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Soluble Expression in Escherichia coli of Active Human Cyclic Nucleotide Phosphodiesterase Isoform 4B2 in Fusion with Maltose-Binding Protein
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- ZHU Sha
- Chongqing Key Laboratory of Biochemical and Molecular Pharmacology, Chongqing Medical University
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- YANG Genqing
- Chongqing Key Laboratory of Biochemical and Molecular Pharmacology, Chongqing Medical University Laboratory Medicine Department, Third Affiliated Hospital of Xinxiang Medical College
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- YANG Xiaolan
- Chongqing Key Laboratory of Biochemical and Molecular Pharmacology, Chongqing Medical University
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- ZHAO Yunsheng
- Chongqing Key Laboratory of Biochemical and Molecular Pharmacology, Chongqing Medical University
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- LI Xiang
- Chongqing Key Laboratory of Biochemical and Molecular Pharmacology, Chongqing Medical University
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- DENG Ping
- Chongqing Key Laboratory of Biochemical and Molecular Pharmacology, Chongqing Medical University
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- XIE Yanling
- Chongqing Key Laboratory of Biochemical and Molecular Pharmacology, Chongqing Medical University
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- GAN Zhiyong
- Chongqing Key Laboratory of Biochemical and Molecular Pharmacology, Chongqing Medical University
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- LIU Yin
- Chongqing Key Laboratory of Biochemical and Molecular Pharmacology, Chongqing Medical University
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- LI Zhirong
- Chongqing Key Laboratory of Biochemical and Molecular Pharmacology, Chongqing Medical University
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- LIAO Juan
- Chongqing Key Laboratory of Biochemical and Molecular Pharmacology, Chongqing Medical University
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- YU Ming’an
- Chongqing Key Laboratory of Biochemical and Molecular Pharmacology, Chongqing Medical University
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- LIAO Fei
- Chongqing Key Laboratory of Biochemical and Molecular Pharmacology, Chongqing Medical University
Bibliographic Information
- Other Title
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- Soluble Expression in<i>Escherichia coli</i>of Active Human Cyclic Nucleotide Phosphodiesterase Isoform 4B2 in Fusion with Maltose-Binding Protein
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Description
Recombinant expression in Escherichia coli of human cyclic nucleotide phosphodiesterase 4B2 (hPDE4B2) fused to maltose-binding-protein (MBP-hPDE4B2) was investigated. hPDE4B2 DNA amplified via nested RT-PCR with total RNAs from U937 cells was ligated with pMAL-p2x. After induction at 18 °C for 16 h, soluble MBP-hPDE4B2 was produced in E. coli. MBP-hPDE4B2 after amylose-resin chromatography showed 35% homogeneity, and its Michaelis-Menten constant was 10±2 μM (n=3). Rolipram had a dissociation constant of 9±2 nM (n=2), and zinc ion was a potent inhibitor. Hence, MBP-hPDE4B2 was expressed in E. coli as a soluble active protein.
Journal
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 73 (4), 968-970, 2009
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
- 1390001206480259712
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- NII Article ID
- 10027540265
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- NII Book ID
- AA10824164
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- ISSN
- 13476947
- 09168451
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- NDL BIB ID
- 10213335
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL Search
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed