Crystallization and Characterization of Agmatine Oxidase from Penicillium chrysogenum
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概要
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Agmatine oxidase was purified and crystallized with an overall yield of about 30% from a mycelial extract of Penicillium chrysogenum by a procedure involving ammonium sulfate fractionation, and DEAE-cellulose, hydroxyapatite, 1, 8-diaminooctane-Sepharose 4B and Sephadex G-200 column chrcmatographies. The purified enzyme was homogeneous on disc gel electrophoresis and the pink crystals appeared as a hexagonal board on addition of solid ammonium sulfate. The molecular weight of the native monomer form was determined to be 160, 000 by gel filtration, and it was composed of two identical subunits. The prosthetic group was identified as copper and its content was determined to be 2 mol per mol of the enzyme. The enzyme was inhibited by hydroxylamine, hydrazine, phenylhydrazine, semicarbazide, KCN, PCMB, Ag+, Hg2+ and Cu2+. The apparent Km values for agmatine, histamine and putrescine were calculated to be 2.51 × 10-4M, 4.25 × 10-4M and 1.64 × 10-2M, respectively.
- 社団法人 日本農芸化学会の論文
著者
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Tani Yoshiki
Department Of Agricultural Chemistry College Of Agriculture Kyoto University
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Yamada Hideaki
Department Of Agricultural Chemistry Faculty Of Agriculture Kyoto University
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ISOBE Kimiyasu
Amano Parmaceutical Co.
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