Purification and Characterization of NADPH-dependent 2-Oxoaldehyde Reductase from Parsley(Food & Nutrition)
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概要
- 論文の詳細を見る
A NADPH-dependent 2-oxoaldehyde reductase, which catalyzes the reduction of 3-deoxyglucosone to 3-deoxyfructose and reduction of methylglyoxal to acetol, was isolated and purified from parsley leaves. 2-Oxoaldehyde compounds were found to be specially good substrates and monocarbonyl compounds were poor substrates for this reductase. The optimum pH of the enzyme activity was 7.0-7.5. The Km for 3-deoxyglucosone and methylglyoxal were 15mM and 13mM, respectively. The molecular weight of the enzyme was estimated to be 67,000 and the enzyme is proposed to be a dimer composed of identical subunits (MW = 35,000). The enzyme activity was completely inhibited by p-chloromercuribenzoate. The reaction catalyzed by the enzyme was virtually irreversible. The changes in methylglyoxal and NADPH by the enzyme were stoichiometrically equivalent.
- 社団法人日本農芸化学会の論文
- 1990-02-23
著者
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早瀬 文孝
明治大学農学部農芸化学科
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Kato H
Univ. Tokyo Tokyo Jpn
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Kato H
Department Of' Agricultural Chemistry The University Of Tokyo
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Kato Hiromichi
Department Of Agricultural Chemistry The University Of Tokyo
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Kato H
Otsuma Women's Univ. Tokyo Jpn
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Hayase Fumitaka
Department Of Agricultural Chemistry Faculty Of Agriculture Meiji University
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Hayase Fumitaka
Department Of Agricultural Chemistry The University Of Tokyo:(present Address) Department Of Agricul
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Nishimura Toshihide
Department Of' Agricultural Chemistry The University Of Tokyo
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Nishimura Toshihide
Department Of Agricultural Chemistry The University Of Tokyo
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Hayase F
Department Of Agricultural Chemistry Meiji University
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Liang Zhi-qun
Department Of Agricultural Chemistry The University Of Tokyo
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LIANG Zhi
Department of Agricultural Chemistry, The University of Tokyo
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