Efficient expression of soluble human FGF-21 and its glucose regulation activity / 药学学报
Acta Pharmaceutica Sinica
; (12): 548-552, 2009.
Article
in Zh
| WPRIM
| ID: wpr-278223
Responsible library:
WPRO
ABSTRACT
The cDNA of human FGF-21 was subcloned into the pSUMO expression vector and the fusion protein was induced to express in Escherichia coli Rosetta (DE3). The recombinant hFGF-21 was expressed in soluble form in the pSUMO expression system. The recombinant fusion protein was purified by Ni-NTA column. The purified recombinant protein was dialyzed against PBS for re-nature. To obtain pure and active recombinant protein, the fusion protein was subjected to cleavage with SUMO protease I. To examine glucose regulation activity of hFGF-21, 3T3-L1 pre-adipocytes were differentiated into adipocytes, glucose up-take activity of hFGF-21 was examined by glucose oxidase and peroxidase (GOD-POD) assay. Compared with no stimulation control, the recombinant hFGF-21 treatment led to a significant increase in glucose consumption of adipocytes and a significant decrease in concentration of glucose in the medium (P < 0.05, P < 0.001).
Full text:
1
Database:
WPRIM
Main subject:
Pharmacology
/
Plasmids
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Solubility
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Recombinant Fusion Proteins
/
DNA, Complementary
/
Adipocytes
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Small Ubiquitin-Related Modifier Proteins
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3T3-L1 Cells
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Escherichia coli
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Fibroblast Growth Factors
Limits:
Animals
/
Humans
Language:
Zh
Journal:
Acta Pharmaceutica Sinica
Year:
2009
Document type:
Article