Purification and characterization of methylglyoxal reductase from Hansenula mrakii
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説明
Abstract Methylglyoxal reductase was purified from Hansenula mrakii IFO 0895 to a homogenous state on polyacrylamide 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 = 1.92 mM) and NADPH ( K m = 40.8 μ M). 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 0.25 mM.
収録刊行物
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- Journal of Fermentation and Bioengineering
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Journal of Fermentation and Bioengineering 71 (2), 134-136, 1991-01
Elsevier BV
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詳細情報 詳細情報について
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- CRID
- 1360847868816306816
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- NII論文ID
- 110002691545
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- NII書誌ID
- AA10702688
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- ISSN
- 0922338X
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- データソース種別
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- Crossref
- CiNii Articles
- OpenAIRE
