Analysis of the functions of the first epidermal growth factor-like domain of factor X.

@article{Rezaie1993AnalysisOT,
  title={Analysis of the functions of the first epidermal growth factor-like domain of factor X.},
  author={Alireza R Rezaie and Pierre F. Neuenschwander and James H Morrissey and Charles T. Esmon},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 11},
  pages={8176-80}
}
Upon activation, factor X participates in the prothrombin activation complex. Similar to 4-carboxyglutamic acid (Gla)-domainless protein C, the Gla-domainless factor X (GDFX) contains a high affinity Ca(2+)-binding site critical for the function of these molecules. In the case of protein C, we recently demonstrated that the high affinity Ca(2+)-binding site critical for activation is outside the first epidermal growth factor (EGF) homology domain. To examine if this is also true for factor X… CONTINUE READING

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