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Production and enzymatic properties of a prolyl tripeptidyl peptidase of Streptococcus anginosus
https://mdu.repo.nii.ac.jp/records/1537
https://mdu.repo.nii.ac.jp/records/15373b7d37e8-22d3-4121-9453-29450232fecf
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
matsumoto_shigaku_38-1-01.pdf (848.4 kB)
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| Item type | Journal Article(1) | |||||||
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| 公開日 | 2012-08-06 | |||||||
| タイトル | ||||||||
| タイトル | Production and enzymatic properties of a prolyl tripeptidyl peptidase of Streptococcus anginosus | |||||||
| 言語 | en | |||||||
| 言語 | ||||||||
| 言語 | eng | |||||||
| キーワード | ||||||||
| 言語 | en | |||||||
| 主題Scheme | Other | |||||||
| 主題 | enzyme | |||||||
| キーワード | ||||||||
| 言語 | en | |||||||
| 主題Scheme | Other | |||||||
| 主題 | prolyl tripeptidase | |||||||
| キーワード | ||||||||
| 言語 | en | |||||||
| 主題Scheme | Other | |||||||
| 主題 | Streptococcus | |||||||
| キーワード | ||||||||
| 言語 | en | |||||||
| 主題Scheme | Other | |||||||
| 主題 | anginosus | |||||||
| 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 | journal article | |||||||
| その他（別言語等）のタイトル | ||||||||
| その他のタイトル | Streptococcus anginosus のプロリルトリペプチジルペプチダーゼの産生と酵素性状 | |||||||
| 著者 |
AKIKO, KISO
× AKIKO, KISO
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| 抄録 | ||||||||
| 内容記述タイプ | Abstract | |||||||
| 内容記述 | Streptococcus anginosus is considered to be implicated in the etiology of oral infectious diseases as well as abscess formation in various body sites. We investigated the production and the enzymatic properties of PTP of S. anginosus NCTC 10713. This enzyme was found only in cell extract and active on tripeptide substrates containing proline residue at P1 position, particularly H−Ala−Ala−Pro−p−nitroanilide. The enzyme was produced by all 8 species of tested streptococci, indicating occurrence of this enzyme is rather ubiquitous within streptococci. This PTP was purified to homogeneity from the cell extract by the procedures including ammonium sulfate precipitation, chromatography, gel filtration and electrophoresis. The enzyme was inhibited by serine enzyme inhibitors and chelating reagents, indicating this PTP is a serine metalloenzyme with a molecular mass of 66 kDa. The enzyme was active against H−Ala−Ala−Pro−p−nitroanilide and H−Ala−Phe−Pro−p−nitroanilide in neutral pH solutions. The activity was completely lost by heating at 50°C for 10min. | |||||||
| 書誌情報 |
松本歯学 巻 38, 号 1, p. 1-11, 発行日 2012-04-30 |
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| 出版者 | ||||||||
| 出版者 | 松本歯科大学学会 | |||||||
| ISSN | ||||||||
| 収録物識別子タイプ | ISSN | |||||||
| 収録物識別子 | 0385-1613 | |||||||
| 書誌レコードID | ||||||||
| 収録物識別子タイプ | NCID | |||||||
| 収録物識別子 | AN00232590 | |||||||
| フォーマット | ||||||||
| 内容記述タイプ | Other | |||||||
| 内容記述 | application/pdf | |||||||
| 著者版フラグ | ||||||||
| 出版タイプ | VoR | |||||||
| 出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||||
