Fibrinogen Detroit - an abnormal fibrinogen with non-functional NH2-terminal polymerization domain

Abstract Fibrinogen Detroit was found to have affinity for thrombin activated fibrinogen-Sepharose conjugates prepared from normal fibrinogen. On the other hand, thrombin activated fibrinogen-Sepharose conjugates prepared from fibrinogen Detroit did not, to any appreciable extent, bind normal fibrinogen nor the plasmic degradation product, Fragment D. It is concluded that the N-DSK domain in fibrinogen Detroit, containing the mutation (Aα 19 Arg → Ser), is abnormal with regard to binding whereas the Fragment D domain has normal binding properties.