Nucleoside triphosphate diphosphatase from germinated pea cotyledon chromatin
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概要
- 論文の詳細を見る
Nucleoside triphosphate diphosphatase purified from germinated pea cotyledon chromatin catalyzed the phosphohydrolysis of nucleoside triphosphate or diphosphate to nucleoside monophosphate and Pi. This enzyme differed from the cytoplasmic phosphatase in the cotyledon; it had no activity against the other phosphate esters. The enzyme was activated by Mg^<2+> and Mn^<2+>, and had a pH optimum of 7.0 and a Km of 9.6×10^<-6> _M for GTP, 1.2×10^<-5> _M for UTP, 2.7×10^<-5> _M for CTP and 1.7×10^<-4> _M for ATP. Pyrophosphate inhibited the activity with both nucleoside triphosphate and diphosphate as substrates. The degree of the inhibition by pyrophosphate to each nucleoside triphosphate as substrate was the reverse of the affinity of the substrate.
- 日本植物生理学会の論文
著者
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Takahashi Eiichi
Department Of Agricultural Chemistry. Kyoto University
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Matsumoto Hideaki
Institutefor Agricultural And Biological Science Okayama University
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Hirasawa Eiji
Department Of Biology. Faculty Of Science Osaka City University
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Hirasawa Eiji
Department Of Agricultural Chemistry Kyoto University
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Matsumoto Hideaki
Department Of Agricultural Chemistry Kyoto University
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Takahashi Eiichi
Department Of Agricultural Chemistry Kyoto University
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Matsumoto Hideaki
Department Of Agirucltural Chemistry Kyoto University
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Takahashi Eiichi
Department Of Agirucltural Chemistry Kyoto University
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