| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2021959 | Protein Expression and Purification | 2007 | 7 Pages |
Abstract
A system for the expression of recombinant lumbrokinase (rPI239) was developed in the yeast Pichia pastoris. A total supernatant protein content of 0.174 g/L of high density fermentation broth was obtained. The rPI239 exhibited in vitro fibrinolytic activity. The in vivo activity of rPI239 was measured by prothrombin time, kaolin part thrombin time, thrombin time, and fibrinolytic activity. This work presents the high-density fermentation of rPI239 from P. pastoris and shows that the recombinant protein has similar fibrinolytic activity both in vivo and in vitro.
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Authors
Tao Ge, Shi-Hong Fu, Li-Hong Xu, Qing Tang, Huan-Yu Wang, Kun-Ping Guan, Guo-Dong Liang,