Antistasin, a leech-derived inhibitor of factor Xa. Kinetic analysis of enzyme inhibition and identification of the reactive site.

@article{Dunwiddie1989AntistasinAL,
  title={Antistasin, a leech-derived inhibitor of factor Xa. Kinetic analysis of enzyme inhibition and identification of the reactive site.},
  author={Christopher T. Dunwiddie and Nancy A. Thornberry and Herbert G. Bull and Mohinder Sardana and Paul A. Friedman and John William Jacobs and E Hatheway Simpson},
  journal={The Journal of biological chemistry},
  year={1989},
  volume={264 28},
  pages={16694-9}
}
Antistasin is a 119-amino acid protein isolated from the salivary glands of the Mexican leech Haementeria officinalis. The determination of the primary structure of antistasin revealed that the protein is highly disulfide-bonded with a 2-fold internal homology. Antistasin exhibits a potent anticoagulant activity purportedly due to the selective inhibition of Factor Xa (Tuszinsky, G. P., Gasic, T. B., and Gasic, G. J. (1987) J. Biol. chem. 262, 9718-9723). In the present study a detailed kinetic… CONTINUE READING
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