HPLC-based bioactivity profiling of plant extracts: a kinetic assay for the identification of monoamine oxidase-A inhibitors using human recombinant monoamine oxidase-A

被引：19
作者：
Dittmann, K
Riese, U
Hamburger, M
机构：
[1] Univ Basel, Inst Pharmaceut Biol, Dept Pharm, CH-4056 Basel, Switzerland
[2] Univ Jena, Inst Pharm, D-07743 Jena, Germany
来源：
PHYTOCHEMISTRY | 2004年 / 65卷 / 21期
关键词：
monoamine oxidase A; human recombinant; GST-fusion protein; HPLC; activity profiling; plant extract; lead discovery;
D O I：
10.1016/j.phytochem.2004.07.024
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
An assay for the HPLC-based search for monoamine oxidase-A (MAO-A) inhibitors in plant extracts was established. It combines human recombinant MAO-A, expressed as GST-fusion protein in yeast, with a kinetic measurement of the conversion of kynuramine to 4-hydroxyquinoline. Substrate selectivity and kinetic parameters of the GST-fusion protein were comparable to the wild-type enzyme. The applicability of the assay to HPLC-based activity profiling was tested with plant extracts spiked with small amounts of known MAO inhibitors. (C) 2004 Elsevier Ltd. All rights reserved.
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收藏
页码：2885 / 2891
页数：7
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