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Kinetic analysis of an enzymatic hydrolysis of p-nitrophenyl acetate with carboxylesterase by pressure-assisted capillary electrophoresis/dynamic frontal analysis

https://tokushima-u.repo.nii.ac.jp/records/2008415
https://tokushima-u.repo.nii.ac.jp/records/2008415
e082fef8-acbb-4f59-bee0-67c1028d8845
名前 / ファイル ライセンス アクション
am_12_48_5846.pdf am_12_48_5846.pdf (1.44 MB)
Item type 文献 / Documents(1)
公開日 2020-11-30
アクセス権
アクセス権 open access
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
出版社版DOI
関連識別子 https://doi.org/10.1039/D0AY01736A
関連名称 10.1039/D0AY01736A
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 analysis of an enzymatic hydrolysis of p-nitrophenyl acetate with carboxylesterase by pressure-assisted capillary electrophoresis/dynamic frontal analysis
著者 ミネ, マサノリ

× ミネ, マサノリ

ja ミネ, マサノリ

ja-Kana ミネ, マサノリ

en Mine, Masanori

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マツモト, ナオヤ

× マツモト, ナオヤ

ja マツモト, ナオヤ

ja-Kana マツモト, ナオヤ

en Matsumoto, Naoya

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水口, 仁志

× 水口, 仁志

WEKO 807
徳島大学 教育研究者総覧 303129/profile-ja.html
e-Rad 30333991

ja 水口, 仁志
ISNI

ja-Kana ミズグチ, ヒトシ

en Mizuguchi, Hitoshi

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髙栁, 俊夫

× 髙栁, 俊夫

WEKO 549
徳島大学 教育研究者総覧 241977/profile-ja.html
e-Rad 50263554

ja 髙栁, 俊夫
ISNI

ja-Kana タカヤナギ, トシオ

en Takayanagi, Toshio

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抄録
内容記述 An enzymatic hydrolysis of p‐nitrophenyl acetate with carboxyesterase was analyzed by capillary electrophoresis/dynamic frontal analysis (CE/DFA). A plateau signal was expected with the anionic product of p‐nitrophenol by the CE/DFA applying in‐capillary reaction and the continuous CE resolution of the product from the substrate zone. However, the plateau height was not sufficient, and/or the plateau signal fluctuated and drifted. Therefore, a pressure assist was utilized in the CE/DFA to detect the product zone fast and to average the fluctuated plateau signal by mixing in a laminar flow. The plateau signal became relatively flat and its height was developed by the pressure‐assisted capillary electrophoresis/dynamic frontal analysis (pCE/DFA). The plateau height was used for the Michaelis‐Menten analysis, and a Michaelis‐Menten constant was determined as KM = 0.83 mmol L−1. An enzyme inhibition was also examined with bis (p‐nitrophenyl) phosphate by adding it in the separation buffer. The height of the plateau signal decreased by the inhibition, and a 50% inhibitory concentration was determined as IC50 = 0.79 μmol L−1. The values of KM and IC50 obtained in this study agreed well with the reported values. Since the proposed pCE/DFA includes electrophoretic migration of the substrate zone in a capillary, it is also noticed that the deactivation of the enzyme by ethanol on the preparation of the substrate solution can be avoided, as well as the exclusion of the inhibition by the product.
書誌情報 en : Analytical Methods

巻 12, 号 48, p. 5846-5851, 発行日 2020-10-26
収録物ID
収録物識別子タイプ ISSN
収録物識別子 17599679
出版者
出版者 The Royal Society of Chemistry
EID
識別子 372525
言語
言語 eng
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