Purification and Some Properties of an Aminopeptidase from the Seeds of<i>Cannabis sativa</i>

  • ARIMA Kazunari
    Plant Gene Expression Center, Department of Plant and Microbial Biology, University of California
  • UCHIKOBA Tetsuya
    Department of Chemistry, Faculty of Science, Kagoshima University
  • SHIMADA Masayuki
    Department of Chemistry, Faculty of Science, Kagoshima University
  • YONEZAWA Hiroo
    Department of Chemistry, Faculty of Science, Kagoshima University
  • KANEDA Makoto
    Department of Chemistry, Faculty of Science, Kagoshima University

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  • Purification and Some Properties of an Aminopeptidase from the Seeds of Cannabis sativa.

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  An aminopeptidase (HSA) with a molecular mass of 78 kDa was purified from hemp (Cannabis sativa) seeds. The activity was inhibited by monoiodeacetic acid, p-chloromercuri-phenylsulfonic acid, and Zn2+ ion. The specificity of HSA was similar to that of a leucyl aminopeptidase [EC 3.4.11.1] from mammalian cytosol. However, other enzyme properties were different from these of leucyl aminopeptidase.<br>

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