Estreptokinase, plasminokinase is a purified bacterial protein produced from the strains of group C β-haemolytic S. griseus.
STREPTOKINASE
Synonym
Estreptokinase, plasminokinase.
Biological Source
Estreptokinase, plasminokinase is a purified bacterial
protein produced from the strains of group C β-haemolytic S. griseus.
Preparation
Streptokinase is a bacterial derived enzyme of serine
pro-tease group. The ancestral protease activity lies within the first 230
amino-acid residues at the N-terminal part of the protein that evolves from
serine protease due to the replacement of histamine at 57th amino acid by
glycine. The amino terminal residue polypeptide chain shows sequence homology
to serine protease. Duplication and fusion of gene generate an ancestral
streptokinase gene. Streptokinase is produced by fermentation using
streptococcal culture and is isolated from the culture filtrate. It is produced
in the form of a lyophilized powder in sterile vials containing 2,50,000 to
7,50,000 IUs.
Characteristics
Streptokinase is a bacterial protein with half-life of 23
minutes. Its anisolylated plasminogen activator complex (APSAC) has a higher
half-life of six hours.
Chemical Constituents
Streptokinase is the purified bacterial protein with about
484 amino-acid residues.
Uses
Streptokinase is the first available agent for dissolving
blood clots. It binds to plasminogen in a 1:1 ratio and changes molecular
conformation. Thus, the complex formed becomes an active enzyme and promotes
the activity of fibrinolytic enzyme plasmin. Plasmin breaks fibrin clots.
Anistreptase or the anisolylated plasminogen streptokinase activator complex
(APSAC) can also be used in a similar way for degrading blood clots.
Streptokinase and anistreptase are both used in the treatment of pulmonary
embolism, venous, and arterial thrombosis and coronary artery thrombosis. It is
also sometimes administered along with heparin to counter act a paradoxical
increase in local thrombin.
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