Cardiac V1 and V3 myosins differ in their hydrolytic and mechanical activities in vitro.

@article{Vanburen1995CardiacVA,
  title={Cardiac V1 and V3 myosins differ in their hydrolytic and mechanical activities in vitro.},
  author={Peter C Vanburen and David Eisenbud Joe Harris and Norman R. Alpert and David M. Warshaw},
  journal={Circulation research},
  year={1995},
  volume={77 2},
  pages={439-44}
}
The two mammalian cardiac myosin heavy chain isoforms, alpha and beta, have 93% amino acid homology, but hearts expressing these myosins exhibit marked differences in their mechanical activities. To further understand the function of these cardiac myosins as molecular motors, we compared the ability of these myosins to hydrolyze ATP and to both translocate actin filaments and generate force in an in vitro motility assay. V1 myosin has twice the actin-activated ATPase activity and three times… CONTINUE READING