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• W2058577093 abstract "A calmodulin-binding protein called caldesmon was purified from chicken gizzard muscle as the major calmodulin-binding protein in this tissue. Its molecular weight estimated by sodium dodecyl sulfate/polyacrylamide gel electrophoresis was 150,000, and two of these polypeptides constituted the native molecule. Caldesmon is an actin-binding protein also, binding F-actin reversibly in the presence or absence of Ca2+. The interaction of caldesmon with F-actin was abolished by the binding of calmodulin with the caldesmon. Because the interaction between caldesmon and calmodulin was Ca2+-dependent but the interaction between caldesmon and F-actin was not, Ca2+ acts as a flip-flop switch between the formations of two complexes, caldesmon.calmodulin and caldesmon.F-actin: increasing the formation of the former complex at increased Ca2+ level and the formation of the latter complex at decreased Ca2+ level. The equilibrium of the formations of both complexes was achieved at a Ca2+ concentration near 1 microM." @default.
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• W2058577093 date "1981-09-01" @default.
• W2058577093 modified "2023-10-18" @default.
• W2058577093 title "Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin." @default.
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• W2058577093 doi "https://doi.org/10.1073/pnas.78.9.5652" @default.
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