Properties of the Vanadate-Sensitive ATPase of the Plasma Membrane Vesicles from Rice Roots
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概要
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The plasma membrane vesicles were purified by aqueous two phase partitioning from rice roots (Oryza sativa L. cv. Nipponbare). The ATPase activity of the purified plasma membrane fraction (U_3 fraction) increased more than 4-fold by the addition of Triton X-100, and was not inhibited by trypsin digestion pretreatment. Vanadate inhibited 70% of the ATPase activity of the Triton-washed U_3 fraction. The K_m value was 1.45 mM, and vanadate and ADP inhibited the activity uncompetitively and competitively, respectively. The ATPase activity was dependent on Mg^<2+>, and Co^<2+> could be completely substituted for Mg^<2+>, while Fe^<2+> and Mn^<2+> partially. KCl increased the activity by 20% with saturation at 5 mM. The order of the stimulation by monovalent cations was NH_4^+>K^+>Li^+, choline ^+>Na^+. the optimum pH for the activity was 6. The vesicles of the U_3 fraction were reconstituted with deoxycholate and soybean phospholipids. the proton pumping activity of the fraction was inhibited by vanadate. Based on the results obtained, it was concluded that vanadate-sensitive ATPase, which is presented on the plasma membrane of rice roots acts as a proton pump.
- 社団法人日本土壌肥料学会の論文
著者
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WAKIUCHI Nariaki
Department of Agricultural Chemistry, Faculty of Agriculture, Kobe University
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HARADA Hisatomi
Department of Agricultural Chemistry, Faculty of Agriculture, Kobe University
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OJI Yoshikiyo
Department of Agricultural Chemistry, Faculty of Agriculture, Kobe University
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SHIGA Hitoichi
Department of Agricultural Chemistry, Faculty of Agriculture, Kobe University
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Oji Yoshikiyo
Department Of Agricultural Chemistry Faculty Of Agriculture Kobe University
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Harada H
National Institute Of Livestock And Grassland Science:(present Office)agriculture Forestry And Fishe
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Shiga H
Department Of Agricultural Chemistry Faculty Of Agriculture Kobe University
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Wakiuchi Nariaki
Department Of Agricultural Chemistry Faculty Of Agriculture Kobe University
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