The acid stabilization of plasminogen activator inhibitor-1 depends on protonation of a single group that affects loop insertion into beta-sheet A.

@article{Kvassman1995TheAS,
  title={The acid stabilization of plasminogen activator inhibitor-1 depends on protonation of a single group that affects loop insertion into beta-sheet A.},
  author={J O Kvassman and Daniel A Lawrence and Joseph D. Shore},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 46},
  pages={27942-7}
}
The serpin plasminogen activator inhibitor-1 (PAI-1) spontaneously adopts an inactive or latent conformation by inserting the N-terminal part of the reactive center loop as strand 4 into the major beta-sheet (sheet A). To examine factors that may regulate reactive loop insertion in PAI-1, we determined the inactivation rate of the inhibitor in the pH range 4.5-13. Below pH 9, inactivation led primarily to latent PAI-1, and one predominant effect of pH on the corresponding rate constant could be… CONTINUE READING

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 20 extracted citations

New antithrombotic drugs.

Clinical pharmacology and therapeutics • 2009

Similar Papers

Loading similar papers…