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Hereditary dysfibrinogenaemia: structural and functional studies on three fibrinogen variants.

Dysfunctional fibrinogens occurring in three unrelated families were studied. Fibrinogen Erfurt I consists of B beta chains with a slightly lower molecular mass than normal. The same structural abnormality was also detected in fibrin beta chains. The variant is present in platelets too. Fibrinogen Erfurt II is characterized by the absent thrombin-induced release of FPA. With fibrinogen Berlin cleavage of the B beta chains by thrombin is slow but complete. All carriers of the three abnormal fibrinogens seem to be heterozygous for the underlying mutant gene.