『徳島大学 教育・研究者情報データベース (EDB)』---[学外] /
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EID=180235EID:180235, Map:0, LastModified:2012年10月11日(木) 21:49:58, Operator:[大家 隆弘], Avail:TRUE, Censor:0, Owner:[辻 明彦], Read:継承, Write:継承, Delete:継承.
種別 (必須): 学術論文 (審査論文) [継承]
言語 (必須): 英語 [継承]
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審査 (推奨):
カテゴリ (推奨):
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学究種別 (推奨):
組織 (推奨): 1.徳島大学.大学院ソシオテクノサイエンス研究部.ライフシステム部門.生命情報工学 (2006年4月1日〜2016年3月31日) [継承]
著者 (必須): 1.辻 明彦
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2. (英) Kikuchi Yayoi (日) (読)
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3. (英) Ogawa Kentaro (日) (読)
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4. (英) Saika Hiroko (日) (読)
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5.湯浅 恵造 ([徳島大学.大学院社会産業理工学研究部.生物資源産業学域.応用生命系.生体分子機能学分野]/[徳島大学.生物資源産業学部.生物資源産業学科.応用生命講座])
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6.長浜 正巳
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題名 (必須): (英) Purification and characterization of cathepsin B-like cysteine protease from cotyledons of daikon radish, Raphanus sativus  (日)    [継承]
副題 (任意):
要約 (任意): (英) Plant cathepsin B-like cysteine protease (CBCP) plays a role in disease resistance and in protein remobilization during germination. The ability of animal cathepsin B to function as a dipeptidyl carboxypeptidase has been attributed to the presence of a dihistidine (His110-His111) motif in the occluding loop, which represents a unique structure of cathepsin B. However, a dihistidine motif is not present in the predicted sequence of the occluding loop of plant CBCP, as determined from cDNA sequence analysis, and the loop is shorter. In an effort to investigate the enzymatic properties of plant CBCP, which possesses the unusual occluding loop, we have purified CBCP from the cotyledons of daikon radish (Raphanus sativus) by chromatography through Sephacryl S-200, DEAE-cellulose, hydroxyapatite and organomercurial-Sepharose. The molecular mass of the enzyme was estimated to be 28 kDa by SDS/PAGE under reducing conditions. The best synthetic substrate for CBCP was t-butyloxycarbonyl Leu-Arg-Arg-4-methylcoumaryl 7-amide, as is the case with human cathepsin B. However, the endopeptidase activity of CBCP towards glucagon and adrenocorticotropic hormone showed broad cleavage specificity. Human cathepsin B preferentially cleaves model peptides via its dipeptidyl carboxypeptidase activity, whereas daikon CBCP displays both endopeptidase and exopeptidase activities. In addition, CBCP was found to display carboxymonopeptidase activity against the substrate o-aminobenzoyl-Phe-Arg-Phe(4-NO(2)). Daikon CBCP is less sensitive (1/7000) to CA-074 than human cathepsin B. Expression analysis of CBCP at the protein and RNA levels indicated that daikon CBCP activity in cotyledons is regulated by post-transcriptional events during germination.  (日)    [継承]
キーワード (推奨): 1. (英) Cathepsin B (日) (読) [継承]
2. (英) Chromatography (日) (読) [継承]
3. (英) Cotyledon (日) (読) [継承]
4. (英) Cysteine Endopeptidases (日) (読) [継承]
5. (英) Gene Expression Regulation, Plant (日) (読) [継承]
6. (英) Germination (日) (読) [継承]
7. (英) Humans (日) (読) [継承]
8. (英) Molecular Weight (日) (読) [継承]
9. (英) Plant Proteins (日) (読) [継承]
10. (英) RNA, Messenger (日) (読) [継承]
11. (英) Raphanus (日) (読) [継承]
12. (英) Substrate Specificity (日) (読) [継承]
発行所 (推奨):
誌名 (必須): The FEBS Journal ([Federation of European Biochemical Societies])
(pISSN: 1742-464X, eISSN: 1742-4658)

ISSN (任意): 1742-4658
ISSN: 1742-464X (pISSN: 1742-464X, eISSN: 1742-4658)
Title: The FEBS journal
Title(ISO): FEBS J
Supplier: Federation of European Biochemical Societies
Publisher: Wiley Publishing
 (NLM Catalog  (Wiley  (Scopus  (CrossRef (Scopus information is found. [need login])
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(必須): 275 [継承]
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(必須): 5429 5443 [継承]
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年月日 (必須): 西暦 2008年 11月 初日 (平成 20年 11月 初日) [継承]
URL (任意):
DOI (任意): 10.1111/j.1742-4658.2008.06674.x    (→Scopusで検索) [継承]
PMID (任意): 18959767    (→Scopusで検索) [継承]
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備考 (任意): 1.(英) Article.Affiliation: Department of Biological Science and Technology, University of Tokushima Graduate School, Japan. tsuji@bio.tokushima-u.ac.jp  (日)    [継承]
2.(英) Article.PublicationTypeList.PublicationType: Journal Article  (日)    [継承]

標準的な表示

和文冊子 ● Akihiko Tsuji, Yayoi Kikuchi, Kentaro Ogawa, Hiroko Saika, Keizo Yuasa and Masami Nagahama : Purification and characterization of cathepsin B-like cysteine protease from cotyledons of daikon radish, Raphanus sativus, The FEBS Journal, Vol.275, No.21, 5429-5443, 2008.
欧文冊子 ● Akihiko Tsuji, Yayoi Kikuchi, Kentaro Ogawa, Hiroko Saika, Keizo Yuasa and Masami Nagahama : Purification and characterization of cathepsin B-like cysteine protease from cotyledons of daikon radish, Raphanus sativus, The FEBS Journal, Vol.275, No.21, 5429-5443, 2008.

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