Purification and Characterization of Phospholipase B from Candida utilis

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著者

    • FUJITA Tomonari
    • Laboratory of Food Biochemistry, Department of Bioresources, Faculty of Agriculture, Ehime University
    • WATANABE Yasuo
    • Laboratory of Food Biochemistry, Department of Bioresources, Faculty of Agriculture, Ehime University
    • TAMAI Youichi
    • Laboratory of Food Biochemistry, Department of Bioresources, Faculty of Agriculture, Ehime University

抄録

Phospholipase B (PLB) from the <I>asporogenous</I> yeast <I>Candida utilis</I> was purified to homogeneity from a culture broth. The apparent molecular mass was 90–110 kDa by SDS–PAGE. The enzyme had two pH optima, one acidic (pH 3.0) and the other alkaline (pH 7.5). At acidic pH the enzyme hydrolyzed all phospholipids tested without metal ions. On the other hand, the PLB showed substrate specificity and required metal ions for alkaline activity.<BR>The cDNA sequence of the PLB was analyzed by a combination of several PCR procedures. The PLB encoded a protein consisting of 643 amino acids. The amino acid sequence contained a lipase consensus sequence (GxSxG) and catalytic arginine and aspartic acid motifs which were identified as the catalytic triad in the PLB from <I>Kluyveromyces lactis</I>, suggesting that the catalytic mechanism of the PLB is similar to that of cytosolic phospholipase A<SUB>2</SUB> (cPLA<SUB>2</SUB>), found in mammalian tissues.

収録刊行物

  • Bioscience, biotechnology, and biochemistry  

    Bioscience, biotechnology, and biochemistry 70(2), 377-386, 2006-02-23 

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

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各種コード

  • NII論文ID(NAID)
    10018534107
  • NII書誌ID(NCID)
    AA10824164
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    09168451
  • NDL 記事登録ID
    7833431
  • NDL 雑誌分類
    ZR7(科学技術--農林水産--農産) // ZR2(科学技術--生物学--生化学) // ZP1(科学技術--化学・化学工業)
  • NDL 請求記号
    Z53-G223
  • データ提供元
    CJP書誌  NDL  J-STAGE 
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