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学科主题: 药学
题名:
Studies on the adenosine deaminase-catalyzed conversion of adenosine and nucleoside prodrugs by different capillary electrophoresis modes
作者: Pei, Lu; Xie, Lujia; Lin, Qian; Ling, Xiaomei; Guan, Zhu; Yang, Zhenjun
关键词: Different capillary electrophoresis modes ; Adenosine deaminase ; Adenosine ; Nucleoside prodrugs ; Steady-state parameters
刊名: ANALYTICAL BIOCHEMISTRY
发表日期: 2011-07-01
DOI: 10.1016/j.ab.2011.03.014
卷: 414, 期:1, 页:131-137
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology
类目[WOS]: Biochemical Research Methods ; Biochemistry & Molecular Biology ; Chemistry, Analytical
研究领域[WOS]: Biochemistry & Molecular Biology ; Chemistry
关键词[WOS]: ZONE-ELECTROPHORESIS ; MEDIATED MICROANALYSIS ; ENZYME ; GUANOSINE ; PURINE ; DRUGS ; MICROREACTOR ; INHIBITION ; ACTIVATION ; MECHANISM
英文摘要:

Four kinds of fast and efficient capillary electrophoresis modes, i.e., immobilized enzymatic reactor (IER), electrophoretically mediated microanalysis (EMMA), capillary zone electrophoresis (CZE), and micellar electrokinetic chromatography (MEKC), were first developed to study the adenosine deaminase (ADA)-catalyzed conversion of adenosine and nucleoside prodrugs, which is critical for releasing prodrugs into the intracellular compartment for phosphorylation. The enzyme-activated prodrug approach is a strategy that has been successfully employed to improve physicochemical and pharmacokinetic properties of potential therapeutic agents, especially in the search for antiviral nucleoside analogues. Adenosine, amino-ddG, and amino-D4G could be converted by ADA to different extents under our experimental conditions. Steady-state parameters K(m), V(max), and k(cat) were also determined. The substrate efficiencies (k(cat)/K(m)) of adenosine, amino-ddG, and amino-D4G were 0.19 +/- 0.01, 0.047 +/- 0.005, and 0.017 +/- 0.010 mu M(-1)s(-1), respectively. The enzymatic reaction could be performed at a nanoliter scale and all manipulation steps were combined into a fully automated assay in on-line modes, which opened the possibilities of high-throughput screening of large libraries of synthetic nucleoside analogues for biological activity and a relative mechanism study of nucleoside and its analogues. (C) 2011 Elsevier Inc. All rights reserved.

语种: 英语
所属项目编号: 2006AA02Z144 ; 7102107 ; K20090207 ; 2009ZX09301-010 ; 81072612
项目资助者: National High-Tech Research and Development Program of China (863 Program) ; Natural Science Foundation of Beijing ; Open Foundation of State Key Laboratory of Natural and Biomimetic Drugs ; National New Drug Research and Development Project of China ; National Natural Science Foundation
WOS记录号: WOS:000290704300018
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内容类型: 期刊论文
URI标识: http://ir.bjmu.edu.cn/handle/400002259/63390
Appears in Collections:北京大学药学院_期刊论文

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作者单位: Peking Univ, Sch Pharmaceut Sci, State Key Lab Nat & Biomimet Drugs, Beijing 100191, Peoples R China

Recommended Citation:
Pei, Lu,Xie, Lujia,Lin, Qian,et al. Studies on the adenosine deaminase-catalyzed conversion of adenosine and nucleoside prodrugs by different capillary electrophoresis modes[J]. ANALYTICAL BIOCHEMISTRY,2011,414(1):131-137.
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