Purification, characterization, and molecular cloning of a thermostable superoxide dismutase from Thermoascus aurantiacus |
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Authors: | E Shijin Guo Fangxian Liu Shouan Chen Jing Wang Yanjun Li Duochuan |
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Institution: | Department of Environmental Biology, Shandong Agricultural University, Taian, Shandong, China. |
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Abstract: | 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. |
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