中國醫藥大學機構典藏 China Medical University Repository, Taiwan:Item 310903500/28717
English  |  正體中文  |  简体中文  |  全文笔数/总笔数 : 29490/55136 (53%)
造访人次 : 1507290      在线人数 : 705
RC Version 7.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
搜寻范围 查询小技巧：
  • 您可在西文检索词汇前后加上"双引号"，以获取较精准的检索结果
  • 若欲以作者姓名搜寻，建议至进阶搜寻限定作者字段，可获得较完整数据
    •  进阶搜寻
    主页 ‧ 登入 ‧ 上传 ‧ 说明 ‧ 关于CMUR ‧ 管理 到手机版


    jsp.display-item.identifier=請使用永久網址來引用或連結此文件: http://ir.cmu.edu.tw/ir/handle/310903500/28717


    题名: Studies of needling depth in acupuncture treatment
    作者: Lin, JG
    贡献者: 中醫學院中醫所;Lin, JG, CHINA MED COLL,INST CHINESE MED SCI,91 RD SHYUE SHYH,TAICHUNG,TAIWAN
    日期: 1997
    上传时间: 2010-09-24 13:43:53 (UTC+8)
    出版者: CHINESE MEDICAL ASSOCIATION
    摘要: N-Acetyltransferase activities with p-aminobenzoic acid and 2-aminofluorene were determined in Helicobacter pylori from gastroduodenal disease patients. The N-acetyltransferase activity was determined using an acetyl CoA recycling assay and high pressure liquid chromatography. The N-acetyltransferase activities from a-number of Helicobacter pylori samples were found to be 0.91 +/- 0.12 nmole/min/mg protein for the acetylation of 2-aminofluorene and 0.75 +/- 0.22 nmole/min/mg protein for the acetylation of p-aminobenzoic acid. The apparent K-m and V-max values obtained were 1.10 +/- 0.08 mM and 2.34 +/- 0.14 nmol/min/mg protein for 2-aminofluorene, and 0.92 +/- 0.09 mM and 2.08 +/- 0.16 nmol/min/mg protein for p-aminobenzoic acid. The optimal pH value for the enzyme activity was 6.0 for both substrates tested. The optimal temperature for enzyme activity was 37 degrees C for both substrates. The N-acetyltransferase activity was inhibited by iodacetamide: at 0.25 mM iodacetamide, activity was reduced 50% and 1.0 mM iodacetamide inhibited activity more than 90%. Among a series of divalent cations and salts, Cu2+ and Zn2+ were demonstrated to be the most potent inhibitors. Among the protease inhibitors, only ethylenediaminetetraacetic acid significantly protected N-acetyltransferase. Iodoacetic acid, in contrast to the other agents, markedly inhibited N-acetyltransferase. This is the first demonstration of acetyl CoA:arylamine N-acetyltransferase activity in Helicobacter. pylori. (C) 1997 Elsevier Science Ireland Ltd.
    關聯: CHINESE MEDICAL JOURNAL 110(2):154-156
    显示于类别:[中國醫學研究所] 期刊論文

    文件中的档案:

    没有与此文件相关的档案.



    在CMUR中所有的数据项都受到原著作权保护.

    TAIR相关文章

     

    DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - 回馈