The polymerization of fibrinogen Dusart (A alpha 554 Arg-->Cys) after removal of carboxy terminal regions of the A alpha-chains.

@article{Siebenlist1993ThePO,
  title={The polymerization of fibrinogen Dusart (A alpha 554 Arg-->Cys) after removal of carboxy terminal regions of the A alpha-chains.},
  author={Kevin R. Siebenlist and Michael W. Mosesson and James P Diorio and Juan Jose Soria and C. Gonz{\'a}lez Soria and Jacques Philippe Caen},
  journal={Blood coagulation & fibrinolysis : an international journal in haemostasis and thrombosis},
  year={1993},
  volume={4 1},
  pages={
          61-5
        }
}
The six polypeptide chains of normal fibrinogen are covalently linked by interchain disulphide bonds, and there are no free sulphydryl groups. Fibrinogen Dusart is a congenital fibrinogen variant in which A alpha 554 Arg is replaced by Cys; albumin is disulphide linked to these fibrinogen molecules, possibly at A alpha 554 Cys. Functionally, Dusart fibrinogen displays markedly abnormal fibrin polymerization, characterized by delayed lateral fibril association and matrix fibre bundles that are… CONTINUE READING

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