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- W2361049462 abstract "【Objective】The objective of this study is to investigate the expression characteristics of duck leptin in E.coli BL21 and the bioactivity of the expression product.【Method】The recombinant duck leptin gene prokaryotic expression strain was constructed. The recombinant strain was induced in different times and different concentrations of IPTG. After purification, renaturation and condensation, the product was injected into Kunming mice. The body weight, food intake and body fat content of mice were analyzed. 【Result】The fusion protein was specifically expressed. The results of SDS-PAGE analysis indicated that the molecular weight of the fusion protein was about 20 kD, which included the 16 kD protein expressed from duck leptin gene. The target protein was expressed with the induction of 0.2 mmol/L IPTG, which was about 57% of total protein in bacteria. The recombinant protein reduced body weight、food intake and body weight on the testing in Kunming mice.【Conclusion】Duck leptin was high-level expressed in E.coli BL21. The purified recombinant protein was proved to be biologically active." @default.
- W2361049462 created "2016-06-24" @default.
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- W2361049462 date "2007-01-01" @default.
- W2361049462 modified "2023-09-23" @default.
- W2361049462 title "Fusion Expression of Duck leptin Gene in Escherichia coli and Determination of Recombinant Protein Bioactivity" @default.
- W2361049462 hasPublicationYear "2007" @default.
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