Reconstitution and Characterization of H^+-Translocating ATPase from the Plasma Membrane of Phaseolus mungo L. Roots

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概要

• 論文の詳細を見る

• Plasma membrane H^+-translocating ATPase was partially purified from mung bean (Phaseolus mungo L.) roots and reconstituted into soybean phospholipid (asolectin) liposomes by the n-octylglucoside dilution method. The resulting proteoliposomes were mainly unilamellar vesicles ranging in size from 0.05 to 0.2 μm. The existence of ATP-drived H^+-pumping across the proteoliposomes was demonstrated by the quenching of quinacrine fluorescence in the presence of Mg^<2+>. The quenching could be abolished by an uncoupler, FCCP, and an inhibitor of H^+-translocating ATPase, vanadate. The reconstituted ATPase consisted of three major polypeptides of 105 KDa, 67 KDa and 57 KDa. Its pH optimum, divalent cation stimulation and vanadate sensitivity were similar to those of partially purified ATPase. However, the specificity toward ATP was much greater following reconstitution. Also reconstitution reduced the degree of inhibition by DCCD. Local anesthetics (e.g. dibucaine) had no effect on H^+-pumping activity but increased the ATPase activity when proteoliposomes were reconstituted in their presence.

• 日本植物生理学会の論文

著者

• Kasamo Kunihiro

  Department of Applied Physiology, National Institute of Agrobiological Resources

• Kasamo Kunihiro

  Department Of Cell Biology National Institute Of Agrobiological Resources Tsukuba Science City

関連論文

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• Isolation of Subunits of Coupling Factor 1 from Maize and Spinach Chloroplasts and Properties of Combinations of Subunits with ATPase Activity
• Response of Tonoplast and Plasma Membrane ATPases in Chilling-Sensitive and-Insensitive Rice Oryza sativa L.) Culture Cells to Low Temperature
• Inhibition of Tonoplast and Plasma Membrane H^+-ATPase Activity in Rice (Oryza sativa L.) Culture Cells by Local Anesthetics
• Reconstitution and Characterization of H^+-Translocating ATPase from the Plasma Membrane of Phaseolus mungo L. Roots
• Mg^-activated and -inhibited ATPases from mung bean hypocotyls
• In vitro binding of IAA to plasma membrane-rich fractions containing Mg^-activated ATPase from mung bean hypocotyls
• Comparison of Plasma Membrane and Tonoplast H^+-Translocating ATPases in Phaseolus mungo L. Roots

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