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Please use this identifier to cite or link to this item: http://hdl.handle.net/11178/4772

Title: 異常プリオン分解酵素の機能解明(物質生命化学科)
Other Titles: Characterization of prion-degrading enzyme from Nocardiopsis sp. TOA-1(DEPARTMENT OF APPLIED CHEMISTRY AND BIOCHEMISTRY)
Authors: 長濱, 善昭
岡部, 正明
叶内, 宏明
岡, 達三
満生, 慎二
境, 正志
Nagahama, Yoshiaki
Okabe, Masaaki
Kanouchi, Hiroaki
Oka, Tatsuzo
Mitsuiki, Shinji
Sakai, Masashi
ナガハマ, ヨシアキ
オカベ, マサアキ
カノウチ, ヒロアキ
オカ, タツゾウ
ミツイキ, シンジ
サカイ, マサシ
九州産業大学工学研究科 / 鹿児島大学農学部獣医学科 / 鹿児島大学農学部獣医学科 / 鹿児島大学農学部獣医学科 / 九州産業大学工学部 / 九州産業大学工学部
Keywords: prion
Nocardiopsis sp.
Issue Date: Dec-2007
Publisher: 九州産業大学工学部
Abstract: 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.
URI: http://hdl.handle.net/11178/4772
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