Purification and Characterization of Methylglyoxal Reductase from Hansenula mrakii
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概要
- 論文の詳細を見る
Methylglyoxal reductase was purified from Hansenula mrakii IFO 0895 to a homogenous state on fpolyacrylamide gel electrophoresis. The enzyme consisted of a single polypeptide chain with a molecular weight of 34,000. THe enzyme was specific to methylglyoxal(K_m=1.92mM)and NADPH(K_m=40.8μM). The activity of the enzyme was inhibited by p-chloromercuribenzoate and HgCl_2. NADP also inhibited the activity of the enzyme, and the K_i value was calculated to be 0.25mM.
- 社団法人日本生物工学会の論文
- 1991-02-25
著者
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Inoue Y
Research Institute For Food Science Kyoto University
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Inoue Yoshiharu
Research Institute For Food S-cience Kyoto University
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MURATA KOUSAKU
Research Institute for Food Science, Kyoto University
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KIMURA AKIRA
Research Institute for Food Science, Kyoto University
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Kimura A
Kyoto Univ. Kyoto
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Kimura Akira
Research Institute For Food Science Kyoto University
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Kimura A
Hokkaido Univ. Sapporo Jpn
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Inoue Y
Kyoto Univ. Kyoto
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Murata Kousaku
Research Institute For Food Science Kyoto Univeristy
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Kimura A
Research Institute For Food Science Kyoto University
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TRAN LINH-THUOC
Research Institute for Food Science, Kyoto University
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YOSIKAWA KOJI
Research Institute for Food Science, Kyoto University
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YOSHIKAWA KOJI
Research Institute for Food Science, Kyoto University
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Tran Linh-thuoc
Research Institute For Food Science Kyoto University
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Yoshikawa Koji
Research Institute For Food Science Kyoto University
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Kimura Akira
Research Center for Solar Energy Chemistry, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8531, Japan
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