Purification and Characterization of Cu, Zn Superoxide Dismutase from Ark Shell Scapharca broughtonii
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概要
- 論文の詳細を見る
A superoxide dismutase has been purified to apparent homogeneity from the muscular tissue of the ark shell, Scaqharca broughtonii, by ammonium sulfate fractionation, and consecutive column chromatographies using DEAE-Sephadex and Sephadex G-100. This enzyme has a molecular weight of 71,700 and is composed of two identical subunits of M_r 35,800,which are joined by noncovalent interactions. The purified enzyme was stable over the range of pH 5.0-10.0 at 4℃ for 24 h and at temperatures below 45℃. Cyanide at 0.1 and 1 mM inhibited the activity of the superoxide dismutase 56 and 100%, but 5 mM azide caused 8% inhibition. The optical spectrum of this enzyme had a maximum at 265 nm, and the amino acid composition of the enzyme was similar to that of the other Cu, Zn superoxide dismutases except for the contents of threonine, serine, proline, and leucine. Atomic absorption spectroscopy showed that this enzyme has approximately 2 atoms of Cu^<2+> and Zn^<2+> per mole of enzyme. These results indicate that the purified enzyme from ark shell, Scapharca broughtonii, is a Cu, Zn superoxide dismutase.
- 社団法人日本農芸化学会の論文
- 1998-11-23
著者
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Kim S‐k
Pukyong National Univ. Pusan Kor
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KIM Yong-Tae
Department of Chemistry, Faculty of Science and Engineering, Aoyama Gakuin University
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Kim Y‐t
Department Of Chemistry Faculty Of Science And Engineering Aoyama Gakuin University
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KIM Se-Kwon
Department of Chemistry, Pukyong National University
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Kim Y‐t
Department Of Chemistry College Of Science & Engineering Aoyama Gakuin University
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PARK Sun-Joo
Department of Chemistry, Pukyong National University
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Park Sun-joo
Department Of Chemistry Pukyong National University
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Kim Yong-tae
Department Of Chemistry Faculty Of Science And Engineering Aoyama Gakuin University
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Kim Se-kwon
Department Of Chemistry Pukyong National University
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Kim Yong-tae
Department Of Chemistry College Of Science & Engineering Aoyama Gakuin University
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Kim Se-Kwon
Department of Biological Engineering, Inha University
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Kim Yong-Tae
Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo
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