High density fermentation and activity of a recombinant lumbrokinase (PI239) from Pichia pastoris.
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.
Ge
Tao
T
Institute for Virus Disease Control and Provetion, No.100 YingXin Jie, XuanWu Qu, Beijing 100052, China.
Fu
Shi-Hong
SH
Xu
Li-Hong
LH
Tang
Qing
Q
Wang
Huan-Yu
HY
Guan
Kun-Ping
KP
Liang
Guo-Dong
GD
D017931:DNA Primers; D010450:Endopeptidases / Q000378:metabolism*; D005285:Fermentation; D005342:Fibrinolysis; D005656:Fungal Proteins / Q000378:metabolism*; D005818:Genetic Engineering; D007700:Kinetics; D008970:Molecular Weight; D010843:Pichia / Q000201:enzymology* / Q000235:genetics; D010957:Plasmids; D011517:Prothrombin Time; D011994:Recombinant Proteins / Q000378:metabolism
D017931:DNA Primers; D005656:Fungal Proteins; D011994:Recombinant Proteins; D010450:Endopeptidases; C083421:lumbrokinase