Identification of glycyrrhizin-binding protein kinase as casein kinase II and characterization of its associated phosphate acceptors in mouse liver.

@article{Harada1996IdentificationOG,
  title={Identification of glycyrrhizin-binding protein kinase as casein kinase II and characterization of its associated phosphate acceptors in mouse liver.},
  author={Sachiko Harada and Ayako Karino and Yuhei Shimoyama and Fazel Shamsa and Kenzo Ohtsuki},
  journal={Biochemical and biophysical research communications},
  year={1996},
  volume={227 1},
  pages={102-9}
}
Two forms (G-I and G-II kinases) of casein kinase II(CK-II) in a partially purified CK-II fraction (Mono Q fraction) of mouse liver were separated by means of glycyrrhizin (GL)-affinity column chromatography. Biochemical characterization revealed that these two GL-binding kinases were identical to CK-II. Two phosphate acceptors [p99 (pI 7.0) and p56] copurified with CK-II were identified as ERp99 (Hsp-90-family protein) and calreticulin, respectively. Another protein [p100 (pI 9.0)], which… CONTINUE READING
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