In vitro and in vivo phosphorylation of myelin basic protein by exogenous and endogenous adenosine 3':5'-monophosphate-dependent protein kinases in brain.

@article{Miyamoto1974InVA,
  title={In vitro and in vivo phosphorylation of myelin basic protein by exogenous and endogenous adenosine 3':5'-monophosphate-dependent protein kinases in brain.},
  author={Eishichi Miyamoto and S. Kakiuchi},
  journal={The Journal of biological chemistry},
  year={1974},
  volume={249 9},
  pages={2769-77}
}
Myelin basic protein, an encephalitogenic protein, was phosphorylated by adenosine 3’: 5’-monophosphate (cyclic AMP)-dependent protein kinase from bovine brain, and its phosphorylation was stimulated by cyclic AMP. The ability of the protein to serve as substrate for the protein kinase was comparable to that of histone fractions and better than that of casein, protamine, or phosvitin. The apparent K, of the enzyme for the protein was 2 X 1O-5 M. The protein phosphorylated by the protein kinase… CONTINUE READING

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  • E. MIYAMOTO, G. L. PETZOLD, J. F. Kuo
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