Modulation of plasminogen activator inhibitor 1 by Triton X-100--identification of two consecutive conformational transitions.

@article{Gils1998ModulationOP,
  title={Modulation of plasminogen activator inhibitor 1 by Triton X-100--identification of two consecutive conformational transitions.},
  author={Ann Gils and Paul J Declerck},
  journal={Thrombosis and haemostasis},
  year={1998},
  volume={80 2},
  pages={286-91}
}
Plasminogen activator inhibitor-1 (PAI-1) is a unique member of the serpin superfamily because of its conformational and functional flexibility. In the present study, we have evaluated the influence of the non-ionic detergent Triton X-100 (TX-100) on the functional stability and conformational transitions of PAI-1. At 37 degrees C, TX-100 induced a concentration-dependent decrease of the functional half-life of PAI-1 resulting in half-lives of 177 +/- 54 min (mean +/- SD, n = 3), 19 +/- 2 min… CONTINUE READING

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