Fibrinolysin, Human, Recombinant PL, Human, Recombinant Lyophilized. Lyophilized from aqueous acetic acid, pH 3.4. Recombinant, human plasmin expressed in yeast as plasminogen and activated by urokinase treatment. Plasmin is a two-chain serine protease that catalyzes the hydrolysis of peptide bonds at the carboxylic acid side of arginine and lysine. It also cleaves fibrin clots, thus playing an important role in producing fibrin degradation products (FDP). Specific activity: ≥ 20 units/mg protein. Activity is determined by measuring the rate of hydrolysis of the peptide substrate, N-Tosylglycyl-Lprolyl-L-lysine 4-nitroanilide. Purity: ≥95% by SDS-PAGE. Ref.: Federici, A.B., et al. 1993. Blood 81, 720. Hoffmann, J.J., and Janssen, W.C. 1992. Thromb. Res. 67, 711. |