Characteristics of Adenosinetriphosphatase and Inorganic Pyrophosphatase in Tonoplasts Isolated from Three CAM Species, Ananas comosus, Kalanchoe pinnata and K. daigremontiana
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- CHEN Li-Song
- Faculty of Agriculture, Saga University
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- NOSE Akihiro
- Faculty of Agriculture, Saga University
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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.
収録刊行物
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- Plant production science
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Plant production science 3 (1), 24-31, 2000-03-01
日本作物学会
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詳細情報 詳細情報について
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- CRID
- 1570854176932797952
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- NII論文ID
- 110001720652
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- NII書誌ID
- AA11162156
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- ISSN
- 1343943X
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- 本文言語コード
- en
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- データソース種別
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- CiNii Articles