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Thrombin from Atlantic salmon (Salmo salar) was purified and characterized as a potential new binding agent for the food industry. Purification was performed avoiding inhibitors, using BaSO 4 adsorption and heparin-Sepharose affinity chromatography. Prothrombin activation was performed using a mixture of eggs and gills from salmon. Optimized conditions for the adsorption, elution, and the activation step are presented. The purified thrombin clotted bovine fibrinogen with a specific activity of 1423 U/mg. Sequence data are presented and compared with other species. This method of nontoxic activation and purification will allow salmon thrombin to be used in the food industry.

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