Polymerization and in vitro motility properties of yeast actin: a comparison with rabbit skeletal alpha-actin.

@article{Kim1996PolymerizationAI,
  title={Polymerization and in vitro motility properties of yeast actin: a comparison with rabbit skeletal alpha-actin.},
  author={Eldar Kim and Connie J. Miller and Emil Reisler},
  journal={Biochemistry},
  year={1996},
  volume={35 51},
  pages={16566-72}
}
Actin purified from the yeast (Saccharomyces cerevisae) was polymerized faster than rabbit skeletal alpha-actin by MgCl2. The two actins polymerized at similar rates in the presence of CaCl2. Yeast actin, up to 25 microM, was not polymerized by KCl (100-300 mM); the monovalent salt also inhibited the MgCl2-induced polymerization of actin. The local… CONTINUE READING