Sarcomeric binding pattern of exogenously added intact caldesmon and its C-terminal 20-kDa fragment in skinned fibers of skeletal muscle

@article{Frisbie1999SarcomericBP,
  title={Sarcomeric binding pattern of exogenously added intact caldesmon and its C-terminal 20-kDa fragment in skinned fibers of skeletal muscle},
  author={S. M. Frisbie and Mary C. Reedy and Leepo C. Yu and Bernhard Brenner and Joseph M Chalovich and Theresia Kraft},
  journal={Journal of Muscle Research & Cell Motility},
  year={1999},
  volume={20},
  pages={291-303}
}
Intact caldesmon and particularly the actin-binding C-terminal fragment (20-kDa) of caldesmon have been shown in skeletal muscle fibers to selectively displace low affinity, weakly bound cross-bridges from actin without significantly altering the actin attachment of force producing, strong binding cross-bridges (Brenner et al., 1991; Kraft et al., 1995a… CONTINUE READING