Now showing items 1-4 of 4

    • Characterization of a caldesmon fragment that competes with myosin-ATP binding to actin. 

      Velaz, Laly; Chen, Yi-Der; Chalovich, Joseph M. (East Carolina University, 1993-08)
      The protein caldesmon inhibits actin-activated ATP hydrolysis of myosin and inhibits the binding of myosin*ATP to actin. Afragment isolated from a chymotryptic digest of caldesmon contains features of the intact molecule ...
    • The Interaction of Caldesmon with the COOH Terminus of Actin 

      Crosbie, Rachelle; Adams, Susan; Chalovich, Joseph M.; Reisler, Emil (East Carolina University, 1991-10-25)
      Caldesmon interacts with the NH2-terminal region of actin. It is now shown in airfuge centrifugation experiments that modification of the penultimate cysteine residue of actin significantly weakens its binding to caldesmon ...
    • Localization and Characterization of a 7.3-kDa Region of Caldesmon Which Reversibly Inhibits Actomyosin ATPase Activity 

      Chalovich, Joseph M.; Bryan, Joseph; Benson, Caryl E.; Velaz, Laly (East Carolina University, 1992-08-15)
      Cleavage of caldesmon with chymotrypsin yields a series of fragments which bind both calmodulin and actin and inhibit the binding of myosin subfragments to actin and the subsequent stimulation of ATPase activity. Several ...
    • A Long Helix from the Central Region of Smooth Muscle Caldesmon 

      Wang, C.-L. Albert; Chalovich, Joseph M.; Graceffa, Philip; Lu, Renne C.; Mabuchi, Katsuhide; Stafford, Walter F. (East Carolina University, 1991-07-25)
      The central region of smooth muscle caldesmon is predicted to form α-helices on the basis of its primary structure. We have isolated a fragment (CT54) that contains this region. The hydrodynamic properties and the electron ...