D-Gluconate Dehydrogenase, 2-Keto-D-gluconate Yielding, from Gluconobacter dioxyacetonicus: Purification and Characterizationc
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概要
- 論文の詳細を見る
D-Gluconate dehydrogenase catalyzing the oxidation ofD-gluconate to 2-keto-D-gluconate was solubilized with Triton X-100 from the membrane of Gluconobacter dioxyacetonicus IFO 3271 and purified to an almost homogeneousstate by chromatographies on DEAE-cellulose and CMToyopearl in the presence of 0.1% Triton X-100. The enzyme had three subunits with molecular weights of 64, 000, 45, 000 and 21, 000, and contained approximately 2mol of heme per mol of the enzyme. The prosthetic group of the dehydrogenase was found to be a flavin covalently bound to the enzyme protein. The substrate specificity of the purified enzyme was very strict for D-gluconate and the apparent Michaelis constant for D-gluconate was 2.2mM.The optimum pH and temperature of the purified enzyme were 6.0 and 40°C, respectively.
- 社団法人 日本農芸化学会の論文
著者
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Adachi Osao
Department Of Agricultural Chemistry Yamaguchi University
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Shinagawa Emiko
Department of Agricultural Chemistry, Faculty of Agriculture, Yamaguchi University
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Matsushita Kazunobu
Department of Agricultural Chemistry, Faculty of Agriculture, Yamaguchi University
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Ameyama Minoru
Department of Agricultural Chemistry, Faculty of Agriculture, Yamaguchi University
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MATSUSHITA Kazunobu
Departmentof Agricultural Chemistry, Faculty of Agriculture, Yamaguchi University
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SHINAGAWA Emiko
Departmentof Agricultural Chemistry, Faculty of Agriculture, Yamaguchi University
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