Purification and Characterization of a Novel Thermostable Extracellular Protein Tyrosine Phosphatase from Metarhizium anisopliae Strain CQMa102

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著者

    • YIN Youping
    • Genetic Engineering Research Center, Bioengineering College, Chongqing University
    • ZHAO Hua
    • Genetic Engineering Research Center, Bioengineering College, Chongqing University
    • CAO Yueqing
    • Genetic Engineering Research Center, Bioengineering College, Chongqing University
    • XIA Yuxian
    • Genetic Engineering Research Center, Bioengineering College, Chongqing University

抄録

An extracellular phosphatase was purified to homogeneity from the entomopathogenic fungus <I>Metarhizium anisopliae</I> with a 41.0% yield. The molecular mass and isoelectric point of the purified enzyme were about 82.5 kDa and 9.5 respectively. The optimum pH and temperature were about 5.5 and 75 °C when using <I>O</I>-phospho-<small>L</small>-tyrosine as substrate. The protein displayed high stability in a pH range 3.0–9.5 at 30 °C and was remarkably thermostable at 70 °C. The purified enzyme showed high activity on <I>O</I>-phospho-<small>L</small>-tyrosine and protein tyrosine phosphatase substrate monophosphate (a specific substrate of protein tyrosine phosphatase). Although one peptide of the phosphatase shared identity with one alkaline phosphatase of <I>Neurospora crassa</I>, its substrate specificity and inhibitor sensitivity indicate that the enzyme is a protein tyrosine phosphatase.

収録刊行物

  • Bioscience, biotechnology, and biochemistry  

    Bioscience, biotechnology, and biochemistry 70(8), 1961-1968, 2006-08-23 

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

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各種コード

  • NII論文ID(NAID)
    10018528335
  • 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
    8040513
  • 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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