Purification and Properties of α-Hydroxyglutarate Dehydrogenase of Peptococcus aerogenes
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概要
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α-Hydroxyglutarate dehydrogenase (NAD+ specific) of Peptococcus aerogenes was purified by manganese chloride treatment, ammoniumsulfate fractionation and chromatographies with DEAE-cellulose, hydroxyapatite and Sephadex G-200, and then crystallized in a colorless thin plate form by the addition of ammoniumsulfate. The enzyme has a molecular weight of approximately 53, 000 and consists of two subunits identical in molecular weight (about 32, 000). The isoelectric point of the enzyme is pH 3.7±0.1. The enzyme acts almost exclusively on α-ketoglutarate and ahydroxyglutarate. The Michaelis constants for α-ketoglutarate, NADH, α-hydroxyglutarate and NAD+ are 0.12, 0.028, 0.67 and 0.077mM, respectively.
- 社団法人 日本農芸化学会の論文
著者
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Esaki Nobuyoshi
Laboratory Of Microbial Biochemistry Institute For Chemical Research Kyoto University
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Esaki N
Kyoto Univ. Kyoto Jpn
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SODA Kenji
Laboratory of Microbiology, Institute for Chemical Research, Kyoto University
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OTAWARA Shigeki
Laboratory of Microbial Biochemistry, Institute for Chemical Research, Kyoto University
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OHSHIMA Toshihisa
Laboratory of Microbial Biochemistry, Institute for Chemical Research, Kyoto University
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