Fibrinogen Seattle Releases Half the Normal Amount of Fibrinopeptide B

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Abstract
Fibrinogen Seattle, a clinically silent, slow-clotting dysfibrinogen, releases 50% of the normal amount of fibrinopeptide B as assessed by amino acid analysis. The reduced dysfibrin exhibited equal quantities of chains with Bβ- and β-charge mobility on polyacrylamide gel electrophoresis in 2 Murea at low pH. By these same techniques, the release of fibrinopeptide A was normal. Clots formed by repolymerizing the throm-bin and batroxobin dysfibrin monomers showed a maximal turbidity that was lower than normal. Fibrinogen Seattle was indistinguishable from normal Fibrinogen by radial immunodiffusion and immunoelectrophoresis. Degradation by plasmin and transamination by factor XlIIa were normal. The characteristics of Fibrinopeptide release by fibrinogen Seattle distinguish it from other reported dysfibrinogens.