title: Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin.
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.
mesh_terms: D000199:Actins / Q000378:metabolism*; D000818:Animals; D002118:Calcium / Q000378:metabolism*; D002148:Calmodulin-Binding Proteins; D002352:Carrier Proteins / Q000302:isolation & purification* / Q000378:metabolism; D002645:Chickens; D005895:Gizzard, Avian / Q000032:analysis*; D008970:Molecular Weight
chemical_list: D000199:Actins; D002148:Calmodulin-Binding Proteins; D002352:Carrier Proteins; D002118:Calcium