Plasminogen activator naturally occurring in the saliva of the vampire bat, Desmodus rotundus. Four isoforms have been identified. All are single chain peptides that are structurally homologous to human tissue plasminogen activator, q.v. DSPA-α1 and -α2 are comprised of 477 amino acid residues containing 4 distinct domains; isoforms β and γ are smaller, truncated versions. DSPA-α1 and -α2 bind to fibrin; all isoforms require fibrin as a cofactor for plasminogen activation. Isoln: C. Hawkey, Nature 211, 434 (1966). Cloning, characterization and structure: S. J. Gardell et al., J. Biol. Chem. 264, 17947 (1989). Identification of isoforms: J. Kr"atzschmar et al., Gene 105, 229 (1991). Review of purification, properties and activity: S. J. Gardell, P. A. Friedman, Methods Enzymol. 223, 233-249 (1993). Study of structural mechanism of catalytic activity: M. Renatus et al., Biochemistry 36, 13483 (1997).
DSPA-α1 produced by recombinant technology; mol wt 55-58 kDa. Prepn: B. Baldus et al., WO 9009438; eidem, US 6008019 (1990, 1999 both to Schering AG); T. Petri et al., J. Biotechnol. 39, 75 (1995). CE/MS method for pharmaceutical formulations: J. A. Chakel et al., J. Chromatogr. B 689, 215 (1997). Pharmacology: W.-D. Schleuning, Haemostasis 31, 118 (2001). Clinical evaluation in acute ischemic stroke: W. Hacke et al., Stroke 36, 66 (2005). Review: T. Debens, Curr. Opin. Mol. Ther. 6, 567-575 (2004).
Thrombolytic.
Desmoteplase: Thrombolytic