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Primary Polymerization Sites in the D-Domain of Human Fibrinogen

  • C. S. Ciernievski
  • A. Z. Budzynski
Conference paper

Abstract

The conversion of fibrinogen into a fibrin clot is initiated by the limited thrombin proteolysis resulting in the release of fibrinopeptide A and the exposure of NHS-terminal polymerization sites “A” in the E domain of the fibrinogen molecule.’ Complementary polymerization sites “a” capable of interacting with the NHL-terminal sites have been attributed to the D domain, but their exact location in the fibrinogen molecule is uncertain.2-5 There are inconsistent preliminary data indicating that sites “a” may be present in sequences either γ96-2644 or γ266-411.5 The present studies were initiated to assess this discrepancy and identify the location of a polymerization sites “a” in the D domain.

Keywords

Fibrin Clot Human Fibrinogen Polymerization Site Fibrinogen Molecule Disuccinimidyl Suberate 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Japan 1992

Authors and Affiliations

  • C. S. Ciernievski
    • 1
  • A. Z. Budzynski
    • 2
  1. 1.Department of BiophysicsMedical School in LodzPoland
  2. 2.Department of BiochemistryTemple University School of MedicinePhiladelphiaUSA

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