首页    期刊浏览 2024年11月30日 星期六
登录注册

文章基本信息

  • 标题:Characterization of High- and Low-Molecular Weight Zinc-Dependent Acid Phosphatases in Bovine Liver
  • 本地全文:下载
  • 作者:Junji TSUDA ; Takanobu KIMURA ; Hiroko TANINO
  • 期刊名称:Biological and Pharmaceutical Bulletin
  • 印刷版ISSN:0918-6158
  • 电子版ISSN:1347-5215
  • 出版年度:1998
  • 卷号:21
  • 期号:11
  • 页码:1218-1221
  • DOI:10.1248/bpb.21.1218
  • 出版社:The Pharmaceutical Society of Japan
  • 摘要:We have purified two forms of Zn2+-dependent acid phosphatase (Zn2+-APase) from bovine liver, both of which require Zn2+ to hydrolyze the substrate p-nitrophenyl phosphate in an acidic environment. The apparent molecular weights of these two forms of Zn2+-APase were estimated to be about 100000 and 62000 by gel filtration, and about 44000 and 31000 by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, respectively. The low-molecular weight (LMW) Zn2+-APase catalyzed the hydrolysis of myo-inositol-1-phosphate in the presence of 3 mM Mg2+ at physiological pH, but the high-molecular weight (HMW) enzyme did not. The LMW-Zn2+-APase of bovine liver was recognized by polyclonal antibodies developed against the Zn2+-APase of bovine brain, but the HMW-Zn2+-APase was not.
  • 关键词:zinc-dependent acid phophatase;myo-inositol-1-phosphatase;liver;brain;bovine
国家哲学社会科学文献中心版权所有