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In the last decade, the cathepsins which show tissue-restricted expression pattern have been disconered. In placenta, eight novel genes related to cathepsin L have been recently identified. To characterize the cathepsins highly expressed in placenta, we prepare two recombinant cathepsins, cathepsins-P/J(Cat- P/J) and -6(Cat-6) by E. coli expression system with pTE-3 vector. Cat-P/J hydrolyzed both A-Phe-Arg-MCA, a typical substrate for cathepsins, and Boc-Val-Pro-Arg-MCA, a substrate for a-thronbin, while Cat-6 hydrolyzed only Boc-Val-Pro-Arg-MCA. Though these activities are very weak, this is the frist report describing the difference of substrate specificity between Cat-P/J and -6. Next we tried preparing the recombinant Cat-P/J by a baculovirus expression system becouse it had several advantage to produce functional soluble proteins. The soluble recombinant Cat-P/J wa secreted into the culture medium, and its maximum amount was observed at 4days post-infection. 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マウス胎盤に高発現しているリソソーム・システインプロテアーゼ、カテプシン-P/Jおよび-6の組換えタンパク質の製作
https://doi.org/10.15069/00000607
https://doi.org/10.15069/00000607dd386b98-daa5-4cb9-8990-d765053eed20
名前 / ファイル | ライセンス | アクション |
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KJ00004191087 (1.4 MB)
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Item type | 紀要論文(ELS) / Departmental Bulletin Paper(1) | |||||||||
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公開日 | 2005-03-25 | |||||||||
タイトル | ||||||||||
タイトル | マウス胎盤に高発現しているリソソーム・システインプロテアーゼ、カテプシン-P/Jおよび-6の組換えタンパク質の製作 | |||||||||
タイトル | ||||||||||
言語 | en | |||||||||
タイトル | Preparation of recombinant lysosomal cysteine proteases highly expressed in mouse placenta, cathepsin-P/J and -6. | |||||||||
言語 | ||||||||||
言語 | eng | |||||||||
キーワード | ||||||||||
主題Scheme | Other | |||||||||
主題 | バキュロウイルス発現系 | |||||||||
キーワード | ||||||||||
主題Scheme | Other | |||||||||
主題 | リフォールディング | |||||||||
キーワード | ||||||||||
主題Scheme | Other | |||||||||
主題 | ペプチド基質 | |||||||||
キーワード | ||||||||||
主題Scheme | Other | |||||||||
主題 | HPLC | |||||||||
キーワード | ||||||||||
主題Scheme | Other | |||||||||
主題 | ヒスチジンタグ | |||||||||
キーワード | ||||||||||
言語 | en | |||||||||
主題Scheme | Other | |||||||||
主題 | baculovirus expression system | |||||||||
キーワード | ||||||||||
言語 | en | |||||||||
主題Scheme | Other | |||||||||
主題 | refolding | |||||||||
キーワード | ||||||||||
言語 | en | |||||||||
主題Scheme | Other | |||||||||
主題 | peptide substrates | |||||||||
キーワード | ||||||||||
言語 | en | |||||||||
主題Scheme | Other | |||||||||
主題 | HPLC | |||||||||
キーワード | ||||||||||
言語 | en | |||||||||
主題Scheme | Other | |||||||||
主題 | His-tag | |||||||||
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 | |||||||||
ID登録 | ||||||||||
ID登録 | 10.15069/00000607 | |||||||||
ID登録タイプ | JaLC | |||||||||
ページ属性 | ||||||||||
内容記述タイプ | Other | |||||||||
内容記述 | P(論文) | |||||||||
記事種別(日) | ||||||||||
薬学部 | ||||||||||
記事種別(英) | ||||||||||
en | ||||||||||
School of Pharmaceutical Sciences | ||||||||||
著者名(日) |
定金, 豊
× 定金, 豊× 伊藤, 武朗× 友廣, 岳則× 木葉, 敬子× 川原, 正博
WEKO
654
× 今西, 重雄× 畑中, 保丸× 中込, 和哉 |
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著者名よみ |
サダカネ, ユタカ
× サダカネ, ユタカ× イトウ, タケアキ× トモヒロ, タケノリ× コノハ, ケイコ× カワハラ, マサヒロ× イマニシ, シゲオ× ハタナカ, ヤスマル× ナカゴミ, カズヤ |
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著者名(英) |
SADAKANE, Yutaka
