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アイテム
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AMPLIFICATION AND SUBSTANTIAL PURIFICATION OF CARDIOLIPIN SYNTHASE OF ESCHERICHIA-COLI
https://sucra.repo.nii.ac.jp/records/13840
https://sucra.repo.nii.ac.jp/records/13840a5741da0-672e-47d2-8d78-ecce2123bd07
名前 / ファイル | ライセンス | アクション |
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A1002763.pdf (2.3 MB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2008-08-19 | |||||
タイトル | ||||||
タイトル | AMPLIFICATION AND SUBSTANTIAL PURIFICATION OF CARDIOLIPIN SYNTHASE OF ESCHERICHIA-COLI | |||||
言語 | ||||||
言語 | eng | |||||
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 |
Hiraoka, Shuichi
× Hiraoka, Shuichi× Nukui, Kazuki× Uetake, Nobuyuki× 太田, 明徳× Shibuya, Isao |
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著者 ローマ字 | ||||||
Hiraoka, Shuichi | ||||||
著者 ローマ字 | ||||||
Nukui, Kazuki | ||||||
著者 ローマ字 | ||||||
Uetake, Nobuyuki | ||||||
著者 ローマ字 | ||||||
Ohta, Akinori | ||||||
著者 ローマ字 | ||||||
Shibuya, Isao | ||||||
著者 所属 | ||||||
著者 所属 | ||||||
著者 所属 | ||||||
著者 所属 | ||||||
埼玉大学理学部(現 : 東京大学大学院農学生命科学研究科応用生命工学専攻細胞遺伝研究室) | ||||||
著者 所属(別言語) | ||||||
著者 所属(別言語) | ||||||
著者 所属(別言語) | ||||||
著者 所属(別言語) | ||||||
Department of Biochemistry, Saitama University(Present : Department of Biotechnology, The University of Tokyo) | ||||||
書誌情報 |
JOURNAL OF BIOCHEMISTRY 巻 110, 号 3, p. 443-449, 発行日 1991 |
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年月次 | ||||||
1991-9 | ||||||
出版者名 | ||||||
出版者 | Japanese Biochemical Society | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 0021924X | |||||
抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | A simple, specific, and sensitive assay procedure for cardiolipin synthase of Escherichia coli has been developed. This measures the radioactivity of glycerol formed from phosphatidyl[2-3H]glycerol and is mainly based on the findings that 400 mM phosphate and 0.015% Triton X-100 markedly activate the enzyme. Cardiolipin synthase was amplified 760-fold upon induction with isopropyl β-D-thiogalactoside in cells harboring a pBR322 derivative in which the cls gene encoding this enzyme was preceded by the tac promoter. Under these conditions, cardiolipin content increased, membrane potential decreased, spheroplasts became fragile, cells lost viability, and inducer-resistant mutants appeared at a high frequency. The amplification enabled the isolation of an enzyme preparation with a specific activity approximately 10,000-times higher than that of wild-type whole cell lysate. This purification was simply achieved by extraction of the crude membrane fraction with Triton X-100 and a single phosphocellulose column chromatography. This preparation, together with the crude envelope fraction, was used to characterize the basic properties of E. coli cardiolipin synthase, some of which were utilized in setting up the assay conditions. | |||||
版 | ||||||
[出版社版] | ||||||
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 | |||||
資源タイプ | ||||||
内容記述タイプ | Other | |||||
内容記述 | text | |||||
フォーマット | ||||||
内容記述タイプ | Other | |||||
内容記述 | application/pdf | |||||
作成日 | ||||||
日付 | 2008-08-20 | |||||
日付タイプ | Created | |||||
アイテムID | ||||||
A1002763 |