Summary
The abnormal fibrinogen Haifa is characterized by the fact that calcium present during
enzymatic digestion by plasmin does not protect the Haifa D gamma chain against further
plasmin attack as it does in normal molecules.
Since calcium binding to fibrinogen, ADP - platelet aggregation cofactor activity
and gamma dimerization process induced by factor XIIIa are normal for fibrinogen Haifa,
the corresponding sequences in the gamma chain are not involved. It seems rather that
the anomaly resides near the gamma 302 plasmin cleavage site that is protected when
calcium is bound to the gamma chain and that this affects the availability of the
polymerization site located in the C terminal part of the chain.
Keywords
Dysfibrinogenemia - Fibrinogen - Fibrinogen degradation products - Fibrinolysis