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• W1663036315 abstract "Heavy sarcoplasmic reticulum vesicles loaded with 5 mM CaCl2 in the presence of protease inhibitors were phosphorylated by addition of MgATP in the presence or absence of calmodulin. The major site of phosphorylation was a 60-kDa protein. In the absence of added calmodulin, phosphorylation of the 60-kDa protein reached its maximal value (8 pmol of P/mg of membrane protein) at 1 min. In the presence of 1 microM calmodulin, a 2-fold higher level of phosphorylation (16.1 pmol of P/mg of sarcoplasmic reticulum) was reached within a shorter time (10 s). The phosphoprotein was then spontaneously dephosphorylated. The initial rate of Ca2+ release, which was induced by a Ca2+ jump and determined by stopped-flow fluorometry using chlorotetracycline, decreased upon phosphorylation, whereas it was restored upon dephosphorylation. There was good correlation between the amount of P incorporation into the 60-kDa protein and the extent of inhibition of Ca2+ release. In the presence of added calmodulin the protein kinase activity sharply increased in the [Ca2+] range of 0.2-2 microM with a concentration for half-maximal activation at 0.6 microM. On the other hand, the protein phosphatase activity was virtually independent of calmodulin and [Ca2+] in the [Ca2+] range in which protein kinase was activated. The results suggest that the calmodulin-dependent phosphorylation of the 60-kDa protein plays an important role in the regulation of Ca2+ release from sarcoplasmic reticulum." @default.
• W1663036315 created "2016-06-24" @default.
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• W1663036315 date "1986-09-01" @default.
• W1663036315 modified "2023-09-30" @default.
• W1663036315 title "Involvement of 60-kilodalton phosphoprotein in the regulation of calcium release from skeletal muscle sarcoplasmic reticulum." @default.
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• W1663036315 doi "https://doi.org/10.1016/s0021-9258(18)67296-5" @default.
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