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• W1505772870 abstract "Caldesmon was purified to homogeneity from both chicken gizzard and bovine aortic smooth muscles. Caldesmon purified from bovine aorta was slightly larger than purified from chicken gizzards (Mr = 140,000) when the two were compared electrophoretically. Caldesmon bound tightly to actin saturating at a molar ratio of 1 monomer per 6.6 actin monomers. Ca2+-calmodulin appeared to reduce the affinity of for actin. Caldesmon was also a potent inhibitor of heavy actomeromyosin ATPase activity producing a maximal effect at a ratio of 1 monomer per 7-10 actin monomers. This effect was also antagonized by Ca2+-calmodulin. While inhibited heavy actomeromyosin ATPase activity, it greatly enhanced binding of both unphosphorylated and phosphorylated heavy meromyosin to actin in the presence of MgATP, reducing the Kd for binding by a factor of 40 for each form of heavy meromyosin. Although we did identify a Ca2+-calmodulin-stimulated caldesmon kinase activity in preparations purified under nondenaturing conditions, we observed no effect of phosphorylation (2 mol of PO4/mol of caldesmon) on the capacity to inhibit heavy actomeromyosin ATPase activity. Our results suggest that could serve some role in smooth muscle function by enhancing cross-bridge affinity while inhibiting actomyosin ATPase activity." @default.
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• W1505772870 date "1986-12-01" @default.
• W1505772870 modified "2023-09-26" @default.
• W1505772870 title "The effects of caldesmon on smooth muscle heavy actomeromyosin ATPase activity and binding of heavy meromyosin to actin." @default.
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• W1505772870 doi "https://doi.org/10.1016/s0021-9258(18)66691-8" @default.
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