Mg^<++>-activated and -inhibited ATPases from mung bean hypocotyls
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概要
- 論文の詳細を見る
Mg^<++>-activated and -inhibited ATPases were isolated from dark-grown mung bean hypocotyls. The enzymes hydrolyzed nucleoside tri-, di- and monophosphates and β-glycerophosphate. The effect of Mg^<++> was most marked when ATP and other nucleoside triphosphates were used as substrates. Mg^<++>-activated ATPases: The activity of enzyme-I was localized in the membranes and was not released by treatment with 0.1% deoxycholate. Enzyme-II was released and separated by CM-cellulose column chromatography. Enzyme-V was separated from the soluble fraction of the cell homogenate by DEAE-cellulose column chromato-graphy. The rates of activivation by Mg^<++> of enzyme-II and enzyme-V were very small compared to that of enzyme-I. Mg^<++>-inhibited ATPases: Enzyme-III and-IV were precipitated with 50-80% ammonium sulfate from the soluble fraction of the cell homogenate and were separated by successive column chromatographies on Sepharose 6B and DEAE-cellulose. The activities of enzyme-III and -IV were inhibited by Mg^<++> when ATP, UTP and GTP were used as substrates. Enzyme-III was purified approximately 38-fold, and was more remarkably inhibited by Mg^<++> than was enzyme-IV.
- 日本植物生理学会の論文
著者
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Kasamo Kunihiro
Department of Applied Physiology, National Institute of Agrobiological Resources
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Kasamo Kunihiro
Department Of Biology College Of General Education (kyoyo-gakubu) University Of Tokyo:(present)insti
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Yamaki Tashio
Department of Biology, College of General Education (Kyoyo-gakubu), University of Tokyo
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Yamaki Tashio
Department Of Biology College Of General Education (kyoyo-gakubu) University Of Tokyo
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