| アイテムタイプ |
共通(1) |
| 公開日 |
2017-12-20 |
| タイトル |
|
|
タイトル |
異常プリオン分解酵素の機能解明(物質生命化学科) |
|
言語 |
ja |
| タイトル |
|
|
タイトル |
Characterization of prion-degrading enzyme from Nocardiopsis sp. TOA-1(DEPARTMENT OF APPLIED CHEMISTRY AND BIOCHEMISTRY) |
|
言語 |
en |
| 作成者 |
長濱, 善昭
岡部, 正明
叶内, 宏明
岡, 達三
満生, 慎二
境, 正志
|
| アクセス権 |
|
|
アクセス権 |
open access |
|
アクセス権URI |
http://purl.org/coar/access_right/c_abf2 |
| 主題 |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
prion |
| 主題 |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
protease |
| 主題 |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
Nocardiopsis sp. |
| 内容記述 |
|
|
内容記述タイプ |
Abstract |
|
内容記述 |
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. |
|
言語 |
en |
| 出版者 |
|
|
出版者 |
九州産業大学工学部 |
|
言語 |
ja |
| 言語 |
|
|
言語 |
jpn |
| 資源タイプ |
|
|
資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
|
資源タイプ |
departmental bulletin paper |
| 出版タイプ |
|
|
出版タイプ |
VoR |
|
出版タイプResource |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
| 収録物識別子 |
|
|
収録物識別子タイプ |
NCID |
|
収録物識別子 |
AN00054266 |
| 書誌情報 |
ja : 九州産業大学工学部研究報告
号 44,
p. 121-122,
発行日 2007-12
|
KJ00005128108.pdf
