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- W2016652272 abstract "Abstract Phosphorylase kinase, (αβγδ)4, binds in two subsequent steps 2 mol Ca2+/monomer (αβγδ) to high affinity sites, N1a, and 1–2 mol to low affinity sites, N2. Analogously, the holotroponin TI2C binds 2 mol Ca2+ to high affinity and further 2 mol to low affinity sites. In both protein complexes Ca2+ binds to one specific subunit: in phosphorylase kinase to the δ- and in troponin TI2C to the C-subunit. In both proteins the high affinity sites show Ca2+-Mg2+ competition. Cooperative interactions are observable at the low affinity Mg2+ inducible sites in phosphorylase kinase and at the high affinity sites in troponin. The isolated δ subunit binds 2 mol Ca2+ with low affinity in a positive cooperative manner. Ca2+ binding to the high affinity sites inhibits the phosphorylation of the I subunits of troponin but stimulates that of the α and β subunits of phosphorylase kinase. Phosphorylase kinase exhibits three partial activities: A0, A1 and A2. A0 is Ca2+ independent whereas activation of A1 can be correlated to Ca2+ binding to the sites, N1a, and activation of A2 with Ca2+ binding to the sites, N2. Both Ca2+ binding proteins, δ and troponin C, can activate the kinase activity of calsequestrin which is a membrane component of the sarcoplasmic reticulum." @default.
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- W2016652272 date "1980-01-01" @default.
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- W2016652272 title "Troponin C and calcium dependent regulator protein, two ancestral skeletal muscle calcium binding proteins" @default.
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- W2016652272 doi "https://doi.org/10.1016/0303-2647(80)90029-5" @default.
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