Purification, Crystallization and Properties of Hydantoinase from Pseudomonas striata : Microbial Transformation of Hydantoins to Amino Acids(II)
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概要
- 論文の詳細を見る
A hydantoin hydrolyzing enzyme was purified and crystallized from cells of Pseudomonas striata, by a procedure including protamine sulfate treatment, ammonium sulfate fractionation, DEAE-cellulosse and hydroxylapatite chromatographies, and Sephadex G-200 gel filtration. THe enzyme was homogeneous by the criteria of ultracentrifugation and acrylamide gel electrophoresis. The molecular weight was determinated to be approximately 190,000 by the Sephadex G-200 gel filtration method. Though the enzyme hydrolyzed various aliphatic and aromatic 5-monosubstituted hydantoins, it showed the highest activity and affinity toward dihydrouracil, suggesting its identity with dihydropyrimidinase. The enzyme was strongly inhibited by metal chelating agents and by p-chloromercuribenzoate. It acts on D-isomers of 5-monosubstituted hydantoins to form N-carbamyl-D-amino acids.
- 社団法人日本生物工学会の論文
- 1978-10-25
著者
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YAMADA Hideaki
Department of Agricultural Chemistry, Kyoto University
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KUMAGAI HIDEHIKO
Department of Food Science and Technology, Kyoto University
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Kumagai Hidehiko
Department Of Food Science And Technology Faculty Of Agriculture Kyoto University
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TAKAHASHI SATOMI
Biochemical Research Laboratory, Kanegafuchi Chemical Industry Co., Ltd.,
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KII YOSHIAKI
Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University
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Kii Yoshiaki
Department Of Agricultural Chemistry Faculty Of Agriculture Kyoto University
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Takahashi Satomi
Biochemical Research Laboratory Kanegafuchi Chemical Industry Co. Ltd.
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Yamada Hideaki
Department Of Agricultural Chemistry Faculty Of Agriculture Kyoto University
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KUMAGAI Hidehiko
Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University
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