HIGH-LEVEL EXPRESSION OF STREPTOKINASE IN ESCHERICHIA-COLI

Streptokinase (SK), which activates human plasminogen by promoting its conversion to plasmin, is normally obtained from beta-hemolytic streptococci. Treatment with SK is an effective therapy for improving survival and preserving left ventricular function after coronary thrombosis. We report the cloning, expression in E. coli to levels of 25% of the total cell protein, and characterization of a novel SK (SKC-2) gene, the product of which is functionally equivalent to the naturally-derived protein. The availability of a recombinant streptokinase (rSK) in high yield and purity offers a potentially attractive alternative source of this important therapeutic agent.