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Title: Modulation of smooth muscle actomyosin ATPase by thin filament associated proteins. Author: Horiuchi KY, Miyata H, Chacko S. Journal: Biochem Biophys Res Commun; 1986 May 14; 136(3):962-8. PubMed ID: 2941015. Abstract: Caldesmon binds equally to both gizzard actin and actin containing stoichiometric amounts of bound tropomyosin. The binding of caldesmon to actin inhibits the actin-activation of the Mg-ATPase activity of phosphorylated myosin only when the actin contains bound tropomyosin. The reversal of this inhibition requires Ca2+-calmodulin; but it occurs without complete release of bound caldesmon. Although phosphorylation of the caldesmon occurs during the ATPase assay, a direct correlation between caldesmon phosphorylation and the release of the inhibited actomyosin ATPase is not consistently observed.[Abstract] [Full Text] [Related] [New Search]