Purification, Characterization, and Molecular Cloning of a Thermostable Superoxide Dismutase from Thermoascus aurantiacus
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概要
- 論文の詳細を見る
A thermostable superoxide dismutase [(SOD) EC 1.15.1.1] from a Thermoascus aurantiacus var. levisporus was purified to sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) homogeneity by a series of column chromatographies. The molecular mass of a single band of the enzyme was estimated to be 16.8 kDa by SDS–PAGE. The molecular mass was estimated to be 33.2 kDa by gel filtration on Sephacryl S-100, indicating that the enzyme was composed of two identical subunits of 16.8 kDa each. N-terminal amino acid sequencing (seven residues) yielded VKAVAVL. Using RACE-PCR, a Cu, Zn-SOD gene was cloned from T. aurantiacus var. levisporus. The sequence was 705 bp and contained a 468 bp ORF encoding a Cu, Zn-SOD of 155 amino acid residues.
- 社団法人 日本農芸化学会の論文
- 2007-04-23
著者
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Chen Jing
Department Of Environmental Biology Shandong Agricultural University
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Wang Yanjun
Department Of Environmental Biology Shandong Agricultural University
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Chen Jing
Department Of Biological Sciences And Biotechnology Tsinghua Universty And State Key Laboratory Of B
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E Shijin
Department of Environmental Biology, Shandong Agricultural University
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GUO Fangxian
Department of Environmental Biology, Shandong Agricultural University
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LIU Shouan
Department of Environmental Biology, Shandong Agricultural University
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LI Duochuan
Department of Environmental Biology, Shandong Agricultural University
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E Shijin
Department Of Environmental Biology Shandong Agricultural University
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Guo Fangxian
Department Of Environmental Biology Shandong Agricultural University
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Li Duochuan
Department Of Environmental Biology Shandong Agricultural University
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Liu Shouan
Department Of Environmental Biology Shandong Agricultural University
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Guo Fangxiam
Department of Environmental Biology, Shandong Agricultural University
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