دورية
Isolation, characterization, and cDNA cloning of a vampire bat salivary plasminogen activator*
| العنوان: | Isolation, characterization, and cDNA cloning of a vampire bat salivary plasminogen activator* |
|---|---|
| المؤلفون: | Gardell, S J, Duong, L T, Diehl, R E, York, J D, Hare, T R, Register, R B, Jacobs, J W, Dixon, R A, Friedman, P A |
| المصدر: | Journal of Biological Chemistry; October 1989, Vol. 264 Issue: 30 p17947-17952, 6p |
| مستخلص: | Vampire bat saliva contains a plasminogen activator that presumably assists these hematophagous animals during feeding. Here, we report that the vampire bat salivary plasminogen activator, Bat-PA, is homologous to tissue-type plasminogen activator (t-PA) but contains neither a kringle 2 domain nor a plasmin-sensitive processing site. Three Bat-PA species corresponding to full-length, finger−, and finger−epidermal growth factor homology domain−forms of t-PA have been isolated. Bat-PA(H), the full-length form, was purified and its activity has been characterized. Bat-PA(H) and t-PA are of similar efficacy when monitored for their abilities to catalyze plasminogen activation in the presence of a fibrin cofactor. Interestingly, Bat-PA activity toward plasminogen is stimulated 45,000-fold in the presence of fibrin I; the corresponding value for t-PA is only 205-fold. Bat-PA(H) is the only Bat-PA species which binds tightly to fibrin, although each of the three species exhibit remarkable stimulation by a fibrin cofactor. |
| قاعدة البيانات: | Supplemental Index |
| تدمد: | 00219258 1083351X |
|---|---|
| DOI: | 10.1016/S0021-9258(19)84664-1 |