Characterization of Halophilic Alkaline Phosphatase from Halomonas sp. 593, a Moderately Halophilic Bacterium

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概要

• 論文の詳細を見る

• A halophilic alkaline phosphatase was highly purified (about 510-fold with about 21% yield) from a moderate halophile, Halomonas sp. 593. The N-terminal 35 amino acid sequence of this enzyme was found to be more acidic than those previously isolated from Vibrio spp., and this enzyme was partially resistant to SDS. Several enzymatic properties demonstrated that it showed higher halophilicity than those enzymes from Vibrio spp.

• 社団法人 日本農芸化学会の論文
• 2005-06-23

著者

• Tokunaga Masao

  日本原子力研究開発機構

• Ishibashi Matsujiro

  Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University

• Tokunaga Masao

  Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University

• YAMASHITA Sayaka

  Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University

• Yamashita Sayaka

  Applied And Molecular Microbiology Faculty Of Agriculture Kagoshima University

• Ishibashi Matsujiro

  Applied And Molecular Microbiology Faculty Of Agriculture Kagoshima University

• Tokunaga Masao

  Applied And Molecular Microbiology Faculty Of Agriculture Kagoshima University

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