Drosophila kinesin minimal motor domain expressed in Escherichia coli. Purification and kinetic characterization.

@article{Huang1994DrosophilaKM,
  title={Drosophila kinesin minimal motor domain expressed in Escherichia coli. Purification and kinetic characterization.},
  author={Terry Y Huang and David D Hackney},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 23},
  pages={16493-501}
}
A truncated motor domain of the alpha subunit of Drosophila kinesin was obtained by expression in Escherichia coli and purified to homogeneity in the presence of MgATP. This domain (designated DKH340) extends from the N terminus to amino acid 340. The isolated protein contains a stoichiometric level of tightly bound ADP and has a low basal rate of ATP hydrolysis of 0.029 +/- 0.002 s-1 in the absence of microtubules. The rate of release of bound ADP is 0.026 +/- 0.003 s-1. The approximate… CONTINUE READING

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