Kinetic studies on the association and dissociation of myosin subfragment 1 and actin.

@article{Taylor1991KineticSO,
  title={Kinetic studies on the association and dissociation of myosin subfragment 1 and actin.},
  author={Edwin W. Taylor},
  journal={The Journal of biological chemistry},
  year={1991},
  volume={266 1},
  pages={294-302}
}
The reactions of pyrene-labeled actin with myosin subfragment 1 (S1) and S1-ligand complexes at low ionic strength are described by the schemes [formula: see text] where M refers to a myosin head; A is actin; L is ligand; the asterisk refers to a high fluorescence state of actin; and K1 and K3 are association constants. K1 is reduced approximately 10-fold for M.ADP or M.pyrophosphate versus M alone. The rate constant of the isomerization step (k2) is 150-200 s-1 for A*M, A*M.ADP, and A*M… CONTINUE READING