STREPTOKINASE is a bacterial protein, produced by several species of streptococci, that dissolves the human blood clots. It is a potent activator of plasminogen, the inactive precursor of plasmin.
STREPTOKINASE is a bacterial protein, produced by several species of streptococci, that dissolves the human blood clots. It is a potent activator of plasminogen, the inactive precursor of plasmin.
The introduction of streptokinase into medical practice, marked significant decline in death rates from acute heart attack. During large-scale field trials: ISIS-3 (1992) SK has proven to be as efficacious in myocardial infarction as its more expensive counterparts e.g., tPA (Lancet, 1992). Owing to its lower price compared to the expensive tPA, for a large majority of patients especially in the developing countries, affordable clot-buster therapy with streptokinase still remained elusive. Thus, emerged a dire need to develop a process to produce this protein more efficiently through a recombinant expression host making it even more affordable.
Biosimilar Recombinant Streptokinase (rSK) was developed from in-vitro to animal and to clinical studies in patients with AMI. This rSK product expressed by a non-streptococcal bacterial organism has a dramatic effect on major disadvantageous features of the earlier version of SK, namely the induction of an antigenic response and of acute nonspecific febrile and hypotensive side effects. rSK also result further reduction in infusion associated side effects by eliminating materials with pyrogenic and/or hypotensive effects from preparations.