Recombinant batroxobin expressed highly in Pichia pastoris / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 483-486, 2007.
Article
in Chinese
| WPRIM
| ID: wpr-328000
ABSTRACT
Methylotrophic yeast, Pichia pastoris was used to express recombinant batroxobin, and a technology route of producing recombinant protein was finally established. We synthesized batroxobin gene artificially by means of recursive PCR. pPIC9-batroxobin was constructed and transformed into Pichia pastoris GS115 (his4). Recombinant batroxobin was expressed in yeast engineering strain and it was purified from the culture supernatant. 10 mg of recombinant batroxobin was purified from 1 liter fermentation media, it exhibited specific activity of 238 NIH units/mg and had molecular weight of 30.55 kD. The purified recombinant protein converted fibrinogen into fibrin clot in vitro, and shortened bleeding time in vivo. This study laid a foundation of development of hemostatic of recombinant snake venom thrombin-like enzyme.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Pharmacology
/
Pichia
/
Time Factors
/
Recombinant Proteins
/
Batroxobin
/
Gene Expression
/
Polymerase Chain Reaction
/
Electrophoresis, Polyacrylamide Gel
/
Genetics
/
Hemorrhage
Limits:
Animals
Language:
Chinese
Journal:
Chinese Journal of Biotechnology
Year:
2007
Type:
Article
Similar
MEDLINE
...
LILACS
LIS