Formation, isolation and characterization of a prolyl tripeptidyl peptidase of Porphyromonas gingivalis

Persistent ID (NDL): info:ndljp/pid/9491171

Material type: 博士論文

Author: Matsuo, Kazukoほか

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Publication date: 2015-02-05

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Name of awarding university/degree: 松本歯科大学,博士（歯学）

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Note (General)：: Formation, cellular locations, isolation and enzymatic propertiesof PTP of Porphyromonas gingivalis, an anaerobic periodontalpathogen were investigate...

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投稿雑誌：Matsuo Kazuko, Kiso Akiko, Shibata Yukinaga, Hasegawa Hiromasa, Fujimura Setsuo. Formation, isolation and characterization of a prolyl tripeptidyl peptidase of Porphyromonas gingivalis. 松本歯学(0385-1613)40巻1号 Page1-12(2014.06). © 2016 松本歯科大学学会

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Material Type: 博士論文
Title: Formation, isolation and characterization of a prolyl tripeptidyl peptidase of Porphyromonas gingivalis
Author/Editor: Matsuo, Kazuko
Kiso, Akiko
Shibata, Yukinaga
Hasegawa, Hiromasa
Fujimura, Setsuo
松尾, 和子
木曽, 有紀子
柴田, 幸永
長谷川, 博雅
藤村, 節夫
Publication Date: 2015-02-05
Publication Date (W3CDTF): 2015-02-05
Alternative Title: Porphyromonas gingivalisのプロリルトリペプチジルペプチダーゼの産生，単離および性状
Degree grantor/type: 松本歯科大学
Date Granted: 2015-02-05
Date Granted (W3CDTF): 2015-02-05
Dissertation Number: 甲第167号
Degree Type: 博士（歯学）
Conferring No. (Dissertation): 甲第167号
Text Language Code: eng
Subject Heading: enzyme
prolyl tripeptidase
Porphyromonas gingivalis
Note (General): Formation, cellular locations, isolation and enzymatic propertiesof PTP of Porphyromonas gingivalis, an anaerobic periodontalpathogen were investigated.Almost all activities of this enzyme were detected in the crudeextract of the cell, but the other bacterial fractions such as culturefluids, envelopes and vesicles were not found to contain PTP.PTP was purified from the crude extract prepared by sonicationand centrifugation through five steps including concentration, ionexchange chromatography, gel filtration, hydrophobic interactionchromatography and isoelectric focusing to homogeneity.The enzyme was a serine enzyme since it was inhibited stronglyby Pefabloc SC, diisopropyl fluorophosphate and3,4-dichloroisocoumarin. It hydrolyzed H-Ala-Ala-Pro-pNA andH-Ala-Phe-Pro-pNA. The molecular mass was determined as 45kDa and isoelectric point was 5.7.Optimum pH was moderately broad, and maximum activity wasobserved in the range of pH 7.0 to 9.0.The residual activity after heating at 50℃ for 5 min was 29%,but heating at 60℃ resulted in complete loss of the activity.
2014
identifier:甲第167号
Persistent ID (NDL): info:ndljp/pid/9491171
https://dl.ndl.go.jp/pid/9491171
Collection: 障害者向け資料
Collection (Materials For Handicapped People:1): テキストデータ
Collection (particular): 国立国会図書館デジタルコレクション > デジタル化資料 > 博士論文
https://dl.ndl.go.jp/collections/A00014
Acquisition Basis: 博士論文（自動収集）
Date Accepted (W3CDTF): 2015-09-01T13:12:47+09:00
Date Created (W3CDTF): 2015-07-06
Format (IMT): PDF
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Original Material (URI): https://mdu.repo.nii.ac.jp/?action=pages_view_main&active_action=repository_view_main_item_detail&item_id=2266&item_no=1&page_id=13&block_id=17
Related Material: 投稿雑誌：Matsuo Kazuko, Kiso Akiko, Shibata Yukinaga, Hasegawa Hiromasa, Fujimura Setsuo. Formation, isolation and characterization of a prolyl tripeptidyl peptidase of Porphyromonas gingivalis. 松本歯学(0385-1613)40巻1号 Page1-12(2014.06). © 2016 松本歯科大学学会
Periodical Title (URI): http://id.nii.ac.jp/1070/00002403/
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