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異常プリオン分解酵素の機能解明(物質生命化学科)
Bibliographic Information
- Other Title
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- Characterization of prion-degrading enzyme from Nocardiopsis sp. TOA-1(DEPARTMENT OF APPLIED CHEMISTRY AND BIOCHEMISTRY)
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Description
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
Journal
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- 九州産業大学工学部研究報告
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九州産業大学工学部研究報告 44 121-122, 2007-12
九州産業大学工学部
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Keywords
Details 詳細情報について
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- CRID
- 1050564286128855552
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- NII Article ID
- 110007025428
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- NII Book ID
- AN00054266
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- Web Site
- http://hdl.handle.net/11178/4772
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- Text Lang
- ja
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- Article Type
- departmental bulletin paper
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- Data Source
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- IRDB
- CiNii Articles