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- W2071586220 abstract "Smooth muscle caldesmon was phosphorylated by protein kinase C up to 1.90 mol P/mol caldesmon. Phosphorylated caldesmon was completely digested by trypsin and the produced phosphopeptides were purified by C-8 and C-18 reverse phase chromatography. Four phosphopeptides were isolated. The amino acid sequences of these peptides were determined and two phosphoserines were identified. Both were localized in the C-terminal domain at serine-587 and serine-726. By following the time course of phosphorylation, serine-587 was found to be the preferred site. Effects of the phosphorylation of caldesmon by protein C on the inhibition of acto-H-meromyosin ATPase activity was also examined. While unphosphorylated caldesmon inhibited the ATPase activity by 60%, phosphorylated caldesmon hardly inhibited the ATPase activity. Therefore, it was concluded that the phosphorylation at serine-726 and serine-587 reverses the inhibitory activity of caldesmon." @default.
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- W2071586220 date "1991-08-01" @default.
- W2071586220 modified "2023-10-18" @default.
- W2071586220 title "Determination of the phosphorylation sites of smooth muscle caldesmon by protein kinase C" @default.
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- W2071586220 doi "https://doi.org/10.1016/0003-9861(91)90232-8" @default.
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