Characteristics of Adenosinetriphosphatase and Inorganic Pyrophosphatase in Tonoplasts Isolated from Three CAM Species, Ananas comosus, Kalanchoe pinnata and K. daigremontiana

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The characteristics of adenosinetriphosphatase (ATPase) and inorganic pyrophosphatase (PPase) in the tonoplasts isolated from leaf mesophyll homogenates of Ananas comosus (pineapple), a hexose-utilizing species with high PPi-PFK activities, and Kalanchoe pinnata and K. daigremontiane, starch-utilizing species with high ATP-PFK activities, were investigated. The ATPase and nitrate-sensitive ATPase (?NO_3^--ATPase) activities were higher than the PPase activity of pineapple, but the reverse was the case in the two Kalanchoe species. The optimum pH for ?NO_3^--ATPase in pineappe, K. daigremontiana and K. pinnata was 7.0〜8.25, 7.5〜8.25 and 7.5〜8.25, respectively, and that for PPase was 6.5〜7.5 in all species. The K_m of ?NO_3^--ATPase for Na_2-ATP for pineapple, K. daigremontiana and K. pinnata was 0.47, 0.48 and 0.43 mM, respectively, and V_<max> was 52.6, 27.0 and 40.0 μmol Pi mg^<-1> protein h^<-1>, respectively. The optimum MgSO_4 and Na_4PP_1 concentrations for the PPase activity of the three CAM species were approximately 2 mM and 0.16 mM, respectively. The optimum temperature for the ?NO_3^--ATPase in pineapple, K. daigremontiana and K. pinnata was 35〜43, 35〜43 and 37℃, respectively, and that for PPase was 46〜49℃. In addition, at a high temperature, the decrement of tonoplast ?NO_3^--ATPase and PPase activities in pineapple was less than that in the two Kalanchoe species. Thus, pineapple obviously maintained high tonoplast ?NO_3^--ATPase and PPase activities at high temperatures.

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詳細情報 詳細情報について

  • CRID
    1570854176932797952
  • NII論文ID
    110001720652
  • NII書誌ID
    AA11162156
  • ISSN
    1343943X
  • 本文言語コード
    en
  • データソース種別
    • CiNii Articles

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