Study of the subunit interactions in myosin phosphatase by surface plasmon resonance.

@article{Tth2000StudyOT,
  title={Study of the subunit interactions in myosin phosphatase by surface plasmon resonance.},
  author={Agnes Hofmeister T{\'o}th and Erzs{\'e}bet Kiss and Friedrich W Herberg and P{\'a}l Gergely and David J. Hartshorne and Ferenc Erd{\"o}di},
  journal={European journal of biochemistry},
  year={2000},
  volume={267 6},
  pages={1687-97}
}
The interactions of the catalytic subunit of type 1 protein phosphatase (PP1c) and the N-terminal half (residues 1-511) of myosin phosphatase target subunit 1 (MYPT1) were studied. Biotinylated MYPT1 derivatives were immobilized on streptavidin-biosensor chips, and binding parameters with PP1c were determined by surface plasmon resonance (SPR). The affinity of binding of PP1c was: MYPT11-296 > MYPT11-38 > MYPT123-38. No binding was detected with MYPT11-34, suggesting a critical role for… CONTINUE READING