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  • Title: Kinetics of calcium and calmodulin-dependent protein kinase III from embryonic chicken leg muscle cells.
    Author: Riis B, Nygård O.
    Journal: FEBS Lett; 1997 Apr 21; 407(1):21-4. PubMed ID: 9141474.
    Abstract:
    Embryonic chicken muscle cells (CELM) contain the calmodulin-dependent protein kinase that specifically phosphorylates eukaryotic elongation factor 2. The kinase requires Ca2+ and maximum activity in CELM was observed at 10 microM Ca2+. The ATP concentration required for half the maximum activity of CaM PKIII in CELM was calculated to be 0.15 mM. In CELM, dephosphorylation of eEF-2 was catalyzed by phosphoprotein phosphatase PP2A alone. The activity of PP2A was relatively low and the half-life of added phosphorylated eEF-2 was more than 15 min. Due to the low phosphoprotein phosphatase activity, inhibition of the PP2A activity by addition of okadaic acid had little effect on the eEF-2 phosphorylation kinetics.
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