USE OF A RECOMBINANT INHIBITOR FROM ERYTHRINA CAFFRA FOR PURIFYING SERINE PROTEASES

摘要

In a process for purifying serine proteases from a protein mixture the serine protease is bonded to an immobilized polypeptide having the activity of a DE-3 inhibitor from Erythrina caffra, the unbonded portions are removed from the protein mixture, the serine protease is separated from the inhibitor, the immobilized inhibitor is separated from the soluble serine protease, and the serine protease is isolated. The process is characterized in that a polypeptide which is the product of a prokaryotic or eukaryotic expression of an exogenic nucleic acid is used as the polypeptide. This inhibitor is noted for its improved specific activity and is suitable in particular for purifying plasminogen activators, such as tissue plasminogen activators (t-PA and derivatives).