Purification and characterization of δ-aminolevulinic acid dehydratase from Chlorella regularis
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概要
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δ-Aminolevulinic acid dehydratase (δ-aminolevulinic acid hydrolyase EC 4.2.1.24) which catalyzes the formation of porphobilinogen from two molecules of δ-aminolevulinic acid (ALA) was purified from Chlorella regularis 737-fold by acetone and ammonium sulfate fractionations, DEAE-cellulose column chromatography, and Sephadex G-200 gel filtration. The enzyme had an optimum pH of 8.5 in Tris-HCl buffer and required either Mg^<2+> or Mn^<2+> for its maximum activity. The Km values for Mg^<2+>, Mn^<2+> and ALA were 15 μ_M, 10 μ_M, and 0.5 m_M, respectively. The enzyme was not activated by thiol compounds, but was inhibited by p-chloromercuribenzoate. The molecular weight estimated by gel filtration was 316,000 and the isoelectric point was 5.25.
- 日本植物生理学会の論文
著者
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Shioi Yuzo
Division Of Biology Miyazaki Medical College
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Tamai Hiroko
Division Of Biology Miyazaki Medical College
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Sasa Tsutomu
Division of Biology, Miyazaki Medical College
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Sasa Tsutomu
Division Of Biology Miyazaki Medical College
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