Thrombin cleavage enhances exposure of a heparin binding domain in the N-terminus of the fibrin beta chain.

@article{Odrljin1996ThrombinCE,
  title={Thrombin cleavage enhances exposure of a heparin binding domain in the N-terminus of the fibrin beta chain.},
  author={Tatjana M. Odrljin and John R. Shainoff and Sarah O Lawrence and Patricia J. Simpson-Haidaris},
  journal={Blood},
  year={1996},
  volume={88 6},
  pages={
          2050-61
        }
}
Thrombin (IIa)-cleavage of fibrinogen (FBG) to form polymerized fibrin promotes endothelial cell spreading, proliferation, and von Willebrand factor release, requiring the exposure of the beta 15-42 domain. Studies reported here indicate that IIa-cleavage of fibrinopeptide B enhances exposure of a heparin binding domain at the beta 15-42 neo-N-terminus of fibrin. Crossed immunoelectrophoresis showed heparin-induced mobility shifts indicative of complexing with FBG and with N-terminal CNBr… CONTINUE READING
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