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喜树碱与胰蛋白酶的相互作用
引用本文:贾旭,邓珊珊,李政,苏波,刁家志,刘芯韵,郑芸,刘克武.喜树碱与胰蛋白酶的相互作用[J].化学研究与应用,2006,18(12):1408-1412.
作者姓名:贾旭  邓珊珊  李政  苏波  刁家志  刘芯韵  郑芸  刘克武
作者单位:1. 四川大学生命科学学院,生物资源与生态环境教育部重点实验室,四川,成都,610064
2. 江南大学生物工程学院,江苏,无锡,214036
摘    要:喜树碱(camptothecin,CPT)是从珙桐科乔木喜树中分离得到的一类重要抗癌药物,对动物肿瘤及白血病均有明显的抑制作用1]。CPT分子为五环结构,含有一个吡咯3,4-b]喹啉环,一个共轭吡啶环和一个α-羟基六元内脂环2]。CPT通过嵌合抑制DNA拓扑异构酶Ⅰ的活性,对卵巢癌、结肠直肠癌

关 键 词:喜树碱  胰蛋白酶  紫外光谱  荧光淬灭
文章编号:1004-1656(2006)1408-05
收稿时间:2005-02-15
修稿时间:2005-06-02

Interaction between Trypsin and Camptothecin
JIA Xu,DENG Shan-shan,LI Zheng,SU Bo,Diao Jia-zhi,LIU Xin-yun,ZHENG Yun,LIU Ke-wu.Interaction between Trypsin and Camptothecin[J].Chemical Research and Application,2006,18(12):1408-1412.
Authors:JIA Xu  DENG Shan-shan  LI Zheng  SU Bo  Diao Jia-zhi  LIU Xin-yun  ZHENG Yun  LIU Ke-wu
Institution:1. College of Life Science,Sichuan University,Key Laboratory of Bio-resources and Eco-environment,Ministry of Education,Chengdu 610064,China;2.School of Biotechnology,Southem Yangtze University,Wuxi 214036,China
Abstract:The interaction of trypsin with camptothecin(CPT) in vitro was studied by ultraviolet(UV) absorption spectral and fluorescence spectral methods.Making out value of Ki according to the ratio between 1/v and the amount of inhibitor contributes to the conclusion that CPT is a noncompetitive inhibitor.The interaction between CPT and trypsin is quite strong.CPT can affect the conformation of trypsin in some degree.Fluorescence quenching contributes to nonradiative energy-transfer,which results a static quenching of CPT to trypsin.Their binding constants and the binding sites of CPT were determined.
Keywords:camptothecin  trypsin  ultraviolet spectrum  fluorescen quenching
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