Colorimetric determination of the activity of acetylcholinesterase and its inhibitors by exploiting the iodide-catalyzed oxidation of 3,3',5,5'-tetramethylbenzidine by hydrogen peroxide
文献类型：期刊论文
| 作者 | Ni, Pengjuan1,2; Sun, Yujing1; Dai, Haichao1,2; Jiang, Shu1,2; Lu, Wangdong1,2; Wang, Yilin1,2; Li, Zhen1,2; Li, Zhuang1 |
| 刊名 | Microchimica acta
 |
| 出版日期 | 2016-09-01 |
| 卷号 | 183期号:9页码:2589-2595 |
| 关键词 | Enzyme activity assay Enzyme inhibition Neostigmine Ache Tmb Thiocholine Chromogenic reaction |
| ISSN号 | 0026-3672 |
| DOI | 10.1007/s00604-016-1874-8 |
| 通讯作者 | Li, zhuang(zli@ciac.ac.cn) |
| 英文摘要 | We describe a sensitive and selective colorimetric method for the determination of the activity of the enzyme acetylcholinesterase (ache) and its inhibitors. detection is based on the fact that acetylthiocholine iodide (atci) catalyzes the oxidation of the substrate 3,3',5,5'-tetramethylbenzidine (tmb) by h2o2 to form a blue product (ox-tmb) with an absorption peak at 652 nm, but that oxidation is suppressed if acti previously is hydrolyzed by ache to form thiocholine which decolorizes ox-tmb. in the presence of inhibitor, the activity of ache is inhibited, thereby inducing the recovery of the blue coloration. based on these findings, a highly sensitive method is developed for the determination of ache and its inhibitors. the assay only requires mixing of buffer, solutions of atci, tmb, h2o2 and a sample containing ache and photometric measurement. it works in the 0.05 to 5 muaeuro cent ml(-1) enzyme activity range and has a detection limit as low as 30 mu uaeuro cent ml(-1). the inhibitor neostigmine causes 50 % enzyme inhibition in 14.5 nm concentration. this analytical system has a wide scope in that it may be applied to the determination of the activity of various other hydrolases with proper substrates. |
| WOS关键词 | FLUORESCENCE TURN-ON ; IN-SITU FORMATION ; QUANTUM DOTS ; FLUOROMETRIC ASSAYS ; SENSITIVE DETECTION ; GOLD NANOPARTICLES ; SENSING PLATFORM ; AU NANOPARTICLES ; VISUAL DETECTION ; BIOSENSOR |
| WOS研究方向 | Chemistry |
| WOS类目 | Chemistry, Analytical |
| 语种 | 英语 |
| WOS记录号 | WOS:000381401300013 |
| 出版者 | SPRINGER WIEN |
| URI标识 | http://www.irgrid.ac.cn/handle/1471x/2375396 |
| 专题 | 中国科学院大学 |
| 通讯作者 | Li, Zhuang |
| 作者单位 | 1.Chinese Acad Sci, Changchun Inst Appl Chem, State Key Lab Electroanalyt Chem, Changchun 130022, Jilin, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China |
| 推荐引用方式 GB/T 7714 | Ni, Pengjuan,Sun, Yujing,Dai, Haichao,et al. Colorimetric determination of the activity of acetylcholinesterase and its inhibitors by exploiting the iodide-catalyzed oxidation of 3,3',5,5'-tetramethylbenzidine by hydrogen peroxide[J]. Microchimica acta,2016,183(9):2589-2595. |
| APA | Ni, Pengjuan.,Sun, Yujing.,Dai, Haichao.,Jiang, Shu.,Lu, Wangdong.,...&Li, Zhuang.(2016).Colorimetric determination of the activity of acetylcholinesterase and its inhibitors by exploiting the iodide-catalyzed oxidation of 3,3',5,5'-tetramethylbenzidine by hydrogen peroxide.Microchimica acta,183(9),2589-2595. |
| MLA | Ni, Pengjuan,et al."Colorimetric determination of the activity of acetylcholinesterase and its inhibitors by exploiting the iodide-catalyzed oxidation of 3,3',5,5'-tetramethylbenzidine by hydrogen peroxide".Microchimica acta 183.9(2016):2589-2595. |
入库方式： iSwitch采集
来源：中国科学院大学
浏览0
下载0
收藏0
其他版本
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。