Purification and Cheracterization of Glyozalase I from Hansenula mrakii
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概要
- 論文の詳細を見る
Glyoxalase I was purified from Hansenula mrakii IFO 0895 which was resistant to 25mM methylglyoxal. The molecular weight of the purified enzyme was calculated to be 38,000 by both gel-filtration of Sephadex G-150 and SDS-PAGE. The enxyme was almost specific to methylglyoxal(K_m=0.91mM). The activity of the enzyme was not inhibited by metal ion chelators such as EDTA, which is a potent inhibitor for glyoxalase Is from other sources.
- 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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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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Yoshikawa Koji
Research Center For Nanodevice And Systems Hiroshima 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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