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Application of Promoter Modified Electrodes to Bioelectrochemical Measurements on the Effects of Origin and Modification of Lysine Residues of Cytochrome c

http://hdl.handle.net/2298/10570
http://hdl.handle.net/2298/10570
595e6689-e15b-475a-8de8-4e1ac5b5df35
名前 / ファイル ライセンス アクション
1992Anal 1992Anal Sci-Cytc-Modified-CytOx.pdf (527.6 kB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2009-01-30
タイトル
タイトル Application of Promoter Modified Electrodes to Bioelectrochemical Measurements on the Effects of Origin and Modification of Lysine Residues of Cytochrome c
言語
言語 eng
キーワード
主題 Cytochrome c, cytochrome c oxidase, promoter modified electrode, electron transfer reaction, respiratory chain, molecular recognition
資源タイプ
資源タイプ journal article
著者 Tominaga, Masato

× Tominaga, Masato

WEKO 95756

Tominaga, Masato

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Hayashi, Kuniaki

× Hayashi, Kuniaki

WEKO 95757

Hayashi, Kuniaki

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Taniguchi, Isao

× Taniguchi, Isao

WEKO 95758

Taniguchi, Isao

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別言語の著者 冨永, 昌人

× 冨永, 昌人

WEKO 95762

冨永, 昌人

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谷口, 功

× 谷口, 功

WEKO 95763

谷口, 功

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内容記述
内容記述 Using promoter-modified electrodes, electron-transfer reactions of cytochrome c at an electrode and with cytochrome c oxidase were examined. The electrochemical behavior of cytochromes c from horse, bovine, chicken and tuna hearts at an electrode was similar to each other. Little difference was observed for the reactions between cytochromes c of various origins and cytochrome c oxidase from bovine in a phosphate buffer solution. Also, when a few (less than three) lysine residues of cytochrome c were treated with 4-chloro-3, 5-dinitrobenzoic acid (CDNP) or 2, 4-dinitrofluorobenzene (DNP), the electrode reaction of the modified (especially, mono-substituted) cytochrome c still showed no significant difference from that of the native one. On the other hand, the electron-transfer reaction between CDNP- or DNP-substituted cytochrome c at lysine 13 and/or 72 and cytochrome c oxidase was greatly affected, even when only one or two lysine residues of cytochrome c were modified. Since the cytochrome c molecules of different origins examined have about 3-19 differences in their amino acid sequences, but most lysine residues remain invariant, the present results indicate that lysine residues of cytochrome c play an important role in the interaction with cytochrome c oxidase; however, the promoter modified electrode surface does not recognize cytochrome c molecule very rigorously. The present study also shows that electrochemical techniques with the aid of functional electrodes are applicable as useful, convenient methods to analyze the biological reactions of proteins.
書誌情報 Analytical sciences : the international journal of the Japan Society for Analytical Chemistry

巻 8, 号 6, p. 829-836, 発行年 1992-12
ISSN
収録物識別子 13482246
書誌レコードID
収録物識別子タイプ NCID
収録物識別子 AA10500785
DOI
関連タイプ isIdenticalTo
関連識別子 10.2116/analsci.8.829
権利
権利情報 ©Japan Society for Analytical Chemistry
情報源(ISSN)
関連名称 09106340
フォーマット
内容記述タイプ Other
内容記述 application/pdf
形態
527555 bytes
著者版フラグ
出版タイプ VoR
日本十進分類法
主題Scheme NDC
主題 464
出版者
出版者 Japan Society for Analytical Chemistry
資源タイプ
内容記述タイプ Other
内容記述 論文(Article)
資源タイプ・ローカル
雑誌掲載論文
資源タイプ・NII
Journal Article
資源タイプ・DCMI
text
資源タイプ・ローカル表示コード
01
著作の一部
関連名称 http://dx.doi.org/10.2116/analsci.8.829
コメント
社団法人 日本分析化学会(http://www.jsac.or.jp/)
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