AMP-dependent protein kinase which is known to undergo a site-specific autophosphorylation in skeletal muscle. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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