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Expression and characterization of cathepsin B from tsetse (Glossina morsitans morsitans)
https://obihiro.repo.nii.ac.jp/records/4465
https://obihiro.repo.nii.ac.jp/records/44653ee5af28-2a3b-48a9-a391-7cce619fc91a
名前 / ファイル | ライセンス | アクション |
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fulltext (1.1 MB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||||||||||
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公開日 | 2019-11-07 | |||||||||||||
タイトル | ||||||||||||||
言語 | en | |||||||||||||
タイトル | Expression and characterization of cathepsin B from tsetse (Glossina morsitans morsitans) | |||||||||||||
言語 | ||||||||||||||
言語 | eng | |||||||||||||
キーワード | ||||||||||||||
言語 | en | |||||||||||||
主題Scheme | Other | |||||||||||||
主題 | Cathepsin B | |||||||||||||
キーワード | ||||||||||||||
言語 | en | |||||||||||||
主題Scheme | Other | |||||||||||||
主題 | Enzyme assay | |||||||||||||
キーワード | ||||||||||||||
言語 | en | |||||||||||||
主題Scheme | Other | |||||||||||||
主題 | Tsetse fly | |||||||||||||
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 | |||||||||||||
著者 |
Ruttayaporn, Ngasaman
× Ruttayaporn, Ngasaman× Zhou, Mo× 菅沼, 啓輔
WEKO
357
× Yamasaki, Shino× 河津, 信一郎× 井上, 昇
WEKO
63
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抄録 | ||||||||||||||
内容記述タイプ | Abstract | |||||||||||||
内容記述 | Digestive enzymes in tsetse fly midgut are thought to modulate the development of African trypanosome which is a causative agent of trypanosomosis in human and animal. Cathepsin B is induced after the first blood meal ingestion and being higher in trypanosome infected flies. A DNA fragment encoding pro-cathepsin B (930 bp) (Accession No. AF329480_1) was cloned and expressed in E. coli and P. pastoris protein expression systems. An active recombinant cathepsin B (rGmcathB) produced by P. pastoris was migrating from 35 to 45 kDa under reducing condition. rGmcathB exhibited the highest proteolytic activity at pH 4.0 with wide range temperature 25-30°C, also degraded bovine hemoglobin and serum albumin. rGmcathB exhibited hydrolysis preference for Z-Arg-Arg-MCA (Kcat/KM 7.58 mM-1sec-1) and bovine hemoglobin (Kcat/KM 3.77 × 103 mM-1sec-1). The proteolytic activity of rGmcathB was inhibited by specific cysteine protease inhibitor (E-64) confirmed belonging to papain-like cysteine protease family. These results indicated that rGmcathB shows the activity of cathepsin B and have high affinity with blood protein referring a role in blood meal digestion. In this study, the recombinant protein expressed by E. coli expression system was not enzymatically active as shown in the recombinant protein expressed by P. pastoris expression system. This finding implies that P. pastoris expression system is more suitable for expressing enzymatically active recombinant proteases than E. coli expression system. | |||||||||||||
言語 | en | |||||||||||||
書誌情報 |
en : Japanese Journal of Veterinary Research 巻 61, 号 4, p. 137-147, 発行日 2013 |
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出版者 | ||||||||||||||
言語 | en | |||||||||||||
出版者 | Hokkaido University | |||||||||||||
ISSN | ||||||||||||||
収録物識別子タイプ | PISSN | |||||||||||||
収録物識別子 | 00471917 | |||||||||||||
書誌レコードID | ||||||||||||||
収録物識別子タイプ | NCID | |||||||||||||
収録物識別子 | AA0069128X | |||||||||||||
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 | |||||||||||||
日本十進分類法 | ||||||||||||||
主題Scheme | NDC | |||||||||||||
主題 | 649 |