書誌事項
- タイトル別名
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- Bioorganic Chemistry of Nyctinasty Using Functional Probes
- キノウセイ ブンシ プローブ オ モチイタ ショクブツ シュウミン ウンドウ ノ セイブツ ユウキ カガク ヒョウテキ サイボウ ト ジュヨウタイ タンパクシツ ソシテ カギ コウソ
- 標的細胞と受容体タンパク質, そして鍵酵素
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Circadian rhythmic plant leaf-movement, called nyctinasty, is controlled by a time-course change in the internal concentration of the leaf movement factors (leaf-opening and leaf-closing substances) in the plant body. We revealed that the target cell for the leaf-movement factors is plant motor cell by using novel synthetic fluorescence labeled probes. Using photoaffinity probes 21, the specific binding proteins for potassium lespedezate 1, the leaf-opening substance of Cassia mimosoides L, are detected from the plasma membrane fraction of the plant motor cell. Our study is a rare successful result of the detection of membrane receptors by using a synthetic photoaffinity probe designed on a biologicallly active natural product. These results also advance a guideline for probe design towards successful photoaffinity labeling. The balance of concentration of the leaf movement factors is inversed during the day. The glycoside type leaf movement factor is hydrolyzed with β-glucosidase, the activity of which is regulated by the biological clock. The circadian rhythm observed in the leaf movement is introduced by activation of the β-glucosidase regulated by the biological clock. We synthesized the glyconoamidine gel 43 designed on potassium lespedezate, a glycoside type leaf-opening substance, and succeeded in purification of the β-glucosidase, a key enzyme of circadian rhythmic plant leaf-movement, by affinity chromatography using affinity gel 43.
収録刊行物
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- 有機合成化学協会誌
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有機合成化学協会誌 64 (2), 117-129, 2006
公益社団法人 有機合成化学協会
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詳細情報 詳細情報について
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- CRID
- 1390282680288924672
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- NII論文ID
- 10017252258
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- NII書誌ID
- AN0024521X
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- ISSN
- 18836526
- 00379980
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- NDL書誌ID
- 7831281
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- NDL
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- 使用不可