Cleavage of human high molecular weight kininogen by factor XIa in vitro. Effect on structure and function.

@article{Scott1985CleavageOH,
  title={Cleavage of human high molecular weight kininogen by factor XIa in vitro. Effect on structure and function.},
  author={Cheryl F. Scott and Lynn D Silver and A. David Purdon and Robert W. Colman},
  journal={The Journal of biological chemistry},
  year={1985},
  volume={260 19},
  pages={10856-63}
}
We have recently demonstrated that human high molecular weight kininogen (HMWK) is a pro-cofactor that is cleaved by kallikrein to yield a two-chain cofactor (HMWKa) and the nanopeptide bradykinin. This proteolysis enhances its association with an activating surface, an event necessary for expression of its cofactor activity. We now report that factor XIa is capable of hydrolyzing HMWK and releasing bradykinin in a purified system as well as cleaving and inactivating HMWK in a plasma… CONTINUE READING

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