Fibrinopeptide A, human is a 16-residue short polypeptide cleaved from fibrinogen by thrombin. Fibrinopeptide A, human locates at the NH2-termini of the Aα chain.
The conversion of monomeric fibrinogen into polymeric fibrin is mediated by thrombin, which binds to the central region of fibrinogen and catalyzes cleavage of the 2 short peptides, the 16-residue fibrinopeptide A (FpA) and the 14-residue fibrinopeptide B (FpB), located at the NH2-termini of the Aα and Bβ chains, respectively[1].
Fibrinopeptide A (FPA) is a small polypeptide cleaved from fibrinogen by thrombin, has a short half-life, and is considered a sensitive biochemical marker of thrombin activity, fibrin generation, and ongoing thrombosis[2].
[1]. Riedel T, et al. Fibrinopeptides A and B release in the process of surface fibrin formation. Blood. 2011 Feb 3;117(5):1700-6. [2]. Manolis AS, et al. Plasma level changes of fibrinopeptide A after uncomplicated coronary angioplasty. Clin Cardiol. 1993 Jul;16(7):548-52.