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Kinetic analyses of two-steps oxidation from L-tyrosine to L-dopaquinone with tyrosinase by capillary electrophoresis/dynamic frontal analysis
https://tokushima-u.repo.nii.ac.jp/records/2010171
https://tokushima-u.repo.nii.ac.jp/records/201017134a83c11-adf7-44b2-b239-62e45e818c1a
| 名前 / ファイル | ライセンス | アクション |
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ab_655_114856.pdf (996 KB)
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| Item type | 文献 / Documents(1) | |||||||||||||||||||||||
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| 公開日 | 2022-08-19 | |||||||||||||||||||||||
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| アクセス権 | open access | |||||||||||||||||||||||
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| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||||||||||||||||||||
| 資源タイプ | journal article | |||||||||||||||||||||||
| 出版社版DOI | ||||||||||||||||||||||||
| 関連識別子 | https://doi.org/10.1016/j.ab.2022.114856 | |||||||||||||||||||||||
| 関連名称 | 10.1016/j.ab.2022.114856 | |||||||||||||||||||||||
| 出版タイプ | ||||||||||||||||||||||||
| 出版タイプ | AM | |||||||||||||||||||||||
| 出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||||||||||||||||||||
| タイトル | ||||||||||||||||||||||||
| タイトル | Kinetic analyses of two-steps oxidation from L-tyrosine to L-dopaquinone with tyrosinase by capillary electrophoresis/dynamic frontal analysis | |||||||||||||||||||||||
| 著者 |
ミネ, マサノリ
× ミネ, マサノリ
× 水口, 仁志
WEKO
807
× 髙栁, 俊夫
WEKO
549
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| 内容記述 | Tyrosinase catalyzes the oxidation of L-tyrosine in two stages to produce L-dopa and L-dopaquinone stepwise, and L-dopaquinone is subsequently converted to dopachrome. Most of the conventional analyses subjected only one-step reaction from L-tyrosine to L-dopa or from L-dopa to L-dopaquinone. In this study, kinetic analyses of two-steps oxidation of L-tyrosine with tyrosinase were made by capillary electrophoresis/dynamic frontal analysis (CE/DFA). When L-dopa was introduced into a capillary as a sample plug in a CE/DFA format, the enzymatic oxidation continuously occurred during the electrophoresis, and the product L-dopaquinone was subsequently converted to dopachrome which was detected as a plateau signal. A Michaelis-Menten constant of the second-step kinetic reaction, Km,Do, was determined as 0.45±0.03 mmol L−1. In the analysis of the first-step kinetic reaction from L-tyrosine to L-dopa, L-dopa was not resolved by CE/DFA because both L-tyrosine and L-dopa are electrically neutral. The L-dopa formed and co-migrated at the L-tyrosine zone was calibrated beforehand with the final product of dopachrome detected as a plateau signal. Constantly formed L-dopa was successfully detected as a plateau signal of dopachrome, and a Michaelis-Menten constant of Km,Ty was also determined as 0.061±0.009 mmol L−1 by the CE/DFA. CE/DFA is applicable to two-steps enzymatic reactions. | |||||||||||||||||||||||
| キーワード | ||||||||||||||||||||||||
| 主題 | Capillary electrophoresis | |||||||||||||||||||||||
| キーワード | ||||||||||||||||||||||||
| 主題 | Dynamic frontal analysis | |||||||||||||||||||||||
| キーワード | ||||||||||||||||||||||||
| 主題 | Tyrosinase | |||||||||||||||||||||||
| キーワード | ||||||||||||||||||||||||
| 主題 | Two-steps oxidation | |||||||||||||||||||||||
| キーワード | ||||||||||||||||||||||||
| 主題 | Kinetic analysis | |||||||||||||||||||||||
| 書誌情報 |
en : Analytical Biochemistry 巻 655, p. 114856, 発行日 2022-08-11 |
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| 収録物識別子タイプ | ISSN | |||||||||||||||||||||||
| 収録物識別子 | 00032697 | |||||||||||||||||||||||
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| 収録物識別子タイプ | NCID | |||||||||||||||||||||||
| 収録物識別子 | AA00524867 | |||||||||||||||||||||||
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| 収録物識別子タイプ | NCID | |||||||||||||||||||||||
| 収録物識別子 | AA11537838 | |||||||||||||||||||||||
| 出版者 | ||||||||||||||||||||||||
| 出版者 | Elsevier | |||||||||||||||||||||||
| 権利情報 | ||||||||||||||||||||||||
| 権利情報 | © 2022. This manuscript version is made available under the CC-BY-NC-ND 4.0 license https://creativecommons.org/licenses/by-nc-nd/4.0/ | |||||||||||||||||||||||
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| 識別子 | 389408 | |||||||||||||||||||||||
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| 言語 | eng | |||||||||||||||||||||||
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ミネ, マサノリ, 水口, 仁志, 髙栁, 俊夫, 2022, Kinetic analyses of two-steps oxidation from L-tyrosine to L-dopaquinone with tyrosinase by capillary electrophoresis/dynamic frontal analysis: Elsevier, 114856– p.
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