異常プリオン分解酵素の機能解明(物質生命化学科)

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タイトル別名
  • Characterization of prion-degrading enzyme from Nocardiopsis sp. TOA-1(DEPARTMENT OF APPLIED CHEMISTRY AND BIOCHEMISTRY)

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説明

type:Article

Prion diseases are characterized by conversion of the normal cellular form of the prion protein (PrP^C) into an insoluble, protease-resistant abnormal form (PrP^<Sc>). The aberrant isoform of PrP^C, PrP^<Sc>, which is characterized by relative resistance to proteolysis and insolubility in nondenaturing detergents, is a hallmark of prion diseases. There have been some reports of PrP^<Sc>-degrading enzymes, but these enzymes need additional chemical and physical treatments for the degradation of PrP^<Sc>. A keratinolytic alkaline serine protease (NAPase) from Nocardiopsis sp. TOA-1 degraded a PrP^<Sc> without any chemical or physical treatment. Optimal temperature and pH were 50-70℃ and above pH 10.0. The PrP^<Sc> was completely degraded within several minutes under optimal conditions. These results suggest NAPase have remarkable ability as PrP^<Sc>-degrading enzyme. The mechanism of PrP^<Sc>-degrading was investigated using PrP^<Sc>-model protein PSP (perchloric-acid soluble protein) from pig liver.

identifier:http://repository.kyusan-u.ac.jp/dspace/handle/11178/4772

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詳細情報 詳細情報について

  • CRID
    1050564286128855552
  • NII論文ID
    110007025428
  • NII書誌ID
    AN00054266
  • Web Site
    http://hdl.handle.net/11178/4772
  • 本文言語コード
    ja
  • 資料種別
    departmental bulletin paper
  • データソース種別
    • IRDB
    • CiNii Articles

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