Plasmin

Product description:Plasmin:Plasmin is a serine endopeptidase of the peptidase S1 family. Plasmin is converted to plasminogen by cleavage between Arg561 and Val562. The resulting activated plasmin consists of two disulfide-linked polypeptide chains. The plasmin heavy chain (MW 60 kDa) is derived from the amino terminal region of plasminogen. The light chain originates from the carboxyl-terminus of plasminogen. In vivo, the MW of the heavy chain can vary from 63KDa to 12KDa depending on the extent of proteolysis to the plasminogen from which it is derived. Plasmin is activated by a variety of proteases including urokinase, tissue plasminogen activator, and streptokinase. During the activation of plasminogen, an autolytic peptide of molecular weight 8,200 is released from the Glu-amino terminus to yield a Lys-amino terminus on the heavy chain. The active site of plasmin is on the light chain.
Specificity and Kinetics :
Plasmin exhibits preferential cleavage at the carboxyl side of Lysine and Arginine residues with higher selectivity than trypsin.5 It converts polymerized fibrin into soluble products.
pH Optimum: 8.5 
pH 7.5: about 40% of maximal activity, pH 9.5: about 50% of maximal activity6
Temperature Optimum: 37 °C with rapid inactivation at 56 °C6