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• W2032715302 abstract "Abstract The activity of nonactivated phosphorylase kinase from rabbit skeletal muscle is widely reported to be nearly totally inhibited when free Ca2+ ions are chelated by ethylene glycol bis(β-aminoethyl ether)-N,N′-tetraacetic acid (EGTA). In this report, however, it is shown that prior incubation of nonactivated phosphorylase kinase for a short time with Ca2+ and Mg2+ allows substantial catalytic activity to be expressed in the presence of high concentrations of EGTA in subsequent assays. The divalent metals acted synergistically to promote this EGTA-insensitive activity: incubation with either Ca2+ or Mg2+ alone had only a slight effect. The apparent Ka for Mg2+ was 4 m m , whereas that for Ca2+ was 5 μ m . Induction of the EGTA-insensitive activity by Ca2+ plus Mg2+ was time-dependent and did not plateau after 10 min at either pH 6.8 or 8.2. The formation of this activity was reversed by addition of EGTA and EDTA in excess of both metal ions. A typical specific activity for the EGTA-insensitive activity was on the order of 0.4 μmol phosphate transferred/min/mg at pH 6.8 with phosphorylase as substrate. This specific activity is approximately the same as the Ca2+-dependent activity at pH 6.8 in our buffer system. The EGTA-insensitive activity showed a ratio of activity at pH 6.8 to 8.2 of nearly unity, and the formation of product with time was linear at both pH values. The EGTA-insensitive activity was observable with either glycogen phosphorylase or troponin I as substrates, as well as with autophosphorylation of the phosphorylase kinase." @default.
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• W2032715302 date "1981-07-01" @default.
• W2032715302 modified "2023-09-25" @default.
• W2032715302 title "Synergistic effect of Ca2+ and Mg2+ in promoting an activity of phosphorylase kinase that is insensitive to ethylene glycol bis(β-aminoethyl ether)-N,N′-tetraacetic acid" @default.
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• W2032715302 doi "https://doi.org/10.1016/0003-9861(81)90309-x" @default.
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