× SADAKANE, Yutaka× ITO, Takeaki× TOMOHIRO, Takenori× KONOHA, Keiko× KAWAHARA, Masahiro× IMANISHI, Shigeo× HATANAKA, Yasumaru× NAKAGOMI, Kazuya |
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著者所属(日) | ||||||||||
九州保健福祉大学薬学部 | ||||||||||
著者所属(日) | ||||||||||
富山医科薬科大学薬学部 | ||||||||||
著者所属(日) | ||||||||||
富山医科薬科大学薬学部 | ||||||||||
著者所属(日) | ||||||||||
九州保健福祉大学薬学部 | ||||||||||
著者所属(日) | ||||||||||
九州保健福祉大学薬学部 | ||||||||||
著者所属(日) | ||||||||||
農業生物資源研究所昆虫生産工学研究グループ | ||||||||||
著者所属(日) | ||||||||||
富山医科薬科大学薬学部 | ||||||||||
著者所属(日) | ||||||||||
帝京大学薬学部 | ||||||||||
著者所属(英) | ||||||||||
en | ||||||||||
School of Pharmaceutical Sciences, Kyushu University of Health and Welfare | ||||||||||
著者所属(英) | ||||||||||
en | ||||||||||
Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical Univesity | ||||||||||
著者所属(英) | ||||||||||
en | ||||||||||
Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical Univesity | ||||||||||
著者所属(英) | ||||||||||
en | ||||||||||
School of Pharmaceutical Sciences, Kyushu University of Health and Welfare | ||||||||||
著者所属(英) | ||||||||||
en | ||||||||||
School of Pharmaceutical Sciences, Kyushu University of Health and Welfare | ||||||||||
著者所属(英) | ||||||||||
en | ||||||||||
Insect Biotechnology and Sericology Department, The National Institute of Agrobiological Sciences | ||||||||||
著者所属(英) | ||||||||||
en | ||||||||||
Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical Univesity | ||||||||||
著者所属(英) | ||||||||||
en | ||||||||||
School of Pharmaceutical Sciences, Teikyo University | ||||||||||
抄録(日) | ||||||||||
内容記述タイプ | Other | |||||||||
内容記述 | 胎盤組織に局在するカテプシン(システインプロテアーゼ)は、ここ数年で8種類も同定されたが、いずれも遺伝子レベルの発現が確認されているだけである。本研究では、妊娠後11.5日から15.5日までのマウス胎盤でのみ発現するカテプシン-P/J (Cat-P/J)および-6 (Cat-6) に注目し、組換えタンパク質の製作による機能解明を目指した。両組換えタンパク質は大腸菌pET発現系で製作した。蛍光基質での解析により、Cat-Pはカテプシンの典型的基質であるZ-Phe-Arg-MCAとαスロンビンの基質であるBoc-Val-Pro-Arg-MCAの両者を、Cat-6は後者のみを切断することが明らかになった。これらの活性は非常に弱いものであったが、両者の基質特異性の差が初めて明らかになった。次に高活性の組換え体を得る目的で、昆虫細胞発現系での製作を試みた。組換えCat-P/Jの発現は、感染開始から4日目の培地中で最大となることを確認したが、精製するには至らなかった。 | |||||||||
抄録(英) | ||||||||||
内容記述タイプ | Other | |||||||||
内容記述 | More than twenty cathepsins, a major component of trhe lysosomal proteolytic system, are identified. In the last decade, the cathepsins which show tissue-restricted expression pattern have been disconered. In placenta, eight novel genes related to cathepsin L have been recently identified. To characterize the cathepsins highly expressed in placenta, we prepare two recombinant cathepsins, cathepsins-P/J(Cat- P/J) and -6(Cat-6) by E. coli expression system with pTE-3 vector. Cat-P/J hydrolyzed both A-Phe-Arg-MCA, a typical substrate for cathepsins, and Boc-Val-Pro-Arg-MCA, a substrate for a-thronbin, while Cat-6 hydrolyzed only Boc-Val-Pro-Arg-MCA. Though these activities are very weak, this is the frist report describing the difference of substrate specificity between Cat-P/J and -6. Next we tried preparing the recombinant Cat-P/J by a baculovirus expression system becouse it had several advantage to produce functional soluble proteins. The soluble recombinant Cat-P/J wa secreted into the culture medium, and its maximum amount was observed at 4days post-infection. However, the purification of Cat-P/J was not achieved because of small amount of the recombinant proteins. | |||||||||
雑誌書誌ID | ||||||||||
収録物識別子タイプ | NCID | |||||||||
収録物識別子 | AA11490417 | |||||||||
書誌情報 |
九州保健福祉大学研究紀要 en : Journal of Kyushu University of Health and Welfare 巻 6, p. 287-297, 発行日 2005-03-25 |