Purification of salmon thrombin and its potential as an alternative to mammalian thrombins in fibrin sealants

Stability, sterility, coagulation, and immunologic studies of salmon coagulation proteins with potential use for mammalian wound healing and cell engineering

“…Only antibodies in low titers to thrombin and fibrinogen preparation could be detected in vivo. In another study, we have shown that neither normal subjects nor patients with various autoimmune diseases had circulating antibodies against salmon proteins compared to autoantigenic targets [12,13].…”

“…Salmon fibrinogen and thrombin, purified as previously described [12,13] were used for in vitro polymerization and immunologic studies in rats and rabbits. Fibrinogen was dissolved in 50 mM Tris, 150 mM NaCl and thrombin was stored in a buffer containing 20 mM Tris, pH 7.5, 1 mM EGTA, 1.0 M NaCl.…”

“…Thrombin was filtered through a 50 nm polycarbonate filter (Whatman) to remove bacteria and viruses. Thrombin activity was tested by a chromogenic substrate assays as described [12].…”

“…Recent studies show that salmon-derived thrombin and fibrinogen are biologically equivalent to proteins used in existing FG [12][13][14] and can be used instead of bovine-derived materials. In several animal models including swine aortotomy [15], salmon FG performed either equal to or better than commercially available glues derived from mammalian proteins.…”

Sample displacement chromatography of Atlantic Salmon (Salmo salar) thrombin

“…Thrombin from human and bovine blood has been extensively studied and characterized, and is also used as a component in surgical binding agents in human medicine (Tisseelk; Immuno AG, Vienna, Austria) and in the meat industry (Fibrimexk; Harimex, Loenen, Netherland). Salmon thrombin has been suggested as alternative to mammalian thrombins for the use as binding agent in surgical 0165 applications [1,2]. We have recently presented a non-toxic purification method for Atlantic salmon (Salmo salar) thrombin for the potential use as a component in a fish meat-binding agent [3], by using affinity chromatography (Heparin Sepharose) and ion exchange chromatography (SP Sepharose).…”