Purification and Characterization of Maleate Hydratase from Arthrobacter sp. strain MCI2612
スポンサーリンク
概要
- 論文の詳細を見る
Maleate hydratase, which hydrates maleate to form D-malate, was purified from a crude extract of Arthrobacter sp. strain MCI2612 by DEAE-Toyopearl, Octyl-Sepharose CL-4B, and Ether-5PW column chromatographies. The enzyme was activated by sulfhydryl compounds and ferrous ion. The overall purification was 44.3-fold with a yield of 3.4%. The molecular weight of the enzyme was 90,000 by TSK G3000 SW column chromatography. The maleate hydratase appeared as two bands corresponding to molecular weights of about 58,000 and 28,000 on SDS-polyacrylamide gel electrophoresis. The enzyme had maximum activity at pH 8.5 and 45℃, and was inactivated by chemical agents such as hydroxylamine, p-chloromercuribenzoate, o-phenanthroline, and 2, 2'-dipyridyl. The K_m for maleate was 3.85mM.
- 社団法人日本農芸化学会の論文
- 1993-09-23
著者
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Asano Yasuhisa
Biotechnology Research Center, Toyama Prefectural University
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Asano Yasuhisa
Biotechnology Research Center Faculty Of Engineering Toyama Prefectural University
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Ueda M
Ochanomizu Univ. Tokyo Jpn
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Ueda Makoto
Mitsubishi Kasei Corporation, Research Center
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Yamada Hideaki
Faculty of Engineering, Kansai University
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Asano Yasuhisa
Biotechnology Res. Center And Dep. Of Biotechnology Toyama Prefectural Univ.
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Ueda Makoto
Mitsubishi Chemical Co. Research And Development Division Yokohama Research Center
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Yamada Hideaki
Faculty Of Engineering Kansai University
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Yamada Hideaki
Faculty Of Agriculture Kyoto University
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