Compatible Solutes and Inorganic Ions in the Mangrove Plant Avicennia marina and Their Effects on the Activities of Enzymes

DOI Web Site Web Site XML 被引用文献1件 オープンアクセス
  • Hiroshi Ashihara
    Department of Biology, Faculty of Science, Ochanomizu University, Otsuka, Bunkyo-ku, Tokyo 112, Japan
  • Kyoko Adachi
    Marine Biotechnology Institute Shimizu Laboratories, Shizuoka 424, Japan
  • Miho Otawa
    Department of Biology, Faculty of Science, Ochanomizu University, Otsuka, Bunkyo-ku, Tokyo 112, Japan
  • Eri Yasumoto
    Department of Biology, Faculty of Science, Ochanomizu University, Otsuka, Bunkyo-ku, Tokyo 112, Japan
  • Yuko Fukushima
    Department of Biology, Faculty of Science, Ochanomizu University, Otsuka, Bunkyo-ku, Tokyo 112, Japan
  • Misako Kato
    Department of Biology, Faculty of Science, Ochanomizu University, Otsuka, Bunkyo-ku, Tokyo 112, Japan
  • Hiroshi Sano
    Marine Biotechnology Institute Shimizu Laboratories, Shizuoka 424, Japan
  • Hamako Sasamoto
    Cell Manipulation Laboratory, Forestry and Forest Products Research Institute, Tsukuba, Ibaraki 305, Japan
  • Shigeyuki Baba
    Department of Environmental Science and Technology, College of Agriculture, University of the Ryukyus, Nishihara, Okinawa 903-01, Japan

この論文をさがす

説明

<jats:p>Naturally grown two-month-old seedlings of Avicennia marina contain high concentrations of Na+ and Cl<jats:sup>-</jats:sup>.+ Our NMR studies revealed an accumulation of glycinebetaine, asparagine and stachyose in A. marina. The highest concentration of glycinebetaine was observed in young leaves, while the distribution of stachyose was restricted in stems and roots. A sparagine comprised more than 96% of total free amino acids in roots and 84% in leaves from two-year-old plants. Little or no accumulation of proline or polyols, which are proposed as compatible solutes in other plants, could be detected in A. marina. The activities of phosphofructokinase, pyrophosphate:fructose-6-phosphate 1-phosphotransferase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase (decarboxylating), phosphoenolpyruvate carboxylase and NAD:malate dehydrogenase from young leaves of A. marina were inhibited by NaCl, while the activity of fructose-1,6-bisphosphate aldolase was activated by 50-200 m M NaCl. There was little or no effect of high concentrations (up to 500 mᴍ ) of glycinebetaine on the activities of any of these enzymes. No significant protection by glycinebetaine was detected against NaCl inhibition of these enzymatic activities. Based on these results, possible mechanisms for the salt-resistance of A. marina cells are discussed.</jats:p>

収録刊行物

被引用文献 (1)*注記

もっと見る

問題の指摘

ページトップへ