Fibrinogen Fraction I from Bovine Plasma, 1g

Fibrinogen is a blood protein that is involved in clotting and is converted to fibrin by thrombin. Fibrinogen has an approximate molecular weight of 340 kDa. It consists of three non-identical pairs of disulfidebonded chains. The a-chain has an approximate molecular weight of 63.5 kDa, the b-chain 56 kDa, and the g-chain 47 kDa. At the amino termini, the three chains are connected in a dimeric disulfide knot (DSK). A second DSK occurs later in the molecule. Fibrinogen has approximately 4% carbohydrate content. Fibrinogen has been used in studies of haemostatic therapy in surgical and massive trauma patients. These studies have shown that fibrinogen may prove to be more superior in stopping blood loss when compared to using fresh frozen plasma (FFP). Fibrinogen is an acute phase protein that is part of the coagulation cascade of proteins. The end result of the cascade is the production of thrombin that converts fibrinogen to fibrin. Thrombin rapidly proteolyzes fibrinogen, releasing fibrinopeptide A. The loss of this small peptide is not sufficient to make the resulting fibrin molecule insoluble, but it tends to form complexes with adjacent fibrin and fibrinogen molecules. Thrombin then cleaves a second peptide, fibrinopeptide B, from fibrin and the fibrin monomers formed then polymerize spontaneously to form an insoluble gel. The polymerized fibrin is held together by noncovalent and electrostatic forces and stabilized by the transamidating enzyme, factor XIIIa, that is produced by the action of thrombin on factor XIII. The insoluble fibrin aggregates (clots) and aggregated platelets then block the damaged blood vessel and prevent further bleeding. The amount of fibrinogen in the plasma can serve as a nonspecific indicator of whether or not an inflammatory process is present in the body. Fibrinogen from any mammalian source will be cleaved by thrombin from any mammalian source.