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  • Title: pH-dependent changes in structure and RNA-binding activity of casein kinase 2 from Rana temporaria oocytes.
    Author: Kandror KV, Kapkov DV, Turapov OA, Stepanov AS.
    Journal: FEBS Lett; 1991 Jun 03; 283(2):223-6. PubMed ID: 2044760.
    Abstract:
    It is demonstrated by filter-binding assay that casein kinase 2 from Rana temporaria oocytes binds rRNA in vitro with high affinity. Ligand-blotting shows that rRNA-binding activity is inherent to alpha and alpha' subunits of the enzyme. Increase of pH from 6.5 to 7.5 has little effect on casein kinase but completely suppresses rRNA-binding activity of the enzyme. Sedimentation coefficient of casein kinase 2 also depends on pH: at pH 7.5 it is mainly 10 S, and at pH 6.5-18 S. At pH 6.95 the amounts of both forms are equal. The heavy form of casein kinase 2 practically lacks rRNA-binding activity.
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