Biosynthesis of alicyclic acids from ^<14>C-labeled glucose and erythrose by isolated cells from Vigna angularis leaves
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概要
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Mesophyll cells isolated enzymatically from Vigna angularis leaves were fed ^<14>C-glucose or ^<14>C-erythrose and the time-course of ^<14>C incorporation into shikimic and quinic acids was examined. When ^<14>C-glucose was fed to the cells, the highest radioactivity in quinic acid was observed after 10 hr of incubation, while that in shikimic acid was after 14 hr. In the experiment with ^<14>C-erythrose, the radioactivity in shikimic acid rose strikingly up to the 3rd hour, but ^<14>C in quinic acid increased gradually during the incubation. The incorporation of ^<14>C into shikimic acid was enhanced when unlabeled shikimic or quinic acid was supplied to the cells simultaneously with either ^<14>C-glucose or ^<14>C-erythrose, whereas that into quinic acid was not significantly increased by these alicyclic acids. The difference in incorporation rate of ^<14>C into quinic acid from that into shikimic acid was more conspicuous in the isolated mesophyll cells than in the epicotyls of V. angularis seedlings.
- 日本植物生理学会の論文
著者
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Tazaki Kiyoshi
Department Of Biology Faculty Of Science Kumamoto University
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Tazaki Kiyoshi
Department Of Biology Tokyo Metropolitan University(present)department Of Biology Faculty Of Science
関連論文
- Purification and Characterization of an Aminopeptidase, LPAase 2, from Euonymus Leaves
- Alicyclic acid metabolism in plants V. Biosynthesis of alicyclic acids from ^C-labeled glucose and erythrose in some plant tissues
- Biosynthesis of alicyclic acids from ^C-labeled glucose and erythrose by isolated cells from Vigna angularis leaves
- Purification and Characterization of an Aminopeptidase, the Enzyme-Hydrolyzing Alanine-p-nitroanilide (APAase), from Euonymus Leaves
- Multiple Forms of Aminopeptidase in Euonymus Leaves