Expression of Recombinant Human Interferon-.GAMMA. with Antiviral Activity in the Bi-Cistronic Baculovirus-Insect/Larval System
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- CHEN Wen-Shuo
- Institute of Molecular Medicine, National Tsing Hua University
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- VILLAFLORES Oliver B.
- Department of Chemistry, Chung Yuan Christian University
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- JINN Tzyy-Rong
- Graduate Institute of Chinese Medical Science, China Medical University
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- CHAN Ming-Tsair
- Institute of BioAgricultural Sciences, Academia Sinica
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- CHANG Yen-Chung
- Institute of Molecular Medicine, National Tsing Hua University
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- WU Tzong-Yuan
- Department of Bioscience Technology, Chung Yuan Christian University R&D Center for Membrane Technology, Chung Yuan Christian University
Bibliographic Information
- Other Title
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- Expression of recombinant human interferon-γ with antiviral activity in the Bi-cistronic baculovirus-insect/larval system
- Expression of recombinant human interferon g with antiviral activity in the Bi cistronic baculovirus insect larval system
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Abstract
A bi-cistronic baculovirus-insect/larval system containing a polyhedron promoter, an internal ribosome entry site (IRES), and an egfp gene was developed as a cost-effective platform for the production of recombinant human interferon gamma (rhIFN-γ). There was no significant difference between the amounts of rhIFN-γ produced in the baculovirus-infected Spodoptera frugiferda 21 cells grown in serum-free medium and the serum-supplemented medium, while the Trichoplusia ni (T. ni) and Spodoptera exigua (S. exigua) larvae afforded rhIFN-γ amounting to 1.08±0.04 and 9.74±0.35 μg/mg protein respectively. The presence of non-glycosylated and glycosylated rhIFN-γ was confirmed by immunoblot and lectin blot. The immunological activity of purified rhIFN-γ, with 96% purity by Nickel (II)-nitrilotriacetic acid (Ni-NTA) affinity chromatography, was similar to that commercially available. Moreover, the rhIFN-γ protein from T. ni had more potent antiviral activity. These findings suggest that this IRES-based expression system is a simple and inexpensive alternative for large-scale protein production in anti-viral research.
Journal
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 75 (7), 1342-1348, 2011
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Keywords
Details 詳細情報について
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- CRID
- 1390001206476927360
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- NII Article ID
- 10029329338
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- NII Book ID
- AA10824164
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- ISSN
- 13476947
- 09168451
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- NDL BIB ID
- 11175106
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- PubMed
- 21737931
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- Abstract License Flag
- Disallowed