Studies on the phosphorylation of the type I cAMP-dependent protein kinase.
作者： R.L. Geahlen , E.G. Krebs
DOI: 10.1016/S0021-9258(19)70572-9
关键词:
摘要: The regulatory subunit of the type I cAMP-dependent protein kinase (RI) can be separated into multiple forms on isoelectric focusing gels. RI from bovine skeletal muscle gives rise to bands at pI = 5.57 and 5.45. Phosphate determinations indicate that more acidic band contains protein-bound phosphate. rat three 5.57, 5.45, 5.35. two comigrate with labeled isolated soleus muscles were incubated [32P]orthophosphate. is mainly in unphosphorylated state while primarily phosphorylated. At lest 4 mol phosphate incorporated each dimer following extensive phosphorylation by cGMP-dependent vitro. Two phosphopeptides are observed polyacrylamide gels partial proteolysis vitro phosphorylated RI. One these peptides also intact muscles.
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