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Immobilization of CYP1A2 and CYP Reductase onto Self-assembled Phospholipid Layer and Evaluation of their Activity
https://gifu-pu.repo.nii.ac.jp/records/14734
https://gifu-pu.repo.nii.ac.jp/records/1473496a227c7-7714-4d2b-b07e-7a042ff4e661
Item type | 研究室原著論文(1) | |||||
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公開日 | 2023-03-09 | |||||
タイトル | ||||||
タイトル | Immobilization of CYP1A2 and CYP Reductase onto Self-assembled Phospholipid Layer and Evaluation of their Activity | |||||
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 | |||||
アクセス権 | ||||||
アクセス権 | metadata only access | |||||
アクセス権URI | http://purl.org/coar/access_right/c_14cb | |||||
抄録 | ||||||
値 | We had immobilized cytochrome P450 (CYP) 1A2 and CYP reductase (CPR) onto a selfassembled phospholipid layer containing stearic acid (LDPE-StA-PC-SA) to confirm the functional interaction between CYP 1A2 and CPR. The formation of resorufin from 7-ethoxy resorufin was observed by use of the film immobilizing CYP 1A2 and CPR onto LDPE-StA-PC-SA. It was clarified that the fluidity of LDPE-StA-PC-SA was very important. The actual activity of CYP 1A2 did not depend on the density of CYP 1A2 on LDPE-StA-PC-SA, although its specific activity was affected on its density. The activity of immobilized CYP 1A2 depended on a temperature. It was assumed that the optimal temperature was about 45 ºC. |
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書誌情報 |
J. Photopolym. Sci. Technol. 巻 4, 号 35, p. 309-312, 発行日 2022 |