Staphylokinase

Literature References: Fibrin-specific plasminogen activator lacking enzymatic activity; produced by certain strains of Staphylococcus aureus. Consists of 136 amino acids in a single polypeptide chain without disulfide bridges; several molecular forms have been purified, mol wt 16,500-18,000. Forms a stoichiometric complex with the proenzyme plasminogen, q.v., that becomes biologically active after the conversion of plasminogen to the proteolytic enzyme plasmin, q.v. Profibrinolytic properties: C. H. Lack, Nature 161, 559 (1948); E. B. Gerheim, et al., Proc. Soc. Exp. Biol. Med. 68, 246 (1948). Cloning and expression in Escherichia coli: T. Sako et al., Mol. Gen. Genet. 190, 271 (1983); in Bacillus subtilis: D. Behnke, D. Gerlach, ibid. 210, 528 (1987). High yield production and purification of recombinant form: B. Schlott et al., Biotechnology 12, 185 (1994). Series of articles on isoln, characterization, structure, biochemistry and pharmacology of natural (STAN) and recombinant (STAR) forms: Fibrinolysis 6, 203-242 (1992). Determn in plasma by bioimmunoassay: H. R. Lijnen et al., Thromb. Haemostasis 70, 491 (1993); by ELISA: A. Mike et al., Biol. Pharm. Bull. 17, 564 (1994). Clinical evaluation in peripheral arterial occlusion: S. Vanderschueren et al., Circulation 92, 2050 (1995). Comparative clinical trial vs alteplase, q.v.: idem et al., ibid. 2044. Series of articles on recombinant variants with altered immunoreactivity: D. Collen et al., ibid. 94, 197-216 (1996); 95, 455-472 (1997). Reviews: D. Collen, H. R. Lijnen, Blood 84, 680-686 (1994); H. R. Lijnen, D. Collen, Fibrinolysis 10, 199-126 (1996).