Phosphorylation of casein kinase II.

@article{Pale1991PhosphorylationOC,
  title={Phosphorylation of casein kinase II.},
  author={E Paleń and Jolinda A. Traugh},
  journal={Biochemistry},
  year={1991},
  volume={30 22},
  pages={5586-90}
}
Casein kinase II from rabbit reticulocytes is a tetramer with an alpha,alpha' beta 2 or alpha 2 beta 2 structure; the alpha subunits contain the catalytic activity, and the beta subunits are regulatory in nature [Traugh, J.A., Lin, W. J., Takada-Axelrod, F., & Tuazon, P. T. (1990) Adv. Second Messenger Phosphoprotein Res. 24, 224-229]. When casein kinase II is isolated from rabbit reticulocytes by a rapid two-step purification of the enzyme, both the alpha and beta subunits are phosphorylated… CONTINUE READING
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