Phosphorylase kinase can phosphorylate the inhibitor component of troponin, binding 1 mole of phosphate per mole of TNI.
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Hypothesis-generating for troponin regulation; leaves open in vivo relevance and clinical translation.
Phosphorylase kinase catalyzes the phosphorylation of the inhibitor component (TNI) of troponin in the presence of ATP and Mgz+.Phosphorylation by nonactivated and activated phosphorylase kinase occurs at equal rates with a ratio of activity at pH 6.8 to 8.2 of 0.7.Measurements suggest that 1 mole of phosphate per mole of TN1 is bound after phosphorylation by phosphorylase kinase.Troponin, as isolated, contains endogenous protein-bound phosphate.
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Stull et al. (1972) studied this question.
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