The role of caldesmon in the regulation of smooth muscle contraction was investigated in chemically skinned smooth muscle fibres from the guinea-pig taenia coli. A 19-kDa C-terminal fragment of caldesmon gave a minor (<5%) reduction of force in fully thiophosphorylated fibres, but reduced force by about 50% at intermediate activation levels without affecting the level of light chain phosphorylation. An extraction procedure was developed using incubation in solutions containing high Mg2+ concentrations. Protein analysis revealed a selective decrease in the amount of caldesmon in the fibres. Maximal active force per cross-sectional area was unaffected. The Ca2+ dependence of active force was shifted towards lower Ca2+ concentrations and becam...
AbstractCaldesmon was phosphorylated up to 1.2 molPi/mol using a partially purified endogenous kinas...
Smooth muscle thin filaments are made up of actin, tropomyosin, the inhibitory protein caldesmon and...
SIGLEAvailable from British Library Document Supply Centre-DSC:DXN022102 / BLDSC - British Library D...
AbstractSmooth muscle caldesmon inhibits actomyosin MgATPase in the absence of Ca2+ and is the key r...
Several regions within the 35-kDa COOH-terminal portion of caldesmon have been implicated in the abi...
Caldesmon inhibits actomyosin ATPase and filament sliding in vitro, and therefore may play a role in...
Caldesmons are a family of proteins that bind actin with high affinity as well as myosin, tropomyosi...
AbstractThe viscosity of chicken gizzard smooth muscle tropomyosin is enhanced 4.7-fold in the absen...
Previously we showed that stiffness of relaxed fibers and active force generated in single skinned f...
AbstractInteraction of smooth muscle caldesmon with calmodulin, troponin C, S-100 protein and 67 kDa...
AbstractCalponin (4.1–5.9 μM, pig stomach) inhibited maximal shortening velocity (Vmax) by 20–25% wi...
Thesis (M.A.)--Boston UniversityPLEASE NOTE: Boston University Libraries did not receive an Authoriz...
The protein caldesmon inhibits actin-activated ATP hydrolysis of myosin and inhibits the binding of ...
Caldesmon is universally associated with smooth muscle thin filaments, and reportedly interacts with...
AbstractCaldesmon induces inhibition of MG2+-ATPase activity of actomyosin and relaxation of skinned...
AbstractCaldesmon was phosphorylated up to 1.2 molPi/mol using a partially purified endogenous kinas...
Smooth muscle thin filaments are made up of actin, tropomyosin, the inhibitory protein caldesmon and...
SIGLEAvailable from British Library Document Supply Centre-DSC:DXN022102 / BLDSC - British Library D...
AbstractSmooth muscle caldesmon inhibits actomyosin MgATPase in the absence of Ca2+ and is the key r...
Several regions within the 35-kDa COOH-terminal portion of caldesmon have been implicated in the abi...
Caldesmon inhibits actomyosin ATPase and filament sliding in vitro, and therefore may play a role in...
Caldesmons are a family of proteins that bind actin with high affinity as well as myosin, tropomyosi...
AbstractThe viscosity of chicken gizzard smooth muscle tropomyosin is enhanced 4.7-fold in the absen...
Previously we showed that stiffness of relaxed fibers and active force generated in single skinned f...
AbstractInteraction of smooth muscle caldesmon with calmodulin, troponin C, S-100 protein and 67 kDa...
AbstractCalponin (4.1–5.9 μM, pig stomach) inhibited maximal shortening velocity (Vmax) by 20–25% wi...
Thesis (M.A.)--Boston UniversityPLEASE NOTE: Boston University Libraries did not receive an Authoriz...
The protein caldesmon inhibits actin-activated ATP hydrolysis of myosin and inhibits the binding of ...
Caldesmon is universally associated with smooth muscle thin filaments, and reportedly interacts with...
AbstractCaldesmon induces inhibition of MG2+-ATPase activity of actomyosin and relaxation of skinned...
AbstractCaldesmon was phosphorylated up to 1.2 molPi/mol using a partially purified endogenous kinas...
Smooth muscle thin filaments are made up of actin, tropomyosin, the inhibitory protein caldesmon and...
SIGLEAvailable from British Library Document Supply Centre-DSC:DXN022102 / BLDSC - British Library D...