National Taiwan Ocean University Institutional Repository:Item 987654321/27037
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題名: Biochemical Characterization of a Cambialistic Superoxide Dismutase Isozyme from Diatom Thallassiosira weissflogii: Cloning, Expression, and Enzyme Stability
作者: Jenq-Kuen Huang;Lisa Wen;Hsu Ma;Zong-Xian Huang;Chi-Tsai Lin
貢獻者: NTOU:Institute of Bioscience and Biotechnology
國立臺灣海洋大學:生物科技研究所
關鍵詞: Thallassiosira weissflogii;expression;cambialistic superoxide dismutase (Fe/Mn−SOD)
日期: 2005
上傳時間: 2011-10-21T02:22:24Z
出版者: Journal of Agricultural and Food Chemistry
摘要: Abstract:A cDNA clone of 1081 bp encoding a second putative superoxide dismutase (SOD) from diatom Thallassiosira weissflogii was cloned by the polymerase chain reaction technique. The cDNA encodes a protein of 286 amino acid residues. Alignment of the truncated SOD sequence containing 217 amino acid residues with Mn−SODs from Vibrio mimicus and Escherichia coli, as well as two Fe−SODs from E. coli and Photobacterium leiognathi, this SOD showed greater homology to Mn−SOD. The residues required to coordinate the manganese ion were conserved in all reported Mn−SOD. The recombinant SOD has a half life of deactivation of 14.7 min at 65 °C. Its thermal inactivation rate constant Kd was 3.21 × 10-2 min-1. The enzyme was stable in a broad pH range from 4 to 12. The presence of imidazole (up to 0.8 M) and sodium dodecylsulfate (up to 4%) had little effect on the enzyme's activity. The atomic absorption spectrometric assay showed the presence of 0.3 atom of iron/manganese (2:1) in each SOD subunit. Reconstituted activity suggested that diatom SOD was cambialistic Fe/Mn−SOD.
關聯: 53(16), pp.6319–6325
URI: http://ntour.ntou.edu.tw/handle/987654321/27037
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