Refolding and Activation of Human Prorenin Expressed in Escherichia coli : Application of Recombinant Human Renin for Inhibitor Screening

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Human prorenin was expressed in <I>Escherichia coli</I> as a fusion protein of thioredoxin. The chimeric protein, which accumulated insoluble inclusion bodies, was solubilized in 4 <small>M</small> guanidine–HCl and refolded by an arginine-detergent buffer system and by systematic dialysis. The refolded fusion prorenin was activated by trypsin. The antiserum against human kidney renin specifically inhibited the recombinant human renin activity. Using the recombinant human renin, we screened its inhibitory activity in fermented soybean paste (miso) and demonstrated that miso contained renin inhibitory activity derived from soybean. The IC<SUB>50</SUB> values for soybean and steamed soybean extracts were determined to be 1.9 and 1.6 mg/ml, respectively. This is the first demonstration of renin inhibitory activity in miso and soybean.

収録刊行物

  • Bioscience, biotechnology, and biochemistry  

    Bioscience, biotechnology, and biochemistry 70(12), 2913-2918, 2006-12-23 

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

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各種コード

  • NII論文ID(NAID)
    10018523669
  • 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
    8596341
  • 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  CJP引用  NDL  J-STAGE 
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