書誌事項
- タイトル別名
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- Purification and Properties of NAD-Dependent Malate Dehydrogenase from Mesembryanthemum crystallinum L. Exhibiting Crassulacean Acid Metabolism.
- Purification and Properties of NAD Depe
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抄録
By DEAE-cellulose anion exchange column chromatography, three different forms of NAD-dependent malate dehydrogenase (EC 1.1.1.37) (NAD-MDH) were isolated from leaves of Mesembryanthemum crystallinum L. in the crassulacean acid metabolism mode. NAD-MDH that eluted last from an anion exchange column was purified to a specific activity of 1, 096 units·(mg protein)-1 using Blue Sepharose CL-6B chromatography. Citrate and adenosine 5'-triphosphate effectively inhibited the activity of NAD-MDH. The inhibition of the enzymatic activity by citrate was reversed by inorganic phosphate and the degree of reversal increased with increasing the concentration of oxaloacetate, the substrate of the reaction. The optimal pH for NAD-MDH activity was around 7.5. Citrate inhibited the enzymatic activity over a wide range of pH and caused a shift in the optimal pH. The enzymatic activity in the presence of citrate was increased by adding inorganic phosphate below pH 7.5. On the basic side, higher than pH 7.5, however, the inhibition by citrate was enhanced by adding inorganic phosphate.
収録刊行物
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- 日本作物学会紀事
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日本作物学会紀事 64 (4), 760-766, 1995
日本作物学会
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詳細情報 詳細情報について
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- CRID
- 1390282679260193920
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- NII論文ID
- 110001734351
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- NII書誌ID
- AN00189888
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- ISSN
- 13490990
- 00111848
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- NDL書誌ID
- 3912003
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